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Conserved domains on  [gi|15230288|ref|NP_188541|]
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Protein kinase superfamily protein [Arabidopsis thaliana]

Protein Classification

serine/threonine-protein kinase( domain architecture ID 10142079)

serine/threonine-protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates; such as calcium/calmodulin-dependent protein kinases

CATH:  1.10.510.10
EC:  2.7.11.-
Gene Ontology:  GO:0004674|GO:0006468|GO:0005524
PubMed:  7768349
SCOP:  4003661

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
145-405 1.31e-127

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: 375.28  E-value: 1.31e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKKGElkdQEVAVKVIPKSKMTSaISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIV 224
Cdd:cd05117   3 ELGKVLGRGSFGVVRLAVHKKTG---EEYAVKIIDKKKLKS-EDEEMLRREIEILKRLD-HPNIVKLYEVFEDDKNLYLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLSDFVRPDE 304
Cdd:cd05117  78 MELCTGGELFDRIVKKG-SFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPIKIIDFGLAKIFEEGE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 305 RLNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDFV 383
Cdd:cd05117 157 KLKTVCGTPYYVAPEVLKGKgYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPEWKNVSEEAKDLI 236
                       250       260
                ....*....|....*....|..
gi 15230288 384 KRLLYKDPRKRMTASQALMHPW 405
Cdd:cd05117 237 KRLLVVDPKKRLTAAEALNHPW 258
 
Name Accession Description Interval E-value
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
145-405 1.31e-127

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: 375.28  E-value: 1.31e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKKGElkdQEVAVKVIPKSKMTSaISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIV 224
Cdd:cd05117   3 ELGKVLGRGSFGVVRLAVHKKTG---EEYAVKIIDKKKLKS-EDEEMLRREIEILKRLD-HPNIVKLYEVFEDDKNLYLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLSDFVRPDE 304
Cdd:cd05117  78 MELCTGGELFDRIVKKG-SFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPIKIIDFGLAKIFEEGE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 305 RLNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDFV 383
Cdd:cd05117 157 KLKTVCGTPYYVAPEVLKGKgYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPEWKNVSEEAKDLI 236
                       250       260
                ....*....|....*....|..
gi 15230288 384 KRLLYKDPRKRMTASQALMHPW 405
Cdd:cd05117 237 KRLLVVDPKKRLTAAEALNHPW 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
145-406 5.27e-101

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 306.76  E-value: 5.27e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288    145 ELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSaiSIEDVRREVKILRALsGHQNLVQFYDAFEDNANVYIV 224
Cdd:smart00220   2 EILEKLGEGSFGKVYLARDKK---TGKLVAIKVIKKKKIKK--DRERILREIKILKKL-KHPNIVRLYDVFEDEDKLYLV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288    225 MELCGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFVRPDE 304
Cdd:smart00220  76 MEYCEGGDLFDLLKKRG-RLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLD---EDGHVKLADFGLARQLDPGE 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288    305 RLNDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTE-SGIFRAVLKADPSFDEPPWPsLSFEAKDF 382
Cdd:smart00220 152 KLTTFVGTPEYMAPEVLlGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQlLELFKKIGKPKPPFPPPEWD-ISPEAKDL 230
                          250       260
                   ....*....|....*....|....
gi 15230288    383 VKRLLYKDPRKRMTASQALMHPWI 406
Cdd:smart00220 231 IRKLLVKDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
145-406 3.10e-63

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 207.48  E-value: 3.10e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288   145 ELGEEIGRGHFGytcsaKFKKGELKD--QEVAVKVIPKSKMTSaISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVY 222
Cdd:pfam00069   2 EVLRKLGSGSFG-----TVYKAKHRDtgKIVAIKKIKKEKIKK-KKDKNILREIKILKKLN-HPNIVRLYDAFEDKDNLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288   223 IVMELCGGGELLDRIlARGGKYSEDDAKAVLIQILnvvafchlQGVvhrdlkpenflytskeensmlkvidfglsdfvRP 302
Cdd:pfam00069  75 LVLEYVEGGSLFDLL-SEKGAFSEREAKFIMKQIL--------EGL--------------------------------ES 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288   303 DERLNDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEpPWPSLSFEAKD 381
Cdd:pfam00069 114 GSSLTTFVGTPWYMAPEVLgGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPE-LPSNLSEEAKD 192
                         250       260
                  ....*....|....*....|....*
gi 15230288   382 FVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:pfam00069 193 LLKKLLKKDPSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
137-394 5.07e-54

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 191.38  E-value: 5.07e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 137 SKELQSRIELGEEIGRGHFGYTCSAKFkkgELKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFE 216
Cdd:COG0515   2 SALLLGRYRILRLLGRGGMGVVYLARD---LRLGRPVALKVLRPELAADPEARERFRREARALARLN-HPNIVRVYDVGE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 217 DNANVYIVMELCGGGELLDRiLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGL 296
Cdd:COG0515  78 EDGRPYLVMEYVEGESLADL-LRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLT---PDGRVKLIDFGI 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 297 SDFVRPDE--RLNDIVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWP 373
Cdd:COG0515 154 ARALGGATltQTGTVVGTPGYMAPEQARgEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRP 233
                       250       260
                ....*....|....*....|.
gi 15230288 374 SLSFEAKDFVKRLLYKDPRKR 394
Cdd:COG0515 234 DLPPALDAIVLRALAKDPEER 254
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
142-395 1.25e-33

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 131.09  E-value: 1.25e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  142 SRIELGEEIGRGHFGYTCSAKFKKGElkdQEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANV 221
Cdd:PTZ00263  18 SDFEMGETLGTGSFGRVRIAKHKGTG---EYYAIKCLKKREILKMKQVQHVAQEKSILMELS-HPFIVNMMCSFQDENRV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  222 YIVMELCGGGELLDRiLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGLSDFVR 301
Cdd:PTZ00263  94 YFLLEFVVGGELFTH-LRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNK---GHVKVTDFGFAKKVP 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  302 pdERLNDIVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFdePPWpsLSFEAK 380
Cdd:PTZ00263 170 --DRTFTLCGTPEYLAPEVIQsKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKF--PNW--FDGRAR 243
                        250
                 ....*....|....*
gi 15230288  381 DFVKRLLYKDPRKRM 395
Cdd:PTZ00263 244 DLVKGLLQTDHTKRL 258
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
140-348 1.78e-25

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 110.66  E-value: 1.78e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  140 LQSRIELGEEIGRG-----HFGytcsakfkKGELKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDA 214
Cdd:NF033483   5 LGGRYEIGERIGRGgmaevYLA--------KDTRLDRDVAVKVLRPDLARDPEFVARFRREAQSAASLS-HPNIVSVYDV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  215 FEDNANVYIVMELCGGgELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDF 294
Cdd:NF033483  76 GEDGGIPYIVMEYVDG-RTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILIT---KDGRVKVTDF 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15230288  295 GLSdfvrpdeRL---------NDIVGSAYYVAPEVLHRSYTTE-ADVWSIGVIAYILLCGSRPF 348
Cdd:NF033483 152 GIA-------RAlssttmtqtNSVLGTVHYLSPEQARGGTVDArSDIYSLGIVLYEMLTGRPPF 208
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
171-401 4.26e-20

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


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 94.91  E-value: 4.26e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288    171 QEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFE-DNANVYIVMELCGGGELLDRiLARGGKYSEDDA 249
Cdd:TIGR03903    4 HEVAIKLLRTDAPEEEHQRARFRRETALCARLY-HPNIVALLDSGEaPPGLLFAVFEYVPGRTLREV-LAADGALPAGET 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288    250 KAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFG----LSDFVRPDE----RLNDIVGSAYYVAPEVL 321
Cdd:TIGR03903   82 GRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRPHAKVLDFGigtlLPGVRDADVatltRTTEVLGTPTYCAPEQL 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288    322 H-RSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPsFDEPPWPSlSFEAKDFVKRLLYKDPRKRMTASQA 400
Cdd:TIGR03903  162 RgEPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQLSPVD-VSLPPWIA-GHPLGQVLRKALNKDPRQRAASAPA 239

                   .
gi 15230288    401 L 401
Cdd:TIGR03903  240 L 240
 
Name Accession Description Interval E-value
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
145-405 1.31e-127

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: 375.28  E-value: 1.31e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKKGElkdQEVAVKVIPKSKMTSaISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIV 224
Cdd:cd05117   3 ELGKVLGRGSFGVVRLAVHKKTG---EEYAVKIIDKKKLKS-EDEEMLRREIEILKRLD-HPNIVKLYEVFEDDKNLYLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLSDFVRPDE 304
Cdd:cd05117  78 MELCTGGELFDRIVKKG-SFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPIKIIDFGLAKIFEEGE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 305 RLNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDFV 383
Cdd:cd05117 157 KLKTVCGTPYYVAPEVLKGKgYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPEWKNVSEEAKDLI 236
                       250       260
                ....*....|....*....|..
gi 15230288 384 KRLLYKDPRKRMTASQALMHPW 405
Cdd:cd05117 237 KRLLVVDPKKRLTAAEALNHPW 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
145-406 5.27e-101

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 306.76  E-value: 5.27e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288    145 ELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSaiSIEDVRREVKILRALsGHQNLVQFYDAFEDNANVYIV 224
Cdd:smart00220   2 EILEKLGEGSFGKVYLARDKK---TGKLVAIKVIKKKKIKK--DRERILREIKILKKL-KHPNIVRLYDVFEDEDKLYLV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288    225 MELCGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFVRPDE 304
Cdd:smart00220  76 MEYCEGGDLFDLLKKRG-RLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLD---EDGHVKLADFGLARQLDPGE 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288    305 RLNDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTE-SGIFRAVLKADPSFDEPPWPsLSFEAKDF 382
Cdd:smart00220 152 KLTTFVGTPEYMAPEVLlGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQlLELFKKIGKPKPPFPPPEWD-ISPEAKDL 230
                          250       260
                   ....*....|....*....|....
gi 15230288    383 VKRLLYKDPRKRMTASQALMHPWI 406
Cdd:smart00220 231 IRKLLVKDPEKRLTAEEALQHPFF 254
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
145-405 1.15e-85

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: 267.08  E-value: 1.15e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGytcSAKFKKGELKDQEVAVKVIPKSKMtSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIV 224
Cdd:cd14003   3 ELGKTLGEGSFG---KVKLARHKLTGEKVAIKIIDKSKL-KEEIEEKIKREIEIMKLLN-HPNIIKLYEVIETENKIYLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsmLKVIDFGLSDFVRPDE 304
Cdd:cd14003  78 MEYASGGELFDYIVNNG-RLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGN---LKIIDFGLSNEFRGGS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 305 RLNDIVGSAYYVAPEVLHRS--YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPsfdePPWPSLSFEAKDF 382
Cdd:cd14003 154 LLKTFCGTPAYAAPEVLLGRkyDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKY----PIPSHLSPDARDL 229
                       250       260
                ....*....|....*....|...
gi 15230288 383 VKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd14003 230 IRRMLVVDPSKRITIEEILNHPW 252
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
140-405 3.66e-83

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: 261.15  E-value: 3.66e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 140 LQSRIELGEEIGRGHFGYTCSAKFKK-GELkdqeVAVKVIPKSKMTSA-ISIEDvrrEVKILRALSgHQNLVQFYDAFED 217
Cdd:cd14083   1 IRDKYEFKEVLGTGAFSEVVLAEDKAtGKL----VAIKCIDKKALKGKeDSLEN---EIAVLRKIK-HPNIVQLLDIYES 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 218 NANVYIVMELCGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLS 297
Cdd:cd14083  73 KSHLYLVMELVTGGELFDRIVEKG-SYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSPDEDSKIMISDFGLS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 298 DfVRPDERLNDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLS 376
Cdd:cd14083 152 K-MEDSGVMSTACGTPGYVAPEVLaQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEYEFDSPYWDDIS 230
                       250       260
                ....*....|....*....|....*....
gi 15230288 377 FEAKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd14083 231 DSAKDFIRHLMEKDPNKRYTCEQALEHPW 259
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
145-408 1.48e-76

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: 244.17  E-value: 1.48e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKKGElkdQEVAVKVIPKSKMTSA-ISIEDvrrEVKILRALSgHQNLVQFYDAFEDNANVYI 223
Cdd:cd14167   6 DFREVLGTGAFSEVVLAEEKRTQ---KLVAIKCIAKKALEGKeTSIEN---EIAVLHKIK-HPNIVALDDIYESGGHLYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLSDFVRPD 303
Cdd:cd14167  79 IMQLVSGGELFDRIVEKG-FYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSLDEDSKIMISDFGLSKIEGSG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ERLNDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDF 382
Cdd:cd14167 158 SVMSTACGTPGYVAPEVLaQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDSPYWDDISDSAKDF 237
                       250       260
                ....*....|....*....|....*.
gi 15230288 383 VKRLLYKDPRKRMTASQALMHPWIAG 408
Cdd:cd14167 238 IQHLMEKDPEKRFTCEQALQHPWIAG 263
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
140-413 1.19e-72

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: 234.40  E-value: 1.19e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 140 LQSRIELGEEIGRGHFGYTCSAKFKKGElkdQEVAVKVIPKSKMTSAISIedVRREVKILRALSgHQNLVQFYDAFEDNA 219
Cdd:cd14169   1 INSVYELKEKLGEGAFSEVVLAQERGSQ---RLVALKCIPKKALRGKEAM--VENEIAVLRRIN-HENIVSLEDIYESPT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 220 NVYIVMELCGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLSDF 299
Cdd:cd14169  75 HLYLAMELVTGGELFDRIIERG-SYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATPFEDSKIMISDFGLSKI 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 300 vRPDERLNDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFE 378
Cdd:cd14169 154 -EAQGMLSTACGTPGYVAPELLeQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYEFDSPYWDDISES 232
                       250       260       270
                ....*....|....*....|....*....|....*
gi 15230288 379 AKDFVKRLLYKDPRKRMTASQALMHPWIAGYKKID 413
Cdd:cd14169 233 AKDFIRHLLERDPEKRFTCEQALQHPWISGDTALD 267
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
148-408 1.89e-72

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: 234.12  E-value: 1.89e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIEDvrrEVKILRALSgHQNLVQFYDAFEDNANVYIVMEL 227
Cdd:cd14166   9 EVLGSGAFSEVYLVKQRS---TGKLYALKCIKKSPLSRDSSLEN---EIAVLKRIK-HENIVTLEDIYESTTHYYLVMQL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 228 CGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLSDfVRPDERLN 307
Cdd:cd14166  82 VSGGELFDRILERG-VYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTPDENSKIMITDFGLSK-MEQNGIMS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 308 DIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDFVKRL 386
Cdd:cd14166 160 TACGTPGYVAPEVLaQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFESPFWDDISESAKDFIRHL 239
                       250       260
                ....*....|....*....|..
gi 15230288 387 LYKDPRKRMTASQALMHPWIAG 408
Cdd:cd14166 240 LEKNPSKRYTCEKALSHPWIIG 261
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
145-406 5.44e-71

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: 228.90  E-value: 5.44e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIV 224
Cdd:cd14007   3 EIGKPLGKGKFGNVYLAREKK---SGFIVALKVISKSQLQKSGLEHQLRREIEIQSHLR-HPNILRLYGYFEDKKRIYLI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGELLdRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsmLKVIDFGLSDFVrPDE 304
Cdd:cd14007  79 LEYAPNGELY-KELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGE---LKLADFGWSVHA-PSN 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 305 RLNDIVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFdeppWPSLSFEAKDFV 383
Cdd:cd14007 154 RRKTFCGTLDYLPPEMVEgKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKF----PSSVSPEAKDLI 229
                       250       260
                ....*....|....*....|...
gi 15230288 384 KRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14007 230 SKLLQKDPSKRLSLEQVLNHPWI 252
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
150-406 1.38e-70

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: 227.88  E-value: 1.38e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFG--YTCSAKfKKGelkdQEVAVKVIPKSKmtsAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMEL 227
Cdd:cd14103   1 LGRGKFGtvYRCVEK-ATG----KELAAKFIKCRK---AKDREDVRNEIEIMNQLR-HPRLLQLYDAFETPREMVLVMEY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 228 CGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSmLKVIDFGLSDFVRPDERLN 307
Cdd:cd14103  72 VAGGELFERVVDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSRTGNQ-IKIIDFGLARKYDPDKKLK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 308 DIVGSAYYVAPEVLHR---SYTTeaDVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDFVK 384
Cdd:cd14103 151 VLFGTPEFVAPEVVNYepiSYAT--DMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKWDFDDEAFDDISDEAKDFIS 228
                       250       260
                ....*....|....*....|..
gi 15230288 385 RLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14103 229 KLLVKDPRKRMSAAQCLQHPWL 250
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
140-408 1.77e-70

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: 229.33  E-value: 1.77e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 140 LQSRIELGEEIGRGHFG--YTCsakFKKGelKDQEVAVKVIPKSkmtsaISIEDVRREVKILRALSgHQNLVQFYDAFED 217
Cdd:cd14085   1 LEDFFEIESELGRGATSvvYRC---RQKG--TQKPYAVKKLKKT-----VDKKIVRTEIGVLLRLS-HPNIIKLKEIFET 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 218 NANVYIVMELCGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLS 297
Cdd:cd14085  70 PTEISLVLELVTGGELFDRIVEKG-YYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPDAPLKIADFGLS 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 298 DFVRPDERLNDIVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPFW-ARTESGIFRAVLKADPSFDEPPWPSL 375
Cdd:cd14085 149 KIVDQQVTMKTVCGTPGYCAPEILRgCAYGPEVDMWSVGVITYILLCGFEPFYdERGDQYMFKRILNCDYDFVSPWWDDV 228
                       250       260       270
                ....*....|....*....|....*....|...
gi 15230288 376 SFEAKDFVKRLLYKDPRKRMTASQALMHPWIAG 408
Cdd:cd14085 229 SLNAKDLVKKLIVLDPKKRLTTQQALQHPWVTG 261
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
150-405 3.90e-69

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: 224.07  E-value: 3.90e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTcsakfKKGELK--DQEVAVKVIPKSKMTSaisiEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMEL 227
Cdd:cd14006   1 LGRGRFGVV-----KRCIEKatGREFAAKFIPKRDKKK----EAVLREISILNQLQ-HPRIIQLHEAYESPTELVLILEL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 228 CGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSmLKVIDFGLSDFVRPDERLN 307
Cdd:cd14006  71 CSGGELLDRLAERG-SLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSPQ-IKIIDFGLARKLNPGEELK 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 308 DIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDFVKRL 386
Cdd:cd14006 149 EIFGTPEFVAPEIVNGEpVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDFSEEYFSSVSQEAKDFIRKL 228
                       250
                ....*....|....*....
gi 15230288 387 LYKDPRKRMTASQALMHPW 405
Cdd:cd14006 229 LVKEPRKRPTAQEALQHPW 247
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
145-407 1.53e-68

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: 224.05  E-value: 1.53e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFgytcsAKFKKGELK--DQEVAVKVIPKSKmtsaisiEDVRREVKILRALSGHQNLVQFYDAFEDNANVY 222
Cdd:cd14091   3 EIKEEIGKGSY-----SVCKRCIHKatGKEYAVKIIDKSK-------RDPSEEIEILLRYGQHPNIITLRDVYDDGNSVY 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 223 IVMELCGGGELLDRILARgGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEN-SMLKVIDFGLSDFVR 301
Cdd:cd14091  71 LVTELLRGGELLDRILRQ-KFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGDpESLRICDFGFAKQLR 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 302 PDERLndIVGSAY---YVAPEVLHR-SYTTEADVWSIGVIAYILLCGSRPF-----------WARTESGIFravlkadpS 366
Cdd:cd14091 150 AENGL--LMTPCYtanFVAPEVLKKqGYDAACDIWSLGVLLYTMLAGYTPFasgpndtpeviLARIGSGKI--------D 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15230288 367 FDEPPWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWIA 407
Cdd:cd14091 220 LSGGNWDHVSDSAKDLVRKMLHVDPSQRPTAAQVLQHPWIR 260
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
143-405 3.19e-67

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: 219.92  E-value: 3.19e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFGYT--CSAKfkkgeLKDQEVAVKVIPKSKMTSAIS-----IEDVRREVKILRALSGHQNLVQFYDAF 215
Cdd:cd14093   4 KYEPKEILGRGVSSTVrrCIEK-----ETGQEFAVKIIDITGEKSSENeaeelREATRREIEILRQVSGHPNIIELHDVF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 216 EDNANVYIVMELCGGGELLDrILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFG 295
Cdd:cd14093  79 ESPTFIFLVFELCRKGELFD-YLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILL---DDNLNVKISDFG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 296 LSDFVRPDERLNDIVGSAYYVAPEVL-------HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFD 368
Cdd:cd14093 155 FATRLDEGEKLRELCGTPGYLAPEVLkcsmydnAPGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKYEFG 234
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 15230288 369 EPPWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd14093 235 SPEWDDISDTAKDLISKLLVVDPKKRLTAEEALEHPF 271
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
145-436 3.27e-66

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: 218.38  E-value: 3.27e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKK-GELkdqeVAVKVIPKSKMTSAISieDVRREVKILRALSgHQNLVQFYDAFEDNANVYI 223
Cdd:cd14168  13 EFKEVLGTGAFSEVVLAEERAtGKL----FAVKCIPKKALKGKES--SIENEIAVLRKIK-HENIVALEDIYESPNHLYL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLSDFVRPD 303
Cdd:cd14168  86 VMQLVSGGELFDRIVEKG-FYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQDEESKIMISDFGLSKMEGKG 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ERLNDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDF 382
Cdd:cd14168 165 DVMSTACGTPGYVAPEVLaQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFDSPYWDDISDSAKDF 244
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 15230288 383 VKRLLYKDPRKRMTASQALMHPWIAGYKKIDIPFDILIFKQIKAYLRSSSLRKA 436
Cdd:cd14168 245 IRNLMEKDPNKRYTCEQALRHPWIAGDTALCKNIHESVSAQIRKNFAKSKWRQA 298
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
139-408 1.27e-65

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: 217.17  E-value: 1.27e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 139 ELQSRIELgeeIGRGHFGyTCSakfKKGELKD-QEVAVKVIPKSKmtsaisieDVRREVKILRALSGHQNLVQFYDAFED 217
Cdd:cd14092   6 ELDLREEA---LGDGSFS-VCR---KCVHKKTgQEFAVKIVSRRL--------DTSREVQLLRLCQGHPNIVKLHEVFQD 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 218 NANVYIVMELCGGGELLDRIlARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLS 297
Cdd:cd14092  71 ELHTYLVMELLRGGELLERI-RKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDDAEIKIVDFGFA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 298 DFVRPDERLNDIVGSAYYVAPEVLHRS-----YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLK----ADPSFD 368
Cdd:cd14092 150 RLKPENQPLKTPCFTLPYAAPEVLKQAlstqgYDESCDLWSLGVILYTMLSGQVPFQSPSRNESAAEIMKriksGDFSFD 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 15230288 369 EPPWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWIAG 408
Cdd:cd14092 230 GEEWKNVSSEAKSLIQGLLTVDPSKRLTMSELRNHPWLQG 269
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
150-406 4.45e-65

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: 213.93  E-value: 4.45e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKGElkdQEVAVKVIPKSKMTSaisiEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd14087   9 IGRGSFSRVVRVEHRVTR---QPYAIKMIETKCRGR----EVCESELNVLRRVR-HTNIIQLIEVFETKERVYMVMELAT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLSDFVR--PDERLN 307
Cdd:cd14087  81 GGELFDRIIAKG-SFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPDSKIMITDFGLASTRKkgPNCLMK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 308 DIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDFVKRL 386
Cdd:cd14087 160 TTCGTPEYIAPEILLRKpYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSGEPWPSVSNLAKDFIDRL 239
                       250       260
                ....*....|....*....|
gi 15230288 387 LYKDPRKRMTASQALMHPWI 406
Cdd:cd14087 240 LTVNPGERLSATQALKHPWI 259
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
145-406 7.00e-65

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: 213.22  E-value: 7.00e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSaisIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIV 224
Cdd:cd05122   3 EILEKIGKGGFGVVYKARHKK---TGQIVAIKKINLESKEK---KESILNEIAILKKCK-HPNIVKYYGSYLKKDELWIV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsmLKVIDFGLSDFVRPDE 304
Cdd:cd05122  76 MEFCSGGSLKDLLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGE---VKLIDFGLSAQLSDGK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 305 RLNDIVGSAYYVAPEVLHR-SYTTEADVWSIGVIAYILLCGSRPFwarTESGIFRAVLKAD----PSFDEPPWPSLSFea 379
Cdd:cd05122 153 TRNTFVGTPYWMAPEVIQGkPYGFKADIWSLGITAIEMAEGKPPY---SELPPMKALFLIAtngpPGLRNPKKWSKEF-- 227
                       250       260
                ....*....|....*....|....*..
gi 15230288 380 KDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd05122 228 KDFLKKCLQKDPEKRPTAEQLLKHPFI 254
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
142-407 8.12e-65

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: 214.21  E-value: 8.12e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 142 SRIELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMtSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANV 221
Cdd:cd14086   1 DEYDLKEELGKGAFSVVRRCVQKS---TGQEFAAKIINTKKL-SARDHQKLEREARICRLLK-HPNIVRLHDSISEEGFH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 YIVMELCGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLSDFVR 301
Cdd:cd14086  76 YLVFDLVTGGELFEDIVARE-FYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEVQ 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 302 PD-ERLNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEA 379
Cdd:cd14086 155 GDqQAWFGFAGTPGYLSPEVLRKDpYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPEWDTVTPEA 234
                       250       260
                ....*....|....*....|....*...
gi 15230288 380 KDFVKRLLYKDPRKRMTASQALMHPWIA 407
Cdd:cd14086 235 KDLINQMLTVNPAKRITAAEALKHPWIC 262
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
145-406 3.63e-64

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: 211.96  E-value: 3.63e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKKGELkdqEVAVKVIPKSKMTSA---ISIEDVRREVKILRALSgHQNLVQFYDAFEDNANV 221
Cdd:cd14105   8 DIGEELGSGQFAVVKKCREKSTGL---EYAAKFIKKRRSKASrrgVSREDIEREVSILRQVL-HPNIITLHDVFENKTDV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 YIVMELCGGGELLDrILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPEN-FLYTSKEENSMLKVIDFGLSDFV 300
Cdd:cd14105  84 VLILELVAGGELFD-FLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENiMLLDKNVPIPRIKLIDFGLAHKI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 301 RPDERLNDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEA 379
Cdd:cd14105 163 EDGNEFKNIFGTPEFVAPEIVnYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVNYDFDDEYFSNTSELA 242
                       250       260
                ....*....|....*....|....*..
gi 15230288 380 KDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14105 243 KDFIRQLLVKDPRKRMTIQESLRHPWI 269
Pkinase pfam00069
Protein kinase domain;
145-406 3.10e-63

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 207.48  E-value: 3.10e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288   145 ELGEEIGRGHFGytcsaKFKKGELKD--QEVAVKVIPKSKMTSaISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVY 222
Cdd:pfam00069   2 EVLRKLGSGSFG-----TVYKAKHRDtgKIVAIKKIKKEKIKK-KKDKNILREIKILKKLN-HPNIVRLYDAFEDKDNLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288   223 IVMELCGGGELLDRIlARGGKYSEDDAKAVLIQILnvvafchlQGVvhrdlkpenflytskeensmlkvidfglsdfvRP 302
Cdd:pfam00069  75 LVLEYVEGGSLFDLL-SEKGAFSEREAKFIMKQIL--------EGL--------------------------------ES 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288   303 DERLNDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEpPWPSLSFEAKD 381
Cdd:pfam00069 114 GSSLTTFVGTPWYMAPEVLgGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPE-LPSNLSEEAKD 192
                         250       260
                  ....*....|....*....|....*
gi 15230288   382 FVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:pfam00069 193 LLKKLLKKDPSKRLTATQALQHPWF 217
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
143-405 1.31e-62

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: 207.26  E-value: 1.31e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFGytcSAKFKKGELKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVY 222
Cdd:cd14663   1 RYELGRTLGEGTFA---KVKFARNTKTGESVAIKIIDKEQVAREGMVEQIKREIAIMKLLR-HPNIVELHEVMATKTKIF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 223 IVMELCGGGELLDRIlARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLS---DF 299
Cdd:cd14663  77 FVMELVTGGELFSKI-AKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLL---DEDGNLKISDFGLSalsEQ 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 300 VRPDERLNDIVGSAYYVAPEVL-HRSYT-TEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFdePPWpsLSF 377
Cdd:cd14663 153 FRQDGLLHTTCGTPNYVAPEVLaRRGYDgAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEY--PRW--FSP 228
                       250       260
                ....*....|....*....|....*...
gi 15230288 378 EAKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd14663 229 GAKSLIKRILDPNPSTRITVEQIMASPW 256
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
138-406 2.90e-62

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: 206.86  E-value: 2.90e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 138 KELQSRIELGEEIGRGHFGYTCSAkFKKGelKDQEVAVKVIPKSKMTSAIS-----IEDVRREVKILRALSgHQNLVQFY 212
Cdd:cd14084   2 KELRKKYIMSRTLGSGACGEVKLA-YDKS--TCKKVAIKIINKRKFTIGSRreinkPRNIETEIEILKKLS-HPCIIKIE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 213 DAFEDNANVYIVMELCGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVI 292
Cdd:cd14084  78 DFFDAEDDYYIVLELMEGGELFDRVVSNK-RLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEECLIKIT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 293 DFGLSDFVRPDERLNDIVGSAYYVAPEVL----HRSYTTEADVWSIGVIAYILLCGSRPF-WARTESGIFRAVLKADPSF 367
Cdd:cd14084 157 DFGLSKILGETSLMKTLCGTPTYLAPEVLrsfgTEGYTRAVDCWSLGVILFICLSGYPPFsEEYTQMSLKEQILSGKYTF 236
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 15230288 368 DEPPWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14084 237 IPKAWKNVSEEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
146-405 3.70e-62

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: 205.97  E-value: 3.70e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 146 LGEEIGRGHFGytcsaKFKKGE--LKDQEVAVKVIPKSKMTSAISIEDVRREVKILRaLSGHQNLVQFYDAFEDNANVYI 223
Cdd:cd14079   6 LGKTLGVGSFG-----KVKLAEheLTGHKVAVKILNRQKIKSLDMEEKIRREIQILK-LFRHPHIIRLYEVIETPTDIFM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSDFVRPD 303
Cdd:cd14079  80 VMEYVSGGELFDYIVQKG-RLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDS---NMNVKIADFGLSNIMRDG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ERLNDIVGSAYYVAPEVLH-RSYT-TEADVWSIGVIAYILLCGSRPF--------WARTESGIFravlkADPSFdeppwp 373
Cdd:cd14079 156 EFLKTSCGSPNYAAPEVISgKLYAgPEVDVWSCGVILYALLCGSLPFddehipnlFKKIKSGIY-----TIPSH------ 224
                       250       260       270
                ....*....|....*....|....*....|..
gi 15230288 374 sLSFEAKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd14079 225 -LSPGARDLIKRMLVVDPLKRITIPEIRQHPW 255
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
147-406 1.24e-61

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: 204.71  E-value: 1.24e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 147 GEEIGRGHFgytcsAKFKKGELKD--QEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIV 224
Cdd:cd14099   6 GKFLGKGGF-----AKCYEVTDMStgKVYAGKVVPKSSLTKPKQREKLKSEIKIHRSLK-HPNIVKFHDCFEDEENVYIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGELLDrILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFVRPD- 303
Cdd:cd14099  80 LELCSNGSLME-LLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLD---ENMNVKIGDFGLAARLEYDg 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ERLNDIVGSAYYVAPEVLHRS--YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFdePPWPSLSFEAKD 381
Cdd:cd14099 156 ERKKTLCGTPNYIAPEVLEKKkgHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSF--PSHLSISDEAKD 233
                       250       260
                ....*....|....*....|....*
gi 15230288 382 FVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14099 234 LIRSMLQPDPTKRPSLDEILSHPFF 258
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
150-406 3.87e-61

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: 203.55  E-value: 3.87e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGytcsaKFKKGELK--DQEVAVKVIPKSKM-----------TSAISIEDVRREVKILRALSgHQNLVQFYDAFE 216
Cdd:cd14008   1 LGRGSFG-----KVKLALDTetGQLYAIKIFNKSRLrkrregkndrgKIKNALDDVRREIAIMKKLD-HPNIVRLYEVID 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 217 DNAN--VYIVMELCGGGELLDR-ILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVID 293
Cdd:cd14008  75 DPESdkLYLVLEYCEGGPVMELdSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLT---ADGTVKISD 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 294 FGLSDFV-RPDERLNDIVGSAYYVAPEVLHRSYTT----EADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKadpSFD 368
Cdd:cd14008 152 FGVSEMFeDGNDTLQKTAGTPAFLAPELCDGDSKTysgkAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQN---QND 228
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 15230288 369 EPPWPS-LSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14008 229 EFPIPPeLSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
140-406 6.48e-60

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: 200.63  E-value: 6.48e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 140 LQSRIELGEEIGRGHFgytcsAKFKKGELKD--QEVAVKVIPKSKMTSA---ISIEDVRREVKILRALSgHQNLVQFYDA 214
Cdd:cd14194   3 VDDYYDTGEELGSGQF-----AVVKKCREKStgLQYAAKFIKKRRTKSSrrgVSREDIEREVSILKEIQ-HPNVITLHEV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 215 FEDNANVYIVMELCGGGELLDrILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKE-ENSMLKVID 293
Cdd:cd14194  77 YENKTDVILILELVAGGELFD-FLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNvPKPRIKIID 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 294 FGLSDFVRPDERLNDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPW 372
Cdd:cd14194 156 FGLAHKIDFGNEFKNIFGTPEFVAPEIVnYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYF 235
                       250       260       270
                ....*....|....*....|....*....|....
gi 15230288 373 PSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14194 236 SNTSALAKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
147-406 2.35e-59

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: 199.11  E-value: 2.35e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 147 GEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIEdVRREVKILRALSGHQNLVQFYDAFEDNANVYIVME 226
Cdd:cd14106  13 STPLGRGKFAVVRKCIHKE---TGKEYAAKFLRKRRRGQDCRNE-ILHEIAVLELCKDCPRVVNLHEVYETRSELILILE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 227 LCGGGELlDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLSDFVRPDERL 306
Cdd:cd14106  89 LAAGGEL-QTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPLGDIKLCDFGISRVIGEGEEI 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 307 NDIVGSAYYVAPEVLhrSY---TTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDFV 383
Cdd:cd14106 168 REILGTPDYVAPEIL--SYepiSLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPEELFKDVSPLAIDFI 245
                       250       260
                ....*....|....*....|...
gi 15230288 384 KRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14106 246 KRLLVKDPEKRLTAKECLEHPWL 268
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
150-404 3.96e-59

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: 196.72  E-value: 3.96e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSaiSIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd00180   1 LGKGSFGKVYKARDKE---TGKKVAVKVIPKEKLKK--LLEELLREIEILKKLN-HPNIVKLYDVFETENFLYLVMEYCE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSDFVRPDERLNDI 309
Cdd:cd00180  75 GGSLKDLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDS---DGTVKLADFGLAKDLDSDDSLLKT 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 310 VG---SAYYVAPEVL-HRSYTTEADVWSIGVIAYILlcgsrpfwartesgifravlkadpsfdeppwpslsFEAKDFVKR 385
Cdd:cd00180 152 TGgttPPYYAPPELLgGRYYGPKVDIWSLGVILYEL-----------------------------------EELKDLIRR 196
                       250
                ....*....|....*....
gi 15230288 386 LLYKDPRKRMTASQALMHP 404
Cdd:cd00180 197 MLQYDPKKRPSAKELLEHL 215
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
174-405 6.10e-59

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: 197.70  E-value: 6.10e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 174 AVKVIPKSKM-TSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELCGGGELLDRILARGGkYSEDDAKAV 252
Cdd:cd14098  29 AIKQIVKRKVaGNDKNLQLFQREINILKSLE-HPGIVRLIDWYEDDQHIYLVMEYVEGGDLMDFIMAWGA-IPEQHAREL 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 253 LIQILNVVAFCHLQGVVHRDLKPENFLYTsKEENSMLKVIDFGLSDFVRPDERLNDIVGSAYYVAPEVLHRS-------Y 325
Cdd:cd14098 107 TKQILEAMAYTHSMGITHRDLKPENILIT-QDDPVIVKISDFGLAKVIHTGTFLVTFCGTMAYLAPEILMSKeqnlqggY 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 326 TTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKAdpSFDEPPWPSL--SFEAKDFVKRLLYKDPRKRMTASQALMH 403
Cdd:cd14098 186 SNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKG--RYTQPPLVDFniSEEAIDFILRLLDVDPEKRMTAAQALDH 263

                ..
gi 15230288 404 PW 405
Cdd:cd14098 264 PW 265
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
140-406 5.73e-58

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: 194.91  E-value: 5.73e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 140 LQSRIELGEEIGRGHFgytcsAKFKKGE--LKDQEVAVKVIPKSKMTSaiSIEDVRREVKILRALSgHQNLVQFYDAFED 217
Cdd:cd14078   1 LLKYYELHETIGSGGF-----AKVKLAThiLTGEKVAIKIMDKKALGD--DLPRVKTEIEALKNLS-HQHICRLYHVIET 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 218 NANVYIVMELCGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLS 297
Cdd:cd14078  73 DNKIFMVLEYCPGGELFDYIVAKD-RLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLD---EDQNLKLIDFGLC 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 298 dfVRP----DERLNDIVGSAYYVAPE-VLHRSYT-TEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKAdpSFDEPP 371
Cdd:cd14078 149 --AKPkggmDHHLETCCGSPAYAAPElIQGKPYIgSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSG--KYEEPE 224
                       250       260       270
                ....*....|....*....|....*....|....*
gi 15230288 372 WpsLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14078 225 W--LSPSSKLLLDQMLQVDPKKRITVKELLNHPWV 257
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
145-406 5.75e-58

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: 195.61  E-value: 5.75e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSA---ISIEDVRREVKILRALSgHQNLVQFYDAFEDNANV 221
Cdd:cd14195   8 EMGEELGSGQFAIVRKCREKG---TGKEYAAKFIKKRRLSSSrrgVSREEIEREVNILREIQ-HPNIITLHDIFENKTDV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 YIVMELCGGGELLDrILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKE-ENSMLKVIDFGLSDFV 300
Cdd:cd14195  84 VLILELVSGGELFD-FLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNvPNPRIKLIDFGIAHKI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 301 RPDERLNDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEA 379
Cdd:cd14195 163 EAGNEFKNIFGTPEFVAPEIVnYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSNTSELA 242
                       250       260
                ....*....|....*....|....*..
gi 15230288 380 KDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14195 243 KDFIRRLLVKDPKKRMTIAQSLEHSWI 269
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
145-405 6.97e-58

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: 194.85  E-value: 6.97e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKKGelkDQEVAVKVIPKSKMtsaISIED-VRREVKILRALSgHQNLVQFYDAFEDNANVYI 223
Cdd:cd14095   3 DIGRVIGDGNFAVVKECRDKAT---DKEYALKIIDKAKC---KGKEHmIENEVAILRRVK-HPNIVQLIEEYDTDTELYL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDRIlARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSM-LKVIDFGLSDFVRp 302
Cdd:cd14095  76 VMELVKGGDLFDAI-TSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEDGSKsLKLADFGLATEVK- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 303 dERLNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWA--RTESGIFRAVLKADPSFDEPPWPSLSFEA 379
Cdd:cd14095 154 -EPLFTVCGTPTYVAPEILAETgYGLKVDIWAAGVITYILLCGFPPFRSpdRDQEELFDLILAGEFEFLSPYWDNISDSA 232
                       250       260
                ....*....|....*....|....*.
gi 15230288 380 KDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd14095 233 KDLISRMLVVDPEKRYSAGQVLDHPW 258
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
171-405 8.75e-58

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: 194.81  E-value: 8.75e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 171 QEVAVKVI---PKSkmtsaisiedvRREVKILRALSGHQNLVQFYDAFEdnaNVY-------IVMELCGGGELLDRILAR 240
Cdd:cd14089  27 EKFALKVLrdnPKA-----------RREVELHWRASGCPHIVRIIDVYE---NTYqgrkcllVVMECMEGGELFSRIQER 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 241 G-GKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLSDFVRPDERLNDIVGSAYYVAPE 319
Cdd:cd14089  93 AdSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPNAILKLTDFGFAKETTTKKSLQTPCYTPYYVAPE 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 320 VLHRS-YTTEADVWSIGVIAYILLCGSRPFW----ARTESGIFRAVLKADPSFDEPPWPSLSFEAKDFVKRLLYKDPRKR 394
Cdd:cd14089 173 VLGPEkYDKSCDMWSLGVIMYILLCGYPPFYsnhgLAISPGMKKRIRNGQYEFPNPEWSNVSEEAKDLIRGLLKTDPSER 252
                       250
                ....*....|.
gi 15230288 395 MTASQALMHPW 405
Cdd:cd14089 253 LTIEEVMNHPW 263
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
143-406 2.56e-57

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: 193.18  E-value: 2.56e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFG--YTCSAKfKKGELkdqeVAVKVIPKSKmtsAISIEDVRREVKILRALSgHQNLVQFYDAFEDNAN 220
Cdd:cd14114   3 HYDILEELGTGAFGvvHRCTER-ATGNN----FAAKFIMTPH---ESDKETVRKEIQIMNQLH-HPKLINLHDAFEDDNE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 VYIVMELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSmLKVIDFGLSDFV 300
Cdd:cd14114  74 MVLILEFLSGGELFERIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRSNE-VKLIDFGLATHL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 301 RPDERLNDIVGSAYYVAPEVLHRS----YTteaDVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLS 376
Cdd:cd14114 153 DPKESVKVTTGTAEFAAPEIVEREpvgfYT---DMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDDSAFSGIS 229
                       250       260       270
                ....*....|....*....|....*....|
gi 15230288 377 FEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14114 230 EEAKDFIRKLLLADPNKRMTIHQALEHPWL 259
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
146-406 3.55e-57

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: 193.17  E-value: 3.55e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 146 LGEEIGRGHFGYTCSAKFKKgELKDQEVAVKVIPKSKMTSaisiEDVR----REVKILRALSgHQNLVQFYDAFEDNANV 221
Cdd:cd14080   4 LGKTIGEGSYSKVKLAEYTK-SGLKEKVACKIIDKKKAPK----DFLEkflpRELEILRKLR-HPNIIQVYSIFERGSKV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 YIVMELCGGGELLDRILARgGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSDFVR 301
Cdd:cd14080  78 FIFMEYAEHGDLLEYIQKR-GALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDS---NNNVKLSDFGFARLCP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 302 PDERL---NDIVGSAYYVAPEVLH-RSYT-TEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPsLS 376
Cdd:cd14080 154 DDDGDvlsKTFCGSAAYAAPEILQgIPYDpKKYDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVRFPSSVKK-LS 232
                       250       260       270
                ....*....|....*....|....*....|
gi 15230288 377 FEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14080 233 PECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
147-406 4.08e-57

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: 193.15  E-value: 4.08e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 147 GEEIGRGHFGYTCSAKFKKGELKdqeVAVKVIPKSKMTSAiSIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVME 226
Cdd:cd14097   6 GRKLGQGSFGVVIEATHKETQTK---WAIKKINREKAGSS-AVKLLEREVDILKHVN-HAHIIHLEEVFETPKRMYLVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 227 LCGGGELlDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKE-ENSM---LKVIDFGLS--DFV 300
Cdd:cd14097  81 LCEDGEL-KELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIiDNNDklnIKVTDFGLSvqKYG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 301 RPDERLNDIVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEA 379
Cdd:cd14097 160 LGEDMLQETCGTPIYMAPEVISaHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTQSVWQSVSDAA 239
                       250       260
                ....*....|....*....|....*..
gi 15230288 380 KDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14097 240 KNVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
145-406 6.81e-57

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: 192.24  E-value: 6.81e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTcsaKFKKGELKDQEVAVKVIPKSKMtSAISIEDVRREVKILRaLSGHQNLVQFYDAFEDNANVYIV 224
Cdd:cd14074   6 DLEETLGRGHFAVV---KLARHVFTGEKVAVKVIDKTKL-DDVSKAHLFQEVRCMK-LVQHPNVVRLYEVIDTQTKLYLI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskEENSMLKVIDFGLSDFVRPDE 304
Cdd:cd14074  81 LELGDGGDMYDYIMKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFF--EKQGLVKLTDFGFSNKFQPGE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 305 RLNDIVGSAYYVAPEV-LHRSYTTEA-DVWSIGVIAYILLCGSRPFWARTESGIFRAVLkaDPSFDEPpwPSLSFEAKDF 382
Cdd:cd14074 159 KLETSCGSLAYSAPEIlLGDEYDAPAvDIWSLGVILYMLVCGQPPFQEANDSETLTMIM--DCKYTVP--AHVSPECKDL 234
                       250       260
                ....*....|....*....|....
gi 15230288 383 VKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14074 235 IRRMLIRDPKKRASLEEIENHPWL 258
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
150-405 1.87e-56

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: 190.81  E-value: 1.87e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd05123   1 LGKGSFGKVLLVRKKD---TGKLYAMKVLRKKEIIKRKEVEHTLNERNILERVN-HPFIVKLHYAFQTEEKLYLVLDYVP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRiLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLS-DFVRPDERLND 308
Cdd:cd05123  77 GGELFSH-LSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLD---SDGHIKLTDFGLAkELSSDGDRTYT 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 309 IVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEppwpSLSFEAKDFVKRLL 387
Cdd:cd05123 153 FCGTPEYLAPEVLLGKgYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPE----YVSPEAKSLISGLL 228
                       250       260
                ....*....|....*....|.
gi 15230288 388 YKDPRKRMTASQALM---HPW 405
Cdd:cd05123 229 QKDPTKRLGSGGAEEikaHPF 249
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
143-401 3.18e-56

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: 190.49  E-value: 3.18e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFGYTCSAKFKKGelkDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVY 222
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLL---GRPVAIKVLRPELAEDEEFRERFLREARALARLS-HPNIVRVYDVGEDDGRPY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 223 IVMELCGGGELlDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFVRP 302
Cdd:cd14014  77 IVMEYVEGGSL-ADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLT---EDGRVKLTDFGIARALGD 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 303 DE--RLNDIVGSAYYVAPEVLHRSYTT-EADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEA 379
Cdd:cd14014 153 SGltQTGSVLGTPAYMAPEQARGGPVDpRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPAL 232
                       250       260
                ....*....|....*....|..
gi 15230288 380 KDFVKRLLYKDPRKRMTASQAL 401
Cdd:cd14014 233 DAIILRALAKDPEERPQSAAEL 254
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
171-409 3.26e-56

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: 190.90  E-value: 3.26e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 171 QEVAVKVI---PKSKMTSAiSIEDVR----REVKILRALSGHQNLVQFYDAFEDNANVYIVMELCGGGELLDrILARGGK 243
Cdd:cd14182  29 QEYAVKIIditGGGSFSPE-EVQELReatlKEIDILRKVSGHPNIIQLKDTYETNTFFFLVFDLMKKGELFD-YLTEKVT 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 244 YSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLSDFVRPDERLNDIVGSAYYVAPEVL-- 321
Cdd:cd14182 107 LSEKETRKIMRALLEVICALHKLNIVHRDLKPENILL---DDDMNIKLTDFGFSCQLDPGEKLREVCGTPGYLAPEIIec 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 322 -----HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDFVKRLLYKDPRKRMT 396
Cdd:cd14182 184 smddnHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFGSPEWDDRSDTVKDLISRFLVVQPQKRYT 263
                       250
                ....*....|...
gi 15230288 397 ASQALMHPWIAGY 409
Cdd:cd14182 264 AEEALAHPFFQQY 276
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
143-406 2.35e-55

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: 188.11  E-value: 2.35e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFG--YtcsakfkKGELKD--QEVAVKVIPKSKMTSAiSIEDVRREVKILRALSgHQNLVQFYDAFEDN 218
Cdd:cd06606   1 RWKKGELLGKGSFGsvY-------LALNLDtgELMAVKEVELSGDSEE-ELEALEREIRILSSLK-HPNIVRYLGTERTE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 219 ANVYIVMELCGGGELLDrILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLS- 297
Cdd:cd06606  72 NTLNIFLEYVPGGSLAS-LLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDS---DGVVKLADFGCAk 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 298 --DFVRPDERLNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPfWARTESGIfrAVLKADPSFDEPPW-- 372
Cdd:cd06606 148 rlAEIATGEGTKSLRGTPYWMAPEVIRGEgYGRAADIWSLGCTVIEMATGKPP-WSELGNPV--AALFKIGSSGEPPPip 224
                       250       260       270
                ....*....|....*....|....*....|....
gi 15230288 373 PSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd06606 225 EHLSEEAKDFLRKCLQRDPKKRPTADELLQHPFL 258
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
147-406 3.10e-54

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: 186.08  E-value: 3.10e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 147 GEEIGRGHFG--YTCSAKFKkgelkDQEVAVKVIPKSkmtSAISIEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIV 224
Cdd:cd14090   7 GELLGEGAYAsvQTCINLYT-----GKEYAVKIIEKH---PGHSRSRVFREVETLHQCQGHPNILQLIEYFEDDERFYLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGL-------S 297
Cdd:cd14090  79 FEKMRGGPLLSHIEKRV-HFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVSPVKICDFDLgsgiklsS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 298 DFVRP--DERLNDIVGSAYYVAPEVLH------RSYTTEADVWSIGVIAYILLCGSRPF---------WARTES------ 354
Cdd:cd14090 158 TSMTPvtTPELLTPVGSAEYMAPEVVDafvgeaLSYDKRCDLWSLGVILYIMLCGYPPFygrcgedcgWDRGEAcqdcqe 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 15230288 355 GIFRAVLKADPSFDEPPWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14090 238 LLFHSIQEGEYEFPEKEWSHISAEAKDLISHLLVRDASQRYTAEQVLQHPWV 289
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
137-394 5.07e-54

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 191.38  E-value: 5.07e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 137 SKELQSRIELGEEIGRGHFGYTCSAKFkkgELKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFE 216
Cdd:COG0515   2 SALLLGRYRILRLLGRGGMGVVYLARD---LRLGRPVALKVLRPELAADPEARERFRREARALARLN-HPNIVRVYDVGE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 217 DNANVYIVMELCGGGELLDRiLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGL 296
Cdd:COG0515  78 EDGRPYLVMEYVEGESLADL-LRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLT---PDGRVKLIDFGI 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 297 SDFVRPDE--RLNDIVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWP 373
Cdd:COG0515 154 ARALGGATltQTGTVVGTPGYMAPEQARgEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRP 233
                       250       260
                ....*....|....*....|.
gi 15230288 374 SLSFEAKDFVKRLLYKDPRKR 394
Cdd:COG0515 234 DLPPALDAIVLRALAKDPEER 254
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
145-405 5.17e-54

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: 184.38  E-value: 5.17e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAisiED-VRREVKILRALSgHQNLVQFYDAFEDNANVYI 223
Cdd:cd14185   3 EIGRTIGDGNFAVVKECRHWN---ENQEYAMKIIDKSKLKGK---EDmIESEILIIKSLS-HPNIVKLFEVYETEKEIYL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDRILaRGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSM-LKVIDFGLSDFV-R 301
Cdd:cd14185  76 ILEYVRGGDLFDAII-ESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNPDKSTtLKLADFGLAKYVtG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 302 PderLNDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWA--RTESGIFRAVLKADPSFDEPPWPSLSFE 378
Cdd:cd14185 155 P---IFTVCGTPTYVAPEILsEKGYGLEVDMWAAGVILYILLCGFPPFRSpeRDQEELFQIIQLGHYEFLPPYWDNISEA 231
                       250       260
                ....*....|....*....|....*..
gi 15230288 379 AKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd14185 232 AKDLISRLLVVDPEKRYTAKQVLQHPW 258
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
145-406 6.08e-54

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: 184.77  E-value: 6.08e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKKGELkdqEVAVKVIPKSKMTSA---ISIEDVRREVKILRALSgHQNLVQFYDAFEDNANV 221
Cdd:cd14196   8 DIGEELGSGQFAIVKKCREKSTGL---EYAAKFIKKRQSRASrrgVSREEIEREVSILRQVL-HPNIITLHDVYENRTDV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 YIVMELCGGGELLDrILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKE-ENSMLKVIDFGLSDFV 300
Cdd:cd14196  84 VLILELVSGGELFD-FLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNiPIPHIKLIDFGLAHEI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 301 RPDERLNDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEA 379
Cdd:cd14196 163 EDGVEFKNIFGTPEFVAPEIVnYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSHTSELA 242
                       250       260
                ....*....|....*....|....*..
gi 15230288 380 KDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14196 243 KDFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
150-405 6.71e-54

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: 183.96  E-value: 6.71e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFgytcsAKFKKGELKDQ--EVAVKVIPKSKMTSAiSIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMEL 227
Cdd:cd14009   1 IGRGSF-----ATVWKGRHKQTgeVVAIKEISRKKLNKK-LQENLESEIAILKSIK-HPNIVRLYDVQKTEDFIYLVLEY 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 228 CGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLSDFVRPDERLN 307
Cdd:cd14009  74 CAGGDLSQYIRKRG-RLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDDPVLKIADFGFARSLQPASMAE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 308 DIVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDFVKRL 386
Cdd:cd14009 153 TLCGSPLYMAPEILQfQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSDAVIPFPIAAQLSPDCKDLLRRL 232
                       250
                ....*....|....*....
gi 15230288 387 LYKDPRKRMTASQALMHPW 405
Cdd:cd14009 233 LRRDPAERISFEEFFAHPF 251
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
137-405 2.07e-53

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: 183.63  E-value: 2.07e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 137 SKELQSRIELGEEIGRGhfgytCSAKFKKGELKD--QEVAVKVIPKS--KMTSAiSIEDVR----REVKILRALSGHQNL 208
Cdd:cd14181   5 AKEFYQKYDPKEVIGRG-----VSSVVRRCVHRHtgQEFAVKIIEVTaeRLSPE-QLEEVRsstlKEIHILRQVSGHPSI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 209 VQFYDAFEDNANVYIVMELCGGGELLDrILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSM 288
Cdd:cd14181  79 ITLIDSYESSTFIFLVFDLMRRGELFD-YLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILL---DDQLH 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 289 LKVIDFGLSDFVRPDERLNDIVGSAYYVAPEVL-------HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVL 361
Cdd:cd14181 155 IKLSDFGFSCHLEPGEKLRELCGTPGYLAPEILkcsmdetHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIM 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15230288 362 KADPSFDEPPWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd14181 235 EGRYQFSSPEWDDRSSTVKDLISRLLVVDPEIRLTAEQALQHPF 278
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
142-406 5.22e-53

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: 181.82  E-value: 5.22e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 142 SRIELGEEIGRGHFGytcsaKFKKGELKD--QEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNA 219
Cdd:cd14073   1 HRYELLETLGKGTYG-----KVKLAIERAtgREVAIKSIKKDKIEDEQDMVRIRREIEIMSSLN-HPHIIRIYEVFENKD 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 220 NVYIVMELCGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLSDF 299
Cdd:cd14073  75 KIVIVMEYASGGELYDYISERR-RLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILL---DQNGNAKIADFGLSNL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 300 VRPDERLNDIVGSAYYVAPEVL--HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADpsFDEPPWPSlsf 377
Cdd:cd14073 151 YSKDKLLQTFCGSPLYASPEIVngTPYQGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGD--YREPTQPS--- 225
                       250       260
                ....*....|....*....|....*....
gi 15230288 378 EAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14073 226 DASGLIRWMLTVNPKRRATIEDIANHWWV 254
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
150-406 5.55e-53

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: 183.70  E-value: 5.55e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKgelKDQEVAVKVIPKsKMTSaisieDVRREVKILRALSGHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd14179  15 LGEGSFSICRKCLHKK---TNQEYAVKIVSK-RMEA-----NTQREIAALKLCEGHPNIVKLHEVYHDQLHTFLVMELLK 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRIlARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLSDFVRPDER-LND 308
Cdd:cd14179  86 GGELLERI-KKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESDNSEIKIIDFGFARLKPPDNQpLKT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 309 IVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTES-------GIFRAVLKADPSFDEPPWPSLSFEAK 380
Cdd:cd14179 165 PCFTLHYAAPELLnYNGYDESCDLWSLGVILYTMLSGQVPFQCHDKSltctsaeEIMKKIKQGDFSFEGEAWKNVSQEAK 244
                       250       260
                ....*....|....*....|....*.
gi 15230288 381 DFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14179 245 DLIQGLLTVDPNKRIKMSGLRYNEWL 270
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
143-406 1.07e-52

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: 180.74  E-value: 1.07e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAiSIEDVRREVKILRALSgHQNLVQFYDAFEDNANVY 222
Cdd:cd08215   1 KYEKIRVIGKGSFGSAYLVRRKS---DGKLYVLKEIDLSNMSEK-EREEALNEVKLLSKLK-HPNIVKYYESFEENGKLC 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 223 IVMELCGGGELLDRILAR---GGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSDF 299
Cdd:cd08215  76 IVMEYADGGDLAQKIKKQkkkGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTK---DGVVKLGDFGISKV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 300 VRPDERL-NDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPsfdePPWPS-LS 376
Cdd:cd08215 153 LESTTDLaKTVVGTPYYLSPELCeNKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQY----PPIPSqYS 228
                       250       260       270
                ....*....|....*....|....*....|
gi 15230288 377 FEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd08215 229 SELRDLVNSMLQKDPEKRPSANEILSSPFI 258
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
148-406 1.45e-52

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: 181.76  E-value: 1.45e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGyTCSAKFKKGelKDQEVAVKVIPKSKmtsaisiEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIVMEL 227
Cdd:cd14175   7 ETIGVGSYS-VCKRCVHKA--TNMEYAVKVIDKSK-------RDPSEEIEILLRYGQHPNIITLKDVYDDGKHVYLVTEL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 228 CGGGELLDRILaRGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEN-SMLKVIDFGLSDFVRPDE-R 305
Cdd:cd14175  77 MRGGELLDKIL-RQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDESGNpESLRICDFGFAKQLRAENgL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 306 LNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFW---ARTESGIFRAVLKADPSFDEPPWPSLSFEAKD 381
Cdd:cd14175 156 LMTPCYTANFVAPEVLKRQgYDEGCDIWSLGILLYTMLAGYTPFAngpSDTPEEILTRIGSGKFTLSGGNWNTVSDAAKD 235
                       250       260
                ....*....|....*....|....*
gi 15230288 382 FVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14175 236 LVSKMLHVDPHQRLTAKQVLQHPWI 260
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
144-406 1.82e-52

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: 180.49  E-value: 1.82e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 144 IELGEEIGRGHFGYTCSAKFKKGELKdqeVAVKVIpksKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYI 223
Cdd:cd14193   6 VNKEEILGGGRFGQVHKCEEKSSGLK---LAAKII---KARSQKEKEEVKNEIEVMNQLN-HANLIQLYDAFESRNDIVL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSmLKVIDFGLSDFVRPD 303
Cdd:cd14193  79 VMEYVDGGELFDRIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSREANQ-VKIIDFGLARRYKPR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ERLNDIVGSAYYVAPEVLHRSYTT-EADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDF 382
Cdd:cd14193 158 EKLRVNFGTPEFLAPEVVNYEFVSfPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFEDEEFADISEEAKDF 237
                       250       260
                ....*....|....*....|....
gi 15230288 383 VKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14193 238 ISKLLIKEKSWRMSASEALKHPWL 261
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
148-406 2.21e-52

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: 180.16  E-value: 2.21e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFG--YTCSAKFKKGELkdqevAVKVIpksKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVM 225
Cdd:cd14192  10 EVLGGGRFGqvHKCTELSTGLTL-----AAKII---KVKGAKEREEVKNEINIMNQLN-HVNLIQLYDAFESKTNLTLIM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 226 ELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSmLKVIDFGLSDFVRPDER 305
Cdd:cd14192  81 EYVDGGELFDRITDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNSTGNQ-IKIIDFGLARRYKPREK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 306 LNDIVGSAYYVAPEVLHRSYTT-EADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDFVK 384
Cdd:cd14192 160 LKVNFGTPEFLAPEVVNYDFVSfPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDAEAFENLSEEAKDFIS 239
                       250       260
                ....*....|....*....|..
gi 15230288 385 RLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14192 240 RLLVKEKSCRMSATQCLKHEWL 261
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
145-406 1.05e-51

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: 179.55  E-value: 1.05e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFgytcSAKFKKGELKD--QEVAVKVIPKSKMTS----AISIEDVRREVKILRALSgHQNLVQFYDAFEDN 218
Cdd:cd14096   4 RLINKIGEGAF----SNVYKAVPLRNtgKPVAIKVVRKADLSSdnlkGSSRANILKEVQIMKRLS-HPNIVKLLDFQESD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 219 ANVYIVMELCGGGELLDRILaRGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTS---------------- 282
Cdd:cd14096  79 EYYYIVLELADGGEIFHQIV-RLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEPipfipsivklrkaddd 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 283 --KEENS------------MLKVIDFGLSDFVRPDErLNDIVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRP 347
Cdd:cd14096 158 etKVDEGefipgvggggigIVKLADFGLSKQVWDSN-TKTPCGTVGYTAPEVVKdERYSKKVDMWALGCVLYTLLCGFPP 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15230288 348 FWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14096 237 FYDESIETLTEKISRGDYTFLSPWWDEISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
145-406 1.70e-51

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: 179.05  E-value: 1.70e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGyTCSAKFKKgeLKDQEVAVKVIPKSKmtsaisiEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIV 224
Cdd:cd14178   6 EIKEDIGIGSYS-VCKRCVHK--ATSTEYAVKIIDKSK-------RDPSEEIEILLRYGQHPNIITLKDVYDDGKFVYLV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGELLDRILaRGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEN-SMLKVIDFGLSDFVRPD 303
Cdd:cd14178  76 MELMRGGELLDRIL-RQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESGNpESIRICDFGFAKQLRAE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 E-RLNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPF-----------WARTESGIFravlkadpSFDEP 370
Cdd:cd14178 155 NgLLMTPCYTANFVAPEVLKRQgYDAACDIWSLGILLYTMLAGFTPFangpddtpeeiLARIGSGKY--------ALSGG 226
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15230288 371 PWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14178 227 NWDSISDAAKDIVSKMLHVDPHQRLTAPQVLRHPWI 262
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
146-406 3.16e-51

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: 177.03  E-value: 3.16e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 146 LGEEIGRGHFGytcsAKFKKGELKDQE-VAVKVIPKSKMTSAiSIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIV 224
Cdd:cd06627   4 LGDLIGRGAFG----SVYKGLNLNTGEfVAIKQISLEKIPKS-DLKSVMGEIDLLKKLN-HPNIVKYIGSVKTKDSLYII 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGELLDrILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLyTSKEENsmLKVIDFGLSDFV-RPD 303
Cdd:cd06627  78 LEYVENGSLAS-IIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANIL-TTKDGL--VKLADFGVATKLnEVE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ERLNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTE-SGIFRAVlkadpSFDEPPWPS-LSFEAK 380
Cdd:cd06627 154 KDENSVVGTPYWMAPEVIEMSgVTTASDIWSVGCTVIELLTGNPPYYDLQPmAALFRIV-----QDDHPPLPEnISPELR 228
                       250       260
                ....*....|....*....|....*.
gi 15230288 381 DFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd06627 229 DFLLQCFQKDPTLRPSAKELLKHPWL 254
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
145-406 3.32e-51

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: 179.83  E-value: 3.32e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGyTCSAKFKKGelKDQEVAVKVIPKSKmtsaisiEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIV 224
Cdd:cd14176  22 EVKEDIGVGSYS-VCKRCIHKA--TNMEFAVKIIDKSK-------RDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVV 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGELLDRILaRGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEN-SMLKVIDFGLSDFVRPD 303
Cdd:cd14176  92 TELMKGGELLDKIL-RQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNpESIRICDFGFAKQLRAE 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 E-RLNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPF-----------WARTESGIFravlkadpSFDEP 370
Cdd:cd14176 171 NgLLMTPCYTANFVAPEVLERQgYDAACDIWSLGVLLYTMLTGYTPFangpddtpeeiLARIGSGKF--------SLSGG 242
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15230288 371 PWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14176 243 YWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 278
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
150-406 4.68e-51

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: 176.43  E-value: 4.68e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTcsaKFKKGELKDQEVAVKVIPKSKMTSAiSIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd14071   8 IGKGNFAVV---KLARHRITKTEVAIKIIDKSQLDEE-NLKKIYREVQIMKMLN-HPHIIKLYQVMETKDMLYLVTEYAS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDrILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLSDFVRPDERLNDI 309
Cdd:cd14071  83 NGEIFD-YLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLL---DANMNIKIADFGFSNFFKPGELLKTW 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 310 VGSAYYVAPEVLH-RSYT-TEADVWSIGVIAYILLCGSRPF--------WARTESGIFRAvlkadPSFdeppwpsLSFEA 379
Cdd:cd14071 159 CGSPPYAAPEVFEgKEYEgPQLDIWSLGVVLYVLVCGALPFdgstlqtlRDRVLSGRFRI-----PFF-------MSTDC 226
                       250       260
                ....*....|....*....|....*..
gi 15230288 380 KDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14071 227 EHLIRRMLVLDPSKRLTIEQIKKHKWM 253
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
145-406 6.51e-51

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: 175.90  E-value: 6.51e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHfgyTCSAKFKKGELKDQEVAVKVIPKSKMTSAISIEDVRREVKILRaLSGHQNLVQFYDAFEDNANVYIV 224
Cdd:cd14081   4 RLGKTLGKGQ---TGLVKLAKHCVTGQKVAIKIVNKEKLSKESVLMKVEREIAIMK-LIEHPNVLKLYDVYENKKYLYLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsmLKVIDFGLSDFVRPDE 304
Cdd:cd14081  80 LEYVSGGELFDYLVKKG-RLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNN---IKIADFGMASLQPEGS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 305 RLNDIVGSAYYVAPEVL-HRSYT-TEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKAdpSFDEPpwPSLSFEAKDF 382
Cdd:cd14081 156 LLETSCGSPHYACPEVIkGEKYDgRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRG--VFHIP--HFISPDAQDL 231
                       250       260
                ....*....|....*....|....
gi 15230288 383 VKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14081 232 LRRMLEVNPEKRITIEEIKKHPWF 255
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
150-408 1.21e-50

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: 175.87  E-value: 1.21e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFG--YTCsakfKKGELKDQeVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMEL 227
Cdd:cd05579   1 ISRGAYGrvYLA----KKKSTGDL-YAIKVIKKRDMIRKNQVDSVLAERNILSQAQ-NPFVVKLYYSFQGKKNLYLVMEY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 228 CGGGELLdRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSDF-------- 299
Cdd:cd05579  75 LPGGDLY-SLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDA---NGHLKLTDFGLSKVglvrrqik 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 300 --------VRPDERLNDIVGSAYYVAPEV-LHRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEP 370
Cdd:cd05579 151 lsiqkksnGAPEKEDRRIVGTPDYLAPEIlLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEWPED 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15230288 371 pwPSLSFEAKDFVKRLLYKDPRKRMTA--SQALM-HPWIAG 408
Cdd:cd05579 231 --PEVSDEAKDLISKLLTPDPEKRLGAkgIEEIKnHPFFKG 269
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
148-406 1.60e-50

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: 175.49  E-value: 1.60e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKFKKGELKdqeVAVKVIPKSkmtSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMEL 227
Cdd:cd14190  10 EVLGGGKFGKVHTCTEKRTGLK---LAAKVINKQ---NSKDKEMVLLEIQVMNQLN-HRNLIQLYEAIETPNEIVLFMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 228 CGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENsMLKVIDFGLSDFVRPDERLN 307
Cdd:cd14190  83 VEGGELFERIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRTGH-QVKIIDFGLARRYNPREKLK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 308 DIVGSAYYVAPEVLHR---SYTTeaDVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDFVK 384
Cdd:cd14190 162 VNFGTPEFLSPEVVNYdqvSFPT--DMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMGNWYFDEETFEHVSDEAKDFVS 239
                       250       260
                ....*....|....*....|..
gi 15230288 385 RLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14190 240 NLIIKERSARMSATQCLKHPWL 261
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
145-406 2.15e-50

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: 174.94  E-value: 2.15e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGytcSAKFKKGELKDQEVAVKVIPK------SKMTSAISIEDVRREVKILR-----ALSGHQNLVQFYD 213
Cdd:cd14077   4 EFVKTIGAGSMG---KVKLAKHIRTGEKCAIKIIPRasnaglKKEREKRLEKEISRDIRTIReaalsSLLNHPHICRLRD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 214 AFEDNANVYIVMELCGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVID 293
Cdd:cd14077  81 FLRTPNHYYMLFEYVDGGQLLDYIISHG-KLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILIS---KSGNIKIID 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 294 FGLSDFVRPDERLNDIVGSAYYVAPEVLH-RSYT-TEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADpsFDEPP 371
Cdd:cd14077 157 FGLSNLYDPRRLLRTFCGSLYFAAPELLQaQPYTgPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGK--VEYPS 234
                       250       260       270
                ....*....|....*....|....*....|....*
gi 15230288 372 WpsLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14077 235 Y--LSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
146-405 2.79e-50

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: 174.44  E-value: 2.79e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 146 LGEEIGRGHFGYTCSAKFKKGELKdqeVAVKVIPKSKmTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVM 225
Cdd:cd14069   5 LVQTLGEGAFGEVFLAVNRNTEEA---VAVKFVDMKR-APGDCPENIKKEVCIQKMLS-HKNVVRFYGHRREGEFQYLFL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 226 ELCGGGELLDRILARGGkYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFVRPD-- 303
Cdd:cd14069  80 EYASGGELFDKIEPDVG-MPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLD---ENDNLKISDFGLATVFRYKgk 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ER-LNDIVGSAYYVAPEVLHRS--YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAK 380
Cdd:cd14069 156 ERlLNKMCGTLPYVAPELLAKKkyRAEPVDVWSCGIVLFAMLAGELPWDQPSDSCQEYSDWKENKKTYLTPWKKIDTAAL 235
                       250       260
                ....*....|....*....|....*
gi 15230288 381 DFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd14069 236 SLLRKILTENPNKRITIEDIKKHPW 260
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
148-406 3.87e-50

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: 174.04  E-value: 3.87e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTcsakFKKGELKDQEV-AVKVIpksKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVME 226
Cdd:cd14191   8 ERLGSGKFGQV----FRLVEKKTKKVwAGKFF---KAYSAKEKENIRQEISIMNCLH-HPKLVQCVDAFEEKANIVMVLE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 227 LCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeENSMLKVIDFGLSDFVRPDERL 306
Cdd:cd14191  80 MVSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNK-TGTKIKLIDFGLARRLENAGSL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 307 NDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDFVKR 385
Cdd:cd14191 159 KVLFGTPEFVAPEVInYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISN 238
                       250       260
                ....*....|....*....|.
gi 15230288 386 LLYKDPRKRMTASQALMHPWI 406
Cdd:cd14191 239 LLKKDMKARLTCTQCLQHPWL 259
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
193-406 1.56e-49

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: 172.87  E-value: 1.56e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 193 RREVKILRALSGHQNLVQFYDAFEdnaNVY-------IVMELCGGGELLDRILARGGK-YSEDDAKAVLIQILNVVAFCH 264
Cdd:cd14172  44 RREVEHHWRASGGPHIVHILDVYE---NMHhgkrcllIIMECMEGGELFSRIQERGDQaFTEREASEIMRDIGTAIQYLH 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 265 LQGVVHRDLKPENFLYTSKEENSMLKVIDFGLSDFVRPDERLNDIVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLC 343
Cdd:cd14172 121 SMNIAHRDVKPENLLYTSKEKDAVLKLTDFGFAKETTVQNALQTPCYTPYYVAPEVLGpEKYDKSCDMWSLGVIMYILLC 200
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15230288 344 GSRPFWART----ESGIFRAVLKADPSFDEPPWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14172 201 GFPPFYSNTgqaiSPGMKRRIRMGQYGFPNPEWAEVSEEAKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
137-406 5.75e-49

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: 171.27  E-value: 5.75e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 137 SKELQSRIEL--GEEIGRGHFgytcsAKFKKGELKD--QEVAVKVIPKSKMTSAISIEdVRREVKILRALSGHQNLVQFY 212
Cdd:cd14197   2 SEPFQERYSLspGRELGRGKF-----AVVRKCVEKDsgKEFAAKFMRKRRKGQDCRME-IIHEIAVLELAQANPWVINLH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 213 DAFEDNANVYIVMELCGGGELLDRILA-RGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKV 291
Cdd:cd14197  76 EVYETASEMILVLEYAAGGEIFNQCVAdREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPLGDIKI 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 292 IDFGLSDFVRPDERLNDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEP 370
Cdd:cd14197 156 VDFGLSRILKNSEELREIMGTPEYVAPEILsYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSEE 235
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15230288 371 PWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14197 236 EFEHLSESAIDFIKTLLIKKPENRATAEDCLKHPWL 271
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
142-411 1.09e-48

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: 170.47  E-value: 1.09e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 142 SRIELGEEIGRGHFGYTCSAKFKK-GELkdqeVAVKVIP---KSKMTSAIsiedvRREVKILRAlSGHQNLVQFYDAFED 217
Cdd:cd06623   1 SDLERVKVLGQGSSGVVYKVRHKPtGKI----YALKKIHvdgDEEFRKQL-----LRELKTLRS-CESPYVVKCYGAFYK 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 218 NANVYIVMELCGGGELlDRILARGGKYSEDDAKAVLIQILNVVAFCHLQ-GVVHRDLKPENFLYTSKEEnsmLKVIDFGL 296
Cdd:cd06623  71 EGEISIVLEYMDGGSL-ADLLKKVGKIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSKGE---VKIADFGI 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 297 SDFVRP-DERLNDIVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFrAVLKADPSFDEPPWPS 374
Cdd:cd06623 147 SKVLENtLDQCNTFVGTVTYMSPERIQgESYSYAADIWSLGLTLLECALGKFPFLPPGQPSFF-ELMQAICDGPPPSLPA 225
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 15230288 375 LSF--EAKDFVKRLLYKDPRKRMTASQALMHPWIAGYKK 411
Cdd:cd06623 226 EEFspEFRDFISACLQKDPKKRPSAAELLQHPFIKKADN 264
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
145-407 1.40e-47

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: 168.65  E-value: 1.40e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGyTCSAKFKKgeLKDQEVAVKVIPKSKmtsaisiEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIV 224
Cdd:cd14177   7 ELKEDIGVGSYS-VCKRCIHR--ATNMEFAVKIIDKSK-------RDPSEEIEILMRYGQHPNIITLKDVYDDGRYVYLV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGELLDRILaRGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENS-MLKVIDFGLSDFVRPD 303
Cdd:cd14177  77 TELMKGGELLDRIL-RQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSANAdSIRICDFGFAKQLRGE 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ERLndIVGSAY---YVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFW---ARTESGIFRAVLKADPSFDEPPWPSLS 376
Cdd:cd14177 156 NGL--LLTPCYtanFVAPEVLMRQgYDAACDIWSLGVLLYTMLAGYTPFAngpNDTPEEILLRIGSGKFSLSGGNWDTVS 233
                       250       260       270
                ....*....|....*....|....*....|.
gi 15230288 377 FEAKDFVKRLLYKDPRKRMTASQALMHPWIA 407
Cdd:cd14177 234 DAAKDLLSHMLHVDPHQRYTAEQVLKHSWIA 264
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
193-406 4.02e-47

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: 166.87  E-value: 4.02e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 193 RREVKILRALSGHQNLVQFYDAFEDN----------ANVYIVMELCGGGELLDRILARGGkYSEDDAKAVLIQILNVVAF 262
Cdd:cd14171  46 RTEVRLHMMCSGHPNIVQIYDVYANSvqfpgessprARLLIVMELMEGGELFDRISQHRH-FTEKQAAQYTKQIALAVQH 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 263 CHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGlsdFVRPDErlNDIVG---SAYYVAPEVL-----HR----------- 323
Cdd:cd14171 125 CHSLNIAHRDLKPENLLLKDNSEDAPIKLCDFG---FAKVDQ--GDLMTpqfTPYYVAPQVLeaqrrHRkersgiptspt 199
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 324 --SYTTEADVWSIGVIAYILLCGSRPFWARTES-----GIFRAVLKADPSFDEPPWPSLSFEAKDFVKRLLYKDPRKRMT 396
Cdd:cd14171 200 pyTYDKSCDMWSLGVIIYIMLCGYPPFYSEHPSrtitkDMKRKIMTGSYEFPEEEWSQISEMAKDIVRKLLCVDPEERMT 279
                       250
                ....*....|
gi 15230288 397 ASQALMHPWI 406
Cdd:cd14171 280 IEEVLHHPWL 289
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
171-406 6.87e-47

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: 166.36  E-value: 6.87e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 171 QEVAVKVIPKSkmtSAISIEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIVMELCGGGELLDRILARGgKYSEDDAK 250
Cdd:cd14174  28 KEYAVKIIEKN---AGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLRGGSILAHIQKRK-HFNEREAS 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 251 AVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLSDFVRPDERLNDIV--------GSAYYVAPEVLh 322
Cdd:cd14174 104 RVVRDIASALDFLHTKGIAHRDLKPENILCESPDKVSPVKICDFDLGSGVKLNSACTPITtpelttpcGSAEYMAPEVV- 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 323 RSYTTEA-------DVWSIGVIAYILLCGSRPF---------WARTE------SGIFRAVLKADPSFDEPPWPSLSFEAK 380
Cdd:cd14174 183 EVFTDEAtfydkrcDLWSLGVILYIMLSGYPPFvghcgtdcgWDRGEvcrvcqNKLFESIQEGKYEFPDKDWSHISSEAK 262
                       250       260
                ....*....|....*....|....*.
gi 15230288 381 DFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14174 263 DLISKLLVRDAKERLSAAQVLQHPWV 288
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
143-406 1.02e-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: 165.17  E-value: 1.02e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFG--YTCsAKFKKGELkdqeVAVKVIPKSKMTSAIsIEDVRREVKILRALSgHQNLVQFYDAFEDNAN 220
Cdd:cd06626   1 RWQRGNKIGEGTFGkvYTA-VNLDTGEL----MAMKEIRFQDNDPKT-IKEIADEMKVLEGLD-HPNLVRYYGVEVHREE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 VYIVMELCGGGELLDrILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLS--- 297
Cdd:cd06626  74 VYIFMEYCQEGTLEE-LLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDS---NGLIKLGDFGSAvkl 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 298 ---DFVRPDERLNDIVGSAYYVAPEVLHRSYTTE----ADVWSIGVIAYILLCGSRPfWARTESG---IFRAVLKADPSF 367
Cdd:cd06626 150 knnTTTMAPGEVNSLVGTPAYMAPEVITGNKGEGhgraADIWSLGCVVLEMATGKRP-WSELDNEwaiMYHVGMGHKPPI 228
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 15230288 368 dePPWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd06626 229 --PDSLQLSPEGKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
148-406 1.05e-46

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: 165.42  E-value: 1.05e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFG--YTCSAKFKKGELKDQEVAVKVIPKSKmtsaisiedVRREVKILRALSgHQNLVQFYDAFEDNANVYIVM 225
Cdd:cd14104   6 EELGRGQFGivHRCVETSSKKTYMAKFVKVKGADQVL---------VKKEISILNIAR-HRNILRLHESFESHEELVMIF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 226 ELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEeNSMLKVIDFGLSDFVRPDER 305
Cdd:cd14104  76 EFISGVDIFERITTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRR-GSYIKIIEFGQSRQLKPGDK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 306 LNDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDFVK 384
Cdd:cd14104 155 FRLQYTSAEFYAPEVHqHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDDEAFKNISIEALDFVD 234
                       250       260
                ....*....|....*....|..
gi 15230288 385 RLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14104 235 RLLVKERKSRMTAQEALNHPWL 256
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
144-426 1.06e-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: 165.83  E-value: 1.06e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 144 IELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYI 223
Cdd:cd05580   3 FEFLKTLGTGSFGRVRLVKHKD---SGKYYALKILKKAKIIKLKQVEHVLNEKRILSEVR-HPFIVNLLGSFQDDRNLYM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDRiLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSDFVrpD 303
Cdd:cd05580  79 VMEYVPGGELFSL-LRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDS---DGHIKITDFGFAKRV--K 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ERLNDIVGSAYYVAPEV-LHRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFdePPWpsLSFEAKDF 382
Cdd:cd05580 153 DRTYTLCGTPEYLAPEIiLSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRF--PSF--FDPDAKDL 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 15230288 383 VKRLLYKDPRKRMTA----SQALM-HPWIAGykkidIPFDILIFKQIKA 426
Cdd:cd05580 229 IKRLLVVDLTKRLGNlkngVEDIKnHPWFAG-----IDWDALLQRKIPA 272
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
171-408 1.24e-46

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: 166.20  E-value: 1.24e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 171 QEVAVKVIPKsKMTsaisiEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIVMELCGGGELLDRIlARGGKYSEDDAK 250
Cdd:cd14180  32 QEYAVKIISR-RME-----ANTQREVAALRLCQSHPNIVALHEVLHDQYHTYLVMELLRGGELLDRI-KKKARFSESEAS 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 251 AVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLSD-FVRPDERLNDIVGSAYYVAPEVLHRS-YTTE 328
Cdd:cd14180 105 QLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDGAVLKVIDFGFARlRPQGSRPLQTPCFTLQYAAPELFSNQgYDES 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 329 ADVWSIGVIAYILLCGSRPFWARTESG-------IFRAVLKADPSFDEPPWPSLSFEAKDFVKRLLYKDPRKRMTASQAL 401
Cdd:cd14180 185 CDLWSLGVILYTMLSGQVPFQSKRGKMfhnhaadIMHKIKEGDFSLEGEAWKGVSEEAKDLVRGLLTVDPAKRLKLSELR 264

                ....*..
gi 15230288 402 MHPWIAG 408
Cdd:cd14180 265 ESDWLQG 271
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
157-406 1.56e-46

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: 164.81  E-value: 1.56e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 157 YTCSAKFKKGELKDQEVAvkvipkskmtsaisiedvRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELCGGGELLDR 236
Cdd:cd14088  29 YTCKKFLKRDGRKVRKAA------------------KNEINILKMVK-HPNILQLVDVFETRKEYFIFLELATGREVFDW 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 237 ILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLSDFvrPDERLNDIVGSAYYV 316
Cdd:cd14088  90 ILDQG-YYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYNRLKNSKIVISDFHLAKL--ENGLIKEPCGTPEYL 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 317 APEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTES--------GIFRAVLKADPSFDEPPWPSLSFEAKDFVKRLL 387
Cdd:cd14088 167 APEVVGRQrYGRPVDCWAIGVIMYILLSGNPPFYDEAEEddyenhdkNLFRKILAGDYEFDSPYWDDISQAAKDLVTRLM 246
                       250
                ....*....|....*....
gi 15230288 388 YKDPRKRMTASQALMHPWI 406
Cdd:cd14088 247 EVEQDQRITAEEAISHEWI 265
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
146-406 1.92e-46

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: 164.05  E-value: 1.92e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 146 LGEEIGRGHFgytcsAKFKKG--ELKDQEVAVKVIPKSKMtSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYI 223
Cdd:cd14075   6 IRGELGSGNF-----SQVKLGihQLTKEKVAIKILDKTKL-DQKTQRLLSREISSMEKLH-HPNIIRLYEVVETLSKLHL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDRILaRGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSDFVRPD 303
Cdd:cd14075  79 VMEYASGGELYTKIS-TEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYAS---NNCVKVGDFGFSTHAKRG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ERLNDIVGSAYYVAPEVLH-RSYTTE-ADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFdePPWpsLSFEAKD 381
Cdd:cd14075 155 ETLNTFCGSPPYAAPELFKdEHYIGIyVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTYTI--PSY--VSEPCQE 230
                       250       260
                ....*....|....*....|....*
gi 15230288 382 FVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14075 231 LIRGILQPVPSDRYSIDEIKNSEWL 255
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
141-405 3.05e-46

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: 163.52  E-value: 3.05e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 141 QSRIELGEEIGRGHFGYTcsakfKKGELKDQEV--AVKVIPKSKMTSAisieDVRREVKILRALSgHQNLVQFYDAFEDN 218
Cdd:cd14107   1 HSVYEVKEEIGRGTFGFV-----KRVTHKGNGEccAAKFIPLRSSTRA----RAFQERDILARLS-HRRLTCLLDQFETR 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 219 ANVYIVMELCGGGELLDRiLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSmLKVIDFGLSD 298
Cdd:cd14107  71 KTLILILELCSSEELLDR-LFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTRED-IKICDFGFAQ 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 299 FVRPDERLNDIVGSAYYVAPEVLHRSYTTEA-DVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSF 377
Cdd:cd14107 149 EITPSEHQFSKYGSPEFVAPEIVHQEPVSAAtDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVSWDTPEITHLSE 228
                       250       260
                ....*....|....*....|....*...
gi 15230288 378 EAKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd14107 229 DAKDFIKRVLQPDPEKRPSASECLSHEW 256
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
150-406 4.14e-46

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 163.20  E-value: 4.14e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKGElkdQEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd05578   8 IGKGSFGKVCIVQKKDTK---KMFAMKYMNKQKCIEKDSVRNVLNELEILQELE-HPFLVNLWYSFQDEEDMYMVVDLLL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELldRI-LARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLSDFVRPDERLND 308
Cdd:cd05578  84 GGDL--RYhLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILL---DEQGHVHITDFNIATKLTDGTLATS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 309 IVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWART---ESGIFRAVLKADPSFdeppWPSLSFEAKDFVK 384
Cdd:cd05578 159 TSGTKPYMAPEVFMRAgYSFAVDWWSLGVTAYEMLRGKRPYEIHSrtsIEEIRAKFETASVLY----PAGWSEEAIDLIN 234
                       250       260
                ....*....|....*....|...
gi 15230288 385 RLLYKDPRKRMTASQALM-HPWI 406
Cdd:cd05578 235 KLLERDPQKRLGDLSDLKnHPYF 257
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
143-406 5.76e-46

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: 162.69  E-value: 5.76e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFGytcSAKFKKGELKDQEVAVKVIPKSKMTSAiSIEDVRREVKILRALSgHQNLVQFYDAFEDNANVY 222
Cdd:cd14072   1 NYRLLKTIGKGNFA---KVKLARHVLTGREVAIKIIDKTQLNPS-SLQKLFREVRIMKILN-HPNIVKLFEVIETEKTLY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 223 IVMELCGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtSKEENsmLKVIDFGLSDFVRP 302
Cdd:cd14072  76 LVMEYASGGEVFDYLVAHG-RMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLL-DADMN--IKIADFGFSNEFTP 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 303 DERLNDIVGSAYYVAPEVLH-RSYT-TEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKAD---PSFdeppwpsLSF 377
Cdd:cd14072 152 GNKLDTFCGSPPYAAPELFQgKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKyriPFY-------MST 224
                       250       260
                ....*....|....*....|....*....
gi 15230288 378 EAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14072 225 DCENLLKKFLVLNPSKRGTLEQIMKDRWM 253
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
147-405 1.14e-45

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: 162.77  E-value: 1.14e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 147 GEEIGRGHFGYTCSAKFKKGelkDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVME 226
Cdd:cd05581   6 GKPLGEGSYSTVVLAKEKET---GKEYAIKVLDKRHIIKEKKVKYVTIEKEVLSRLA-HPGIVKLYYTFQDESKLYFVLE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 227 LCGGGELLDRILaRGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFVRPDE-- 304
Cdd:cd05581  82 YAPNGDLLEYIR-KYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLD---EDMHIKITDFGTAKVLGPDSsp 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 305 ----------------RLNDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSF 367
Cdd:cd05581 158 estkgdadsqiaynqaRAASFVGTAEYVSPELLnEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYEF 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15230288 368 DEPPWPslsfEAKDFVKRLLYKDPRKRMTAS-----QALM-HPW 405
Cdd:cd05581 238 PENFPP----DAKDLIQKLLVLDPSKRLGVNenggyDELKaHPF 277
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
140-406 1.60e-45

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: 161.66  E-value: 1.60e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 140 LQSRIELGEEIGRGHFGYTCSAKFKKGelkdQEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNA 219
Cdd:cd14161   1 LKHRYEFLETLGKGTYGRVKKARDSSG----RLVAIKSIRKDRIKDEQDLLHIRREIEIMSSLN-HPHIISVYEVFENSS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 220 NVYIVMELCGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLSDF 299
Cdd:cd14161  76 KIVIVMEYASRGDLYDYISERQ-RLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILL---DANGNIKIADFGLSNL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 300 VRPDERLNDIVGSAYYVAPEVLH-RSYT-TEADVWSIGVIAYILLCGSRPFWARTESGIFRAVlkADPSFDEPPWPSlsf 377
Cdd:cd14161 152 YNQDKFLQTYCGSPLYASPEIVNgRPYIgPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQI--SSGAYREPTKPS--- 226
                       250       260
                ....*....|....*....|....*....
gi 15230288 378 EAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14161 227 DACGLIRWLLMVNPERRATLEDVASHWWV 255
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
145-406 4.98e-45

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: 160.51  E-value: 4.98e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKKGELKdqeVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIV 224
Cdd:cd14116   8 EIGRPLGKGKFGNVYLAREKQSKFI---LALKVLFKAQLEKAGVEHQLRREVEIQSHLR-HPNILRLYGYFHDATRVYLI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGELLdRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSDFVrPDE 304
Cdd:cd14116  84 LEYAPLGTVY-RELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGS---AGELKIADFGWSVHA-PSS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 305 RLNDIVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADpsFDEPPWpsLSFEAKDFV 383
Cdd:cd14116 159 RRTTLCGTLDYLPPEMIEgRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVE--FTFPDF--VTEGARDLI 234
                       250       260
                ....*....|....*....|...
gi 15230288 384 KRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14116 235 SRLLKHNPSQRPMLREVLEHPWI 257
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
150-348 7.20e-45

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: 159.63  E-value: 7.20e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGytcsaKFKKGELKDQEVAVKVIPKSKMTSAIsIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd13999   1 IGSGSFG-----EVYKGKWRGTDVAIKKLKVEDDNDEL-LKEFRREVSILSKLR-HPNIVQFIGACLSPPPLCIVTEYMP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLS-DFVRPDERLND 308
Cdd:cd13999  74 GGSLYDLLHKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLD---ENFTVKIADFGLSrIKNSTTEKMTG 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 15230288 309 IVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPF 348
Cdd:cd13999 151 VVGTPRWMAPEVLrGEPYTEKADVYSFGIVLWELLTGEVPF 191
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
145-405 8.21e-45

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: 160.39  E-value: 8.21e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFK-KGELkdqeVAVKVIpKSKMTSaisIEDVR--REVKILRALSGHQNLVQFYDAFEDNANV 221
Cdd:cd07830   2 KVIKQLGDGTFGSVYLARNKeTGEL----VAIKKM-KKKFYS---WEECMnlREVKSLRKLNEHPNIVKLKEVFRENDEL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 YIVMELCGGgELLDRILARGGKY-SEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEensMLKVIDFGLSDFV 300
Cdd:cd07830  74 YFVFEYMEG-NLYQLMKDRKGKPfSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPE---VVKIADFGLAREI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 301 RPDERLNDIVGSAYYVAPEVL--HRSYTTEADVWSIGVIA---YILlcgsRP-FWARTESG-IFR--AVLKadpSFDEPP 371
Cdd:cd07830 150 RSRPPYTDYVSTRWYRAPEILlrSTSYSSPVDIWALGCIMaelYTL----RPlFPGSSEIDqLYKicSVLG---TPTKQD 222
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 372 WP-------SLSF-------------------EAKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd07830 223 WPegyklasKLGFrfpqfaptslhqlipnaspEAIDLIKDMLRWDPKKRPTASQALQHPY 282
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
150-406 8.79e-45

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


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 159.32  E-value: 8.79e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKgelKDQEVAVKVI-PKSKMTSAIsiedvRREVKILRALS---GHQNLVQFYDAFEDNA--NVYI 223
Cdd:cd05118   7 IGEGAFGTVWLARDKV---TGEKVAIKKIkNDFRHPKAA-----LREIKLLKHLNdveGHPNIVKLLDVFEHRGgnHLCL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGgELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtsKEENSMLKVIDFGLSDFVRPD 303
Cdd:cd05118  79 VFELMGM-NLYELIKDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILI--NLELGQLKLADFGLARSFTSP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ErLNDIVGSAYYVAPEVLHRS--YTTEADVWSIGVIAYILLCGsRPFWARTESG--IFRAVLKADPSfdeppwpslsfEA 379
Cdd:cd05118 156 P-YTPYVATRWYRAPEVLLGAkpYGSSIDIWSLGCILAELLTG-RPLFPGDSEVdqLAKIVRLLGTP-----------EA 222
                       250       260
                ....*....|....*....|....*..
gi 15230288 380 KDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd05118 223 LDLLSKMLKYDPAKRITASQALAHPYF 249
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
143-401 3.21e-44

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: 158.28  E-value: 3.21e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKS----KMTSAISIEDVRREVKILRALSGHQNLVQFYDAFEDN 218
Cdd:cd13993   1 RYQLISPIGEGAYGVVYLAVDLR---TGRKYAIKCLYKSgpnsKDGNDFQKLPQLREIDLHRRVSRHPNIITLHDVFETE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 219 ANVYIVMELCGGGELLDRILARG-GKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENsmLKVIDFGLS 297
Cdd:cd13993  78 VAIYIVLEYCPNGDLFEAITENRiYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEGT--VKLCDFGLA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 298 dfVRPDERLNDIVGSAYYVAPEVL------HRSYTTEA-DVWSIGVIAYILLCGSRPF-WARTESGIFRAVLKADPS-FD 368
Cdd:cd13993 156 --TTEKISMDFGVGSEFYMAPECFdevgrsLKGYPCAAgDIWSLGIILLNLTFGRNPWkIASESDPIFYDYYLNSPNlFD 233
                       250       260       270
                ....*....|....*....|....*....|...
gi 15230288 369 EppWPSLSFEAKDFVKRLLYKDPRKRMTASQAL 401
Cdd:cd13993 234 V--ILPMSDDFYNLLRQIFTVNPNNRILLPELQ 264
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
148-405 3.77e-44

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: 157.84  E-value: 3.77e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKFKKGelKDQEVAVKVIPKSKMTSAiSIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMEL 227
Cdd:cd14121   1 EKLGSGTYATVYKAYRKSG--AREVVAVKCVSKSSLNKA-STENLLTEIELLKKLK-HPHIVELKDFQWDEEHIYLIMEY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 228 CGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEeNSMLKVIDFGLSDFVRPDERLN 307
Cdd:cd14121  77 CSGGDLSRFIRSRR-TLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRY-NPVLKLADFGFAQHLKPNDEAH 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 308 DIVGSAYYVAPE-VLHRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPsFDEPPWPSLSFEAKDFVKRL 386
Cdd:cd14121 155 SLRGSPLYMAPEmILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSKP-IEIPTRPELSADCRDLLLRL 233
                       250
                ....*....|....*....
gi 15230288 387 LYKDPRKRMTASQALMHPW 405
Cdd:cd14121 234 LQRDPDRRISFEEFFAHPF 252
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
193-415 3.90e-44

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: 159.43  E-value: 3.90e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 193 RREVKILRALSGHQNLVQFYDAFEdnaNVY-------IVMELCGGGELLDRILARGGK-YSEDDAKAVLIQILNVVAFCH 264
Cdd:cd14170  42 RREVELHWRASQCPHIVRIVDVYE---NLYagrkcllIVMECLDGGELFSRIQDRGDQaFTEREASEIMKSIGEAIQYLH 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 265 LQGVVHRDLKPENFLYTSKEENSMLKVIDFGLSDFVRPDERLNDIVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLC 343
Cdd:cd14170 119 SINIAHRDVKPENLLYTSKRPNAILKLTDFGFAKETTSHNSLTTPCYTPYYVAPEVLGpEKYDKSCDMWSLGVIMYILLC 198
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15230288 344 GSRPFWAR----TESGIFRAVLKADPSFDEPPWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWIAgyKKIDIP 415
Cdd:cd14170 199 GYPPFYSNhglaISPGMKTRIRMGQYEFPNPEWSEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIM--QSTKVP 272
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
145-406 4.03e-44

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: 159.24  E-value: 4.03e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFG--YTCSakfkKGElKDQEVAVKVIPKSKMTSA--ISIEDVRREVKILRALSgHQNLVQFYDAFEDNAN 220
Cdd:cd14094   6 ELCEVIGKGPFSvvRRCI----HRE-TGQQFAVKIVDVAKFTSSpgLSTEDLKREASICHMLK-HPHIVELLETYSSDGM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 VYIVMELCGGGELLDRILAR---GGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLS 297
Cdd:cd14094  80 LYMVFEFMDGADLCFEIVKRadaGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 298 dfvrpdERLNDI-------VGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTESgIFRAVLKADPSFDE 369
Cdd:cd14094 160 ------IQLGESglvaggrVGTPHFMAPEVVKREpYGKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYKMNP 232
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 15230288 370 PPWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14094 233 RQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWI 269
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
140-406 4.14e-44

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: 158.23  E-value: 4.14e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 140 LQSRIELGEEIGRGHFG--YTCSAKFKkgelkDQEVAVKVIPKSKMTSAISIedVRREVKILRALSgHQNLVQFYDAFED 217
Cdd:cd14183   4 ISERYKVGRTIGDGNFAvvKECVERST-----GREYALKIINKSKCRGKEHM--IQNEVSILRRVK-HPNIVLLIEEMDM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 218 NANVYIVMELCGGGELLDRILArGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFL-YTSKEENSMLKVIDFGL 296
Cdd:cd14183  76 PTELYLVMELVKGGDLFDAITS-TNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLvYEHQDGSKSLKLGDFGL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 297 SDFVrpDERLNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTE--SGIFRAVLKADPSFDEPPWP 373
Cdd:cd14183 155 ATVV--DGPLYTVCGTPTYVAPEIIAETgYGLKVDIWAAGVITYILLCGFPPFRGSGDdqEVLFDQILMGQVDFPSPYWD 232
                       250       260       270
                ....*....|....*....|....*....|...
gi 15230288 374 SLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14183 233 NVSDSAKELITMMLQVDVDQRYSALQVLEHPWV 265
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
146-406 6.62e-44

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: 157.64  E-value: 6.62e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 146 LGEEIGRGHFGYTCSAKFKKgeLKdQEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFE-DNANVYIV 224
Cdd:cd14165   5 LGINLGEGSYAKVKSAYSER--LK-CNVAIKIIDKKKAPDDFVEKFLPRELEILARLN-HKSIIKTYEIFEtSDGKVYIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGELLdRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLSDFVRPDE 304
Cdd:cd14165  81 MELGVQGDLL-EFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLL---DKDFNIKLTDFGFSKRCLRDE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 305 RLNDIV-----GSAYYVAPEVL-HRSYTTEA-DVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFdePPWPSLSF 377
Cdd:cd14165 157 NGRIVLsktfcGSAAYAAPEVLqGIPYDPRIyDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRF--PRSKNLTS 234
                       250       260
                ....*....|....*....|....*....
gi 15230288 378 EAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14165 235 ECKDLIYRLLQPDVSQRLCIDEVLSHPWL 263
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
143-405 9.96e-44

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: 156.73  E-value: 9.96e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIedVRREVKILRALSgHQNLVQFYDAFEDNANVY 222
Cdd:cd14184   2 KYKIGKVIGDGNFAVVKECVERS---TGKEFALKIIDKAKCCGKEHL--IENEVSILRRVK-HPNIIMLIEEMDTPAELY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 223 IVMELCGGGELLDRILArGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSM-LKVIDFGLSDFVr 301
Cdd:cd14184  76 LVMELVKGGDLFDAITS-STKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEYPDGTKsLKLGDFGLATVV- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 302 pDERLNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFwaRTESG----IFRAVLKADPSFDEPPWPSLS 376
Cdd:cd14184 154 -EGPLYTVCGTPTYVAPEIIAETgYGLKVDIWAAGVITYILLCGFPPF--RSENNlqedLFDQILLGKLEFPSPYWDNIT 230
                       250       260
                ....*....|....*....|....*....
gi 15230288 377 FEAKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd14184 231 DSAKELISHMLQVNVEARYTAEQILSHPW 259
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
148-406 1.91e-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: 156.87  E-value: 1.91e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIEDVRrEVKILRALSgHQNLVQFYDAFEDNANVYIVMEL 227
Cdd:cd07829   5 EKLGEGTYGVVYKAKDKK---TGEIVALKKIRLDNEEEGIPSTALR-EISLLKELK-HPNIVKLLDVIHTENKLYLVFEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 228 CgggE-----LLDRilaRGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLS-DFVR 301
Cdd:cd07829  80 C---DqdlkkYLDK---RPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINR---DGVLKLADFGLArAFGI 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 302 PDERLNDIVGSAYYVAPEVL--HRSYTTEADVWSIGVIAYILLCGSRPFWARTESG----IFR-------------AVLK 362
Cdd:cd07829 151 PLRTYTHEVVTLWYRAPEILlgSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIDqlfkIFQilgtpteeswpgvTKLP 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 15230288 363 AD----PSFDEPPW----PSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd07829 231 DYkptfPKWPKNDLekvlPRLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
168-406 3.65e-43

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: 156.34  E-value: 3.65e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 168 LKDQEVAVKVIPKSKMTSAisiEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIVMELCGGGELLDRILARGgKYSED 247
Cdd:cd14173  25 ITNKEYAVKIIEKRPGHSR---SRVFREVEMLYQCQGHRNVLELIEFFEEEDKFYLVFEKMRGGSILSHIHRRR-HFNEL 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 248 DAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLSDFVRPDERLNDI--------VGSAYYVAPE 319
Cdd:cd14173 101 EASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVSPVKICDFDLGSGIKLNSDCSPIstpelltpCGSAEYMAPE 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 320 VLHrSYTTEA-------DVWSIGVIAYILLCGSRPF---------WARTE------SGIFRAVLKADPSFDEPPWPSLSF 377
Cdd:cd14173 181 VVE-AFNEEAsiydkrcDLWSLGVILYIMLSGYPPFvgrcgsdcgWDRGEacpacqNMLFESIQEGKYEFPEKDWAHISC 259
                       250       260
                ....*....|....*....|....*....
gi 15230288 378 EAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14173 260 AAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
144-405 4.68e-43

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: 155.15  E-value: 4.68e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 144 IELGEEIGRGHFGYTCSAKFKKGELKdqeVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYI 223
Cdd:cd14162   2 YIVGKTLGHGSYAVVKKAYSTKHKCK---VAIKIVSKKKAPEDYLQKFLPREIEVIKGLK-HPNLICFYEAIETTSRVYI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDRILARGGkYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGlsdFVRPD 303
Cdd:cd14162  78 IMELAENGDLLDYIRKNGA-LPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLL---DKNNNLKITDFG---FARGV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ERLNDI--------VGSAYYVAPEVLhRS--YT-TEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKaDPSFdePPW 372
Cdd:cd14162 151 MKTKDGkpklsetyCGSYAYASPEIL-RGipYDpFLSDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQVQR-RVVF--PKN 226
                       250       260       270
                ....*....|....*....|....*....|...
gi 15230288 373 PSLSFEAKDFVKRLLYKDPrKRMTASQALMHPW 405
Cdd:cd14162 227 PTVSEECKDLILRMLSPVK-KRITIEEIKRDPW 258
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
145-406 5.56e-43

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 154.72  E-value: 5.56e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGytcsaKFKKGELKD--QEVAVKVIPKsKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVY 222
Cdd:cd14002   4 HVLELIGEGSFG-----KVYKGRRKYtgQVVALKFIPK-RGKSEKELRNLRQEIEILRKLN-HPNIIEMLDSFETKKEFV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 223 IVMELcGGGELLdRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGlsdFVRP 302
Cdd:cd14002  77 VVTEY-AQGELF-QILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGK---GGVVKLCDFG---FARA 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 303 DER----LNDIVGSAYYVAPE-VLHRSYTTEADVWSIGVIAYILLCGSRPFWArteSGIFRAV--LKADPSfdepPWPS- 374
Cdd:cd14002 149 MSCntlvLTSIKGTPLYMAPElVQEQPYDHTADLWSLGCILYELFVGQPPFYT---NSIYQLVqmIVKDPV----KWPSn 221
                       250       260       270
                ....*....|....*....|....*....|..
gi 15230288 375 LSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14002 222 MSPEFKSFLQGLLNKDPSKRLSWPDLLEHPFV 253
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
150-409 9.07e-43

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: 154.31  E-value: 9.07e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFG--YTCSAKFKkgelkDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMEL 227
Cdd:cd05572   1 LGVGGFGrvELVQLKSK-----GRTFALKCVKKRHIVQTRQQEHIFSEKEILEECN-SPFIVKLYRTFKDKKYLYMLMEY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 228 CGGGELLDrILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSDFVRPDERLN 307
Cdd:cd05572  75 CLGGELWT-ILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDS---NGYVKLVDFGFAKKLGSGRKTW 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 308 DIVGSAYYVAPEV-LHRSYTTEADVWSIGVIAYILLCGSRPFwarTESG-----IFRAVLKADPSFDEPPWpsLSFEAKD 381
Cdd:cd05572 151 TFCGTPEYVAPEIiLNKGYDFSVDYWSLGILLYELLTGRPPF---GGDDedpmkIYNIILKGIDKIEFPKY--IDKNAKN 225
                       250       260       270
                ....*....|....*....|....*....|...
gi 15230288 382 FVKRLLYKDPRKRMTASQALM-----HPWIAGY 409
Cdd:cd05572 226 LIKQLLRRNPEERLGYLKGGIrdikkHKWFEGF 258
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
142-413 1.65e-42

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: 156.29  E-value: 1.65e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 142 SRIELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSGhQNLVQFYDAFEDNANV 221
Cdd:cd05573   1 DDFEVIKVIGRGAFGEVWLVRDKD---TGQVYAMKILRKSDMLKREQIAHVRAERDILADADS-PWIVRLHYAFQDEDHL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 YIVMELCGGGELLdRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGLS---- 297
Cdd:cd05573  77 YLVMEYMPGGDLM-NLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDAD---GHIKLADFGLCtkmn 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 298 -----DFVRPDERL---------------------NDIVGSAYYVAPEVLHR-SYTTEADVWSIGVIAYILLCGSRPFWA 350
Cdd:cd05573 153 ksgdrESYLNDSVNtlfqdnvlarrrphkqrrvraYSAVGTPDYIAPEVLRGtGYGPECDWWSLGVILYEMLYGFPPFYS 232
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15230288 351 RTESGIFRAVLKADPSFDEPPWPSLSFEAKDFVKRLLyKDPRKRMTASQALM-HPWiagYKKID 413
Cdd:cd05573 233 DSLVETYSKIMNWKESLVFPDDPDVSPEAIDLIRRLL-CDPEDRLGSAEEIKaHPF---FKGID 292
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
142-414 2.41e-42

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: 153.55  E-value: 2.41e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 142 SRIELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIpksKMTSAIS-IEDVRREVKILRALSGhQNLVQFYDAFEDNAN 220
Cdd:cd06609   1 ELFTLLERIGKGSFGEVYKGIDKR---TNQVVAIKVI---DLEEAEDeIEDIQQEIQFLSQCDS-PYITKYYGSFLKGSK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 VYIVMELCGGGELLDriLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLS-DF 299
Cdd:cd06609  74 LWIIMEYCGGGSVLD--LLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLS---EEGDVKLADFGVSgQL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 300 VRPDERLNDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFwarteSGI--FRAVL---KADPsfdeppwP 373
Cdd:cd06609 149 TSTMSKRNTFVGTPFWMAPEVIkQSGYDEKADIWSLGITAIELAKGEPPL-----SDLhpMRVLFlipKNNP-------P 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 15230288 374 SL-----SFEAKDFVKRLLYKDPRKRMTASQALMHPWIAGYKKIDI 414
Cdd:cd06609 217 SLegnkfSKPFKDFVELCLNKDPKERPSAKELLKHKFIKKAKKTSY 262
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
145-405 2.62e-42

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: 152.78  E-value: 2.62e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKKGELKdqeVAVKVIPKSKMTSAISIEDVRR---EVKILRALS--GHQNLVQFYDAFEDNA 219
Cdd:cd14005   3 EVGDLLGKGGFGTVYSGVRIRDGLP---VAVKFVPKSRVTEWAMINGPVPvplEIALLLKASkpGVPGVIRLLDWYERPD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 220 NVYIVMELCGGGE-LLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeeNSMLKVIDFGLSD 298
Cdd:cd14005  80 GFLLIMERPEPCQdLFDFITERG-ALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLR--TGEVKLIDFGCGA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 299 FVRpDERLNDIVGSAYYVAPE-VLHRSY-TTEADVWSIGVIAYILLCGSRPFwARTESGIFRAVLKadpsfdeppWPSLS 376
Cdd:cd14005 157 LLK-DSVYTDFDGTRVYSPPEwIRHGRYhGRPATVWSLGILLYDMLCGDIPF-ENDEQILRGNVLF---------RPRLS 225
                       250       260
                ....*....|....*....|....*....
gi 15230288 377 FEAKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd14005 226 KECCDLISRCLQFDPSKRPSLEQILSHPW 254
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
145-406 3.59e-42

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: 152.71  E-value: 3.59e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIV 224
Cdd:cd14186   4 KVLNLLGKGSFACVYRARSLH---TGLEVAIKMIDKKAMQKAGMVQRVRNEVEIHCQLK-HPSILELYNYFEDSNYVYLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGL-SDFVRPD 303
Cdd:cd14186  80 LEMCHNGEMSRYLKNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTR---NMNIKIADFGLaTQLKMPH 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ERLNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKAD---PSFdeppwpsLSFEA 379
Cdd:cd14186 157 EKHFTMCGTPNYISPEIATRSaHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADyemPAF-------LSREA 229
                       250       260
                ....*....|....*....|....*..
gi 15230288 380 KDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14186 230 QDLIHQLLRKNPADRLSLSSVLDHPFM 256
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
150-406 5.60e-42

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: 152.08  E-value: 5.60e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYT--CSAKFKKGELKdqeVAVKVIPKSKMTSAIS--IEDVRREVKILRALSgHQNLVQFYDAFEDNANVY-IV 224
Cdd:cd13994   1 IGKGATSVVriVTKKNPRSGVL---YAVKEYRRRDDESKRKdyVKRLTSEYIISSKLH-HPNIVKVLDLCQDLHGKWcLV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGELLDRIlARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSD-FVRPD 303
Cdd:cd13994  77 MEYCPGGDLFTLI-EKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLD---EDGVLKLTDFGTAEvFGMPA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ERL----NDIVGSAYYVAPEVLHR-SYTTEA-DVWSIGVIAYILLCGSRPF-WARTESGIFRAVLKADPSFDEPPWPSLS 376
Cdd:cd13994 153 EKEspmsAGLCGSEPYMAPEVFTSgSYDGRAvDVWSCGIVLFALFTGRFPWrSAKKSDSAYKAYEKSGDFTNGPYEPIEN 232
                       250       260       270
                ....*....|....*....|....*....|...
gi 15230288 377 F---EAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd13994 233 LlpsECRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
150-404 1.10e-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: 150.98  E-value: 1.10e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKGElkDQEVAVKVIPKSKMTSAISIedVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd14120   1 IGHGAFAVVFKGRHRKKP--DLPVAIKCITKKNLSKSQNL--LGKEIKILKELS-HENVVALLDCQETSSSVYLVMEYCN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRILARgGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFL----YTSKEENS--MLKVIDFGLSDFVRPD 303
Cdd:cd14120  76 GGDLADYLQAK-GTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILlshnSGRKPSPNdiRLKIADFGFARFLQDG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ERLNDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKA---DPSFdePPWPSLsfEA 379
Cdd:cd14120 155 MMAATLCGSPMYMAPEVImSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQELKAFYEKNanlRPNI--PSGTSP--AL 230
                       250       260
                ....*....|....*....|....*
gi 15230288 380 KDFVKRLLYKDPRKRMTASQALMHP 404
Cdd:cd14120 231 KDLLLGLLKRNPKDRIDFEDFFSHP 255
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
194-406 1.32e-41

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: 151.12  E-value: 1.32e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 194 REVKILRALSgHQNLVQFYDAFEDNA-NVYIVMELCGGGELL-DRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHR 271
Cdd:cd14109  45 REVDIHNSLD-HPNIVQMHDAYDDEKlAVTVIDNLASTIELVrDNLLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHL 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 272 DLKPENFLYtskeENSMLKVIDFGLSDFVRPDERLNDIVGSAYYVAPEVLHRSYTTEA-DVWSIGVIAYILLCGSRPFWA 350
Cdd:cd14109 124 DLRPEDILL----QDDKLKLADFGQSRRLLRGKLTTLIYGSPEFVSPEIVNSYPVTLAtDMWSVGVLTYVLLGGISPFLG 199
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15230288 351 RTESGIFRAVLKADPSFDEPPWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14109 200 DNDRETLTNVRSGKWSFDSSPLGNISDDARDFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
148-405 1.42e-41

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: 150.82  E-value: 1.42e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKFKKgelKDQEVAVKVIP--KSKMTSAisiedvRREVKILRALSgHQNLVQFYDAFEDNANVYIVM 225
Cdd:cd14108   8 KEIGRGAFSYLRRVKEKS---SDLSFAAKFIPvrAKKKTSA------RRELALLAELD-HKSIVRFHDAFEKRRVVIIVT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 226 ELCgGGELLDRILARgGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSmLKVIDFGLSDFVRPDER 305
Cdd:cd14108  78 ELC-HEELLERITKR-PTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTDQ-VRICDFGNAQELTPNEP 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 306 LNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDFVK 384
Cdd:cd14108 155 QYCKYGTPEFVAPEIVNQSpVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYNVAFEESMFKDLCREAKGFII 234
                       250       260
                ....*....|....*....|.
gi 15230288 385 RLLYKDpRKRMTASQALMHPW 405
Cdd:cd14108 235 KVLVSD-RLRPDAEETLEHPW 254
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
148-406 1.49e-41

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: 151.00  E-value: 1.49e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIED-----VRREVKILRAL--SGHQNLVQFYDAFEDNAN 220
Cdd:cd14004   6 KEMGEGAYGQVNLAIYKS---KGKEVVIKFIFKERILVDTWVRDrklgtVPLEIHILDTLnkRSHPNIVKLLDFFEDDEF 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 VYIVMELCGGG-ELLDRILARGGkYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLSDF 299
Cdd:cd14004  83 YYLVMEKHGSGmDLFDFIERKPN-MDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVIL---DGNGTIKLIDFGSAAY 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 300 VRPDeRLNDIVGSAYYVAPEVLH-RSYT-TEADVWSIGVIAYILLCGSRPFWARTEsgifraVLKADPSFDEppwpSLSF 377
Cdd:cd14004 159 IKSG-PFDTFVGTIDYAAPEVLRgNPYGgKEQDIWALGVLLYTLVFKENPFYNIEE------ILEADLRIPY----AVSE 227
                       250       260
                ....*....|....*....|....*....
gi 15230288 378 EAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14004 228 DLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
148-407 2.36e-41

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: 150.32  E-value: 2.36e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGytcSAKFKKGELKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIVMEL 227
Cdd:cd05611   2 KPISKGAFG---SVYLAKKRSTGDYFAIKVLKKSDMIAKNQVTNVKAERAIMMIQGESPYVAKLYYSFQSKDYLYLVMEY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 228 CGGGELLDRILARGGkYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLSDFVRPDERLN 307
Cdd:cd05611  79 LNGGDCASLIKTLGG-LPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLI---DQTGHLKLTDFGLSRNGLEKRHNK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 308 DIVGSAYYVAPEVLHRSYTTEA-DVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDFVKRL 386
Cdd:cd05611 155 KFVGTPDYLAPETILGVGDDKMsDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPEEVKEFCSPEAVDLINRL 234
                       250       260
                ....*....|....*....|....
gi 15230288 387 LYKDPRKRMTAS---QALMHPWIA 407
Cdd:cd05611 235 LCMDPAKRLGANgyqEIKSHPFFK 258
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
145-406 5.79e-41

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: 149.43  E-value: 5.79e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTsaISIEDVRREVKILrALSGHQNLVQFYDAFEDNANVYIV 224
Cdd:cd06610   4 ELIEVIGSGATAVVYAAYCLP---KKEKVAIKRIDLEKCQ--TSMDELRKEIQAM-SQCNHPNVVSYYTSFVVGDELWLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGELLD---RILARGGkYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLSDFV- 300
Cdd:cd06610  78 MPLLSGGSLLDimkSSYPRGG-LDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILL---GEDGSVKIADFGVSASLa 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 301 ----RPDERLNDIVGSAYYVAPEVLH--RSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPsfdeppwPS 374
Cdd:cd06610 154 tggdRTRKVRKTFVGTPCWMAPEVMEqvRGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQNDP-------PS 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15230288 375 LSFEA---------KDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd06610 227 LETGAdykkysksfRKMISLCLQKDPSKRPTAEELLKHKFF 267
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
148-407 7.64e-41

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: 148.90  E-value: 7.64e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKFKKgelKDQEVAVKVIpksKMTSAiSIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMEL 227
Cdd:cd06614   6 EKIGEGASGEVYKATDRA---TGKEVAIKKM---RLRKQ-NKELIINEILIMKECK-HPNIVDYYDSYLVGDELWVVMEY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 228 CGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsmLKVIDFGLS-DFVRPDERL 306
Cdd:cd06614  78 MDGGSLTDIITQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGS---VKLADFGFAaQLTKEKSKR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 307 NDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWarTESG---IFRAVLKADPSFDEPPwpSLSFEAKDF 382
Cdd:cd06614 155 NSVVGTPYWMAPEVIKRKdYGPKVDIWSLGIMCIEMAEGEPPYL--EEPPlraLFLITTKGIPPLKNPE--KWSPEFKDF 230
                       250       260
                ....*....|....*....|....*
gi 15230288 383 VKRLLYKDPRKRMTASQALMHPWIA 407
Cdd:cd06614 231 LNKCLVKDPEKRPSAEELLQHPFLK 255
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
148-406 7.78e-41

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: 149.30  E-value: 7.78e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYT--CSAKfkkgeLKDQEVAVKVIPKSKMTSAISiEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIVM 225
Cdd:cd14198  14 KELGRGKFAVVrqCISK-----STGQEYAAKFLKKRRRGQDCR-AEILHEIAVLELAKSNPRVVNLHEVYETTSEIILIL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 226 ELCGGGELLDRILAR-GGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLSDFVRPDE 304
Cdd:cd14198  88 EYAAGGEIFNLCVPDlAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYPLGDIKIVDFGMSRKIGHAC 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 305 RLNDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDFV 383
Cdd:cd14198 168 ELREIMGTPEYLAPEILnYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNVDYSEETFSSVSQLATDFI 247
                       250       260
                ....*....|....*....|...
gi 15230288 384 KRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14198 248 QKLLVKNPEKRPTAEICLSHSWL 270
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
150-409 1.52e-40

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: 150.37  E-value: 1.52e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKfkkGELKDQEVAVKVIPKSkmtsaisIEDV----R--REVKILRALSgHQNLVQFYDAFEDNAN--- 220
Cdd:cd07834   8 IGSGAYGVVCSAY---DKRTGRKVAIKKISNV-------FDDLidakRilREIKILRHLK-HENIIGLLDILRPPSPeef 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 --VYIVMELCGGGelLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSD 298
Cdd:cd07834  77 ndVYIVTELMETD--LHKVIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNS---NCDLKICDFGLAR 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 299 FVRPDER---LNDIVGSAYYVAPEVL--HRSYTTEADVWSIGVIAYILLCGsRPFWA-----------------RTESGI 356
Cdd:cd07834 152 GVDPDEDkgfLTEYVVTRWYRAPELLlsSKKYTKAIDIWSVGCIFAELLTR-KPLFPgrdyidqlnlivevlgtPSEEDL 230
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15230288 357 -------FRAVLKADPSFDEPPWPSL----SFEAKDFVKRLLYKDPRKRMTASQALMHPWIAGY 409
Cdd:cd07834 231 kfissekARNYLKSLPKKPKKPLSEVfpgaSPEAIDLLEKMLVFNPKKRITADEALAHPYLAQL 294
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
148-405 1.96e-40

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: 147.94  E-value: 1.96e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISiEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMEL 227
Cdd:cd14082   9 EVLGSGQFGIVYGGKHRK---TGRDVAIKVIDKLRFPTKQE-SQLRNEVAILQQLS-HPGVVNLECMFETPERVFVVMEK 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 228 CGGgELLDRILAR-GGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLSDFVRPDERL 306
Cdd:cd14082  84 LHG-DMLEMILSSeKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPFPQVKLCDFGFARIIGEKSFR 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 307 NDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFwaRTESGIFRAVLKADPSFDEPPWPSLSFEAKDFVKR 385
Cdd:cd14082 163 RSVVGTPAYLAPEVLRNKgYNRSLDMWSVGVIIYVSLSGTFPF--NEDEDINDQIQNAAFMYPPNPWKEISPDAIDLINN 240
                       250       260
                ....*....|....*....|
gi 15230288 386 LLYKDPRKRMTASQALMHPW 405
Cdd:cd14082 241 LLQVKMRKRYSVDKSLSHPW 260
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
143-405 1.98e-40

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: 147.82  E-value: 1.98e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFGYtcsAKFKKGELKDQEVAVKVIPKSKMTSaisiEDVRREVKILRALSgHQNLVQFYDAFEDNANVY 222
Cdd:cd14665   1 RYELVKDIGSGNFGV---ARLMRDKQTKELVAVKYIERGEKID----ENVQREIINHRSLR-HPNIVRFKEVILTPTHLA 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 223 IVMELCGGGELLDRIlARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnSMLKVIDFGLSDFVRP 302
Cdd:cd14665  73 IVMEYAAGGELFERI-CNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPA-PRLKICDFGYSKSSVL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 303 DERLNDIVGSAYYVAPEVLHR-SYTTE-ADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKA--DPSFDEPPWPSLSFE 378
Cdd:cd14665 151 HSQPKSTVGTPAYIAPEVLLKkEYDGKiADVWSCGVTLYVMLVGAYPFEDPEEPRNFRKTIQRilSVQYSIPDYVHISPE 230
                       250       260
                ....*....|....*....|....*..
gi 15230288 379 AKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd14665 231 CRHLISRIFVADPATRITIPEIRNHEW 257
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
143-405 2.06e-40

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: 148.63  E-value: 2.06e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISiEDVRREVKILRALSGHQNLVQFYDAFEDNANVY 222
Cdd:cd07832   1 RYKILGRIGEGAHGIVFKAKDRE---TGETVALKKVALRKLEGGIP-NQALREIKALQACQGHPYVVKLRDVFPHGTGFV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 223 IVMELCGGGeLLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEensMLKVIDFGLSD-FVR 301
Cdd:cd07832  77 LVFEYMLSS-LSEVLRDEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTG---VLKIADFGLARlFSE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 302 PDERL-NDIVGSAYYVAPEVLH--RSYTTEADVWSIGVIAYILLCGSRPFWARTE----SGIFRAV----LKADPSFDEP 370
Cdd:cd07832 153 EDPRLySHQVATRWYRAPELLYgsRKYDEGVDLWAVGCIFAELLNGSPLFPGENDieqlAIVLRTLgtpnEKTWPELTSL 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 15230288 371 P--------------W----PSLSFEAKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd07832 233 PdynkitfpeskgirLeeifPDCSPEAIDLLKGLLVYNPKKRLSAEEALRHPY 285
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
174-403 4.13e-40

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: 147.00  E-value: 4.13e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 174 AVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELCGGGELLDRILARGgKYSEDDAKAVL 253
Cdd:cd14189  30 AVKVIPHSRVAKPHQREKIVNEIELHRDLH-HKHVVKFSHHFEDAENIYIFLELCSRKSLAHIWKARH-TLLEPEVRYYL 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 254 IQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFVRP-DERLNDIVGSAYYVAPEVLHRS-YTTEADV 331
Cdd:cd14189 108 KQIISGLKYLHLKGILHRDLKLGNFFIN---ENMELKVGDFGLAARLEPpEQRKKTICGTPNYLAPEVLLRQgHGPESDV 184
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15230288 332 WSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEppwpSLSFEAKDFVKRLLYKDPRKRMTASQALMH 403
Cdd:cd14189 185 WSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPA----SLSLPARHLLAGILKRNPGDRLTLDQILEH 252
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
147-406 4.41e-40

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 146.78  E-value: 4.41e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 147 GEEIGRGHFGYTCSA-KFKKGELkdqeVAVKVIP--KSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYI 223
Cdd:cd06632   5 GQLLGSGSFGSVYEGfNGDTGDF----FAVKEVSlvDDDKKSRESVKQLEQEIALLSKLR-HPNIVQYYGTEREEDNLYI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLdRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLSDFVRPD 303
Cdd:cd06632  80 FLEYVPGGSIH-KLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILV---DTNGVVKLADFGMAKHVEAF 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ERLNDIVGSAYYVAPEVL---HRSYTTEADVWSIGVIAyILLCGSRPFWARTESgiFRAVLKADPSFDEPPWP-SLSFEA 379
Cdd:cd06632 156 SFAKSFKGSPYWMAPEVImqkNSGYGLAVDIWSLGCTV-LEMATGKPPWSQYEG--VAAIFKIGNSGELPPIPdHLSPDA 232
                       250       260
                ....*....|....*....|....*..
gi 15230288 380 KDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd06632 233 KDFIRLCLQRDPEDRPTASQLLEHPFV 259
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
145-415 2.32e-39

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: 145.39  E-value: 2.32e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKKGELKdqeVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIV 224
Cdd:cd14117   9 DIGRPLGKGKFGNVYLAREKQSKFI---VALKVLFKSQIEKEGVEHQLRREIEIQSHLR-HPNILRLYNYFHDRKRIYLI 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGELLDRiLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsmLKVIDFGLSDFVrPDE 304
Cdd:cd14117  85 LEYAPRGELYKE-LQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGE---LKIADFGWSVHA-PSL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 305 RLNDIVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDeppwPSLSFEAKDFV 383
Cdd:cd14117 160 RRRTMCGTLDYLPPEMIEgRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFP----PFLSDGSRDLI 235
                       250       260       270
                ....*....|....*....|....*....|..
gi 15230288 384 KRLLYKDPRKRMTASQALMHPWIAGYKKIDIP 415
Cdd:cd14117 236 SKLLRYHPSERLPLKGVMEHPWVKANSRRVLP 267
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
146-406 4.15e-39

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: 144.19  E-value: 4.15e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 146 LGEEIGRGHFgytcsAKFKKG--ELKDQEVAVKVIPKSKMTS-AISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVY 222
Cdd:cd14070   6 IGRKLGEGSF-----AKVREGlhAVTGEKVAIKVIDKKKAKKdSYVTKNLRREGRIQQMIR-HPNITQLLDILETENSYY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 223 IVMELCGGGELLDRILARgGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLSDFVRP 302
Cdd:cd14070  80 LVMELCPGGNLMHRIYDK-KRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLL---DENDNIKLIDFGLSNCAGI 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 303 ---DERLNDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFwaRTESGIFRAVLKADPSFDEPPWPS-LSF 377
Cdd:cd14070 156 lgySDPFSTQCGSPAYAAPELLaRKKYGPKVDVWSIGVNMYAMLTGTLPF--TVEPFSLRALHQKMVDKEMNPLPTdLSP 233
                       250       260
                ....*....|....*....|....*....
gi 15230288 378 EAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14070 234 GAISFLRSLLEPDPLKRPNIKQALANRWL 262
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
143-406 5.71e-39

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: 144.37  E-value: 5.71e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPkskmtsaiSIEDVRREVK----ILRALSGHQNLVQFYDAF--- 215
Cdd:cd06608   7 IFELVEVIGEGTYGKVYKARHKK---TGQLAAIKIMD--------IIEDEEEEIKleinILRKFSNHPNIATFYGAFikk 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 216 -----EDNanVYIVMELCGGG---ELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENS 287
Cdd:cd06608  76 dppggDDQ--LWLVMEYCGGGsvtDLVKGLRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLT---EEA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 288 MLKVIDFGLS-DFVRPDERLNDIVGSAYYVAPEV------LHRSYTTEADVWSIGVIAYILLCGSRPFwarTESGIFRAV 360
Cdd:cd06608 151 EVKLVDFGVSaQLDSTLGRRNTFIGTPYWMAPEViacdqqPDASYDARCDVWSLGITAIELADGKPPL---CDMHPMRAL 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 15230288 361 LKAdPSfdEPPwPSLSFEAK------DFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd06608 228 FKI-PR--NPP-PTLKSPEKwskefnDFISECLIKNYEQRPFTEELLEHPFI 275
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
143-405 5.73e-39

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: 143.76  E-value: 5.73e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFGYtcsAKFKKGELKDQEVAVKVIPKSKMTSaisiEDVRREVKILRALSgHQNLVQFYDAFEDNANVY 222
Cdd:cd14662   1 RYELVKDIGSGNFGV---ARLMRNKETKELVAVKYIERGLKID----ENVQREIINHRSLR-HPNIIRFKEVVLTPTHLA 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 223 IVMELCGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnSMLKVIDFGLSDFVRP 302
Cdd:cd14662  73 IVMEYAAGGELFERICNAG-RFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPA-PRLKICDFGYSKSSVL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 303 DERLNDIVGSAYYVAPEVLHRS-YTTE-ADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPS--FDEPPWPSLSFE 378
Cdd:cd14662 151 HSQPKSTVGTPAYIAPEVLSRKeYDGKvADVWSCGVTLYVMLVGAYPFEDPDDPKNFRKTIQRIMSvqYKIPDYVRVSQD 230
                       250       260
                ....*....|....*....|....*..
gi 15230288 379 AKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd14662 231 CRHLLSRIFVANPAKRITIPEIKNHPW 257
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
144-349 9.85e-39

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 143.06  E-value: 9.85e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288    144 IELGEEIGRGHFGYTCSAKFK-KGELKDQEVAVKVIPKSKMTSAIsiEDVRREVKILRALSgHQNLVQFYDAFEDNANVY 222
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGKLKgKGGKKKVEVAVKTLKEDASEQQI--EEFLREARIMRKLD-HPNVVKLLGVCTEEEPLY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288    223 IVMELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFVRP 302
Cdd:smart00219  78 IVMEYMEGGDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVG---ENLVVKISDFGLSRDLYD 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288    303 DErlndivgsaYYV-----------APEVL-HRSYTTEADVWSIGVIAY-ILLCGSRPFW 349
Cdd:smart00219 155 DD---------YYRkrggklpirwmAPESLkEGKFTSKSDVWSFGVLLWeIFTLGEQPYP 205
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
150-406 1.32e-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: 143.23  E-value: 1.32e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKkgELKDQEVAVKVIPKSKMTSAISIedVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd14202  10 IGHGAFAVVFKGRHK--EKHDLEVAVKCINKKNLAKSQTL--LGKEIKILKELK-HENIVALYDFQEIANSVYLVMEYCN 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRILARgGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYT------SKEENSMLKVIDFGLSDFVRPD 303
Cdd:cd14202  85 GGDLADYLHTM-RTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSysggrkSNPNNIRIKIADFGFARYLQNN 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ERLNDIVGSAYYVAPEV-LHRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIfRAVLKADPSFDeppwPSLSFEAKDF 382
Cdd:cd14202 164 MMAATLCGSPMYMAPEViMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDL-RLFYEKNKSLS----PNIPRETSSH 238
                       250       260
                ....*....|....*....|....*...
gi 15230288 383 VKRLLY----KDPRKRMTASQALMHPWI 406
Cdd:cd14202 239 LRQLLLgllqRNQKDRMDFDEFFHHPFL 266
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
145-406 1.40e-38

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: 142.83  E-value: 1.40e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAK-FKKGELkdqeVAVKVIpksKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYI 223
Cdd:cd06613   3 ELIQRIGSGTYGDVYKARnIATGEL----AAVKVI---KLEPGDDFEIIQQEISMLKECR-HPNIVAYFGSYLRRDKLWI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDrILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLS-DFVRP 302
Cdd:cd06613  75 VMEYCGGGSLQD-IYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLT---EDGDVKLADFGVSaQLTAT 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 303 DERLNDIVGSAYYVAPEVL----HRSYTTEADVWSIGVIAYILLCGSRPfwaRTESGIFRAVLKADPSFDEPP------- 371
Cdd:cd06613 151 IAKRKSFIGTPYWMAPEVAaverKGGYDGKCDIWALGITAIELAELQPP---MFDLHPMRALFLIPKSNFDPPklkdkek 227
                       250       260       270
                ....*....|....*....|....*....|....*
gi 15230288 372 WpSLSFEakDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd06613 228 W-SPDFH--DFIKKCLTKNPKKRPTATKLLQHPFV 259
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
148-404 1.45e-38

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: 142.52  E-value: 1.45e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFG--YTCSAKFKkGELkdqeVAVKvipKSKMTSAISIEDVR--REVKILRALSGHQNLVQFYDAFEDNANVYI 223
Cdd:cd13997   6 EQIGSGSFSevFKVRSKVD-GCL----YAVK---KSKKPFRGPKERARalREVEAHAALGQHPNIVRYYSSWEEGGHLYI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDRI--LARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGLSdfVR 301
Cdd:cd13997  78 QMELCENGSLQDALeeLSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNK---GTCKIGDFGLA--TR 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 302 PDERLNDIVGSAYYVAPEVL--HRSYTTEADVWSIGVIAYILLCG-----SRPFWARTESGifravlkaDPSFdePPWPS 374
Cdd:cd13997 153 LETSGDVEEGDSRYLAPELLneNYTHLPKADIFSLGVTVYEAATGeplprNGQQWQQLRQG--------KLPL--PPGLV 222
                       250       260       270
                ....*....|....*....|....*....|
gi 15230288 375 LSFEAKDFVKRLLYKDPRKRMTASQALMHP 404
Cdd:cd13997 223 LSQELTRLLKVMLDPDPTRRPTADQLLAHD 252
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
145-406 1.88e-38

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: 142.40  E-value: 1.88e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKKGelkDQEVAVKVIPkskMTSaiSIEDVRREVKILRAlSGHQNLVQFYDAFEDNANVYIV 224
Cdd:cd06612   6 DILEKLGEGSYGSVYKAIHKET---GQVVAIKVVP---VEE--DLQEIIKEISILKQ-CDSPYIVKYYGSYFKNTDLWIV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsmLKVIDFGLSdfvrpdE 304
Cdd:cd06612  77 MEYCGAGSVSDIMKITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQ---AKLADFGVS------G 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 305 RLND-------IVGSAYYVAPEVLHRS-YTTEADVWSIGVIAyILLCGSRPFWARTESgiFRAVL----KADPSFDEPP- 371
Cdd:cd06612 148 QLTDtmakrntVIGTPFWMAPEVIQEIgYNNKADIWSLGITA-IEMAEGKPPYSDIHP--MRAIFmipnKPPPTLSDPEk 224
                       250       260       270
                ....*....|....*....|....*....|....*
gi 15230288 372 WpslSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd06612 225 W---SPEFNDFVKKCLVKDPEERPSAIQLLQHPFI 256
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
145-406 2.69e-38

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: 142.05  E-value: 2.69e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKKGELKdqeVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFED-NANVYI 223
Cdd:cd14163   3 QLGKTIGEGTYSKVKEAFSKKHQRK---VAIKIIDKSGGPEEFIQRFLPRELQIVERLD-HKNIIHVYEMLESaDGKIYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDRILaRGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEensmLKVIDFGLSDFVRPD 303
Cdd:cd14163  79 VMELAEDGDVFDCVL-HGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGFT----LKLTDFGFAKQLPKG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ER--LNDIVGSAYYVAPEVL----HRSytTEADVWSIGVIAYILLCGSRPFwarTESGIFRAVLKADPSFDEPPWPSLSF 377
Cdd:cd14163 154 GRelSQTFCGSTAYAAPEVLqgvpHDS--RKGDIWSMGVVLYVMLCAQLPF---DDTDIPKMLCQQQKGVSLPGHLGVSR 228
                       250       260
                ....*....|....*....|....*....
gi 15230288 378 EAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14163 229 TCQDLLKRLLEPDMVLRPSIEEVSWHPWL 257
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
150-425 4.86e-38

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


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 143.12  E-value: 4.86e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd05570   3 LGKGSFGKVMLAERKK---TDELYAIKVLKKEVIIEDDDVECTMTEKRVLALANRHPFLTGLHACFQTEDRLYFVMEYVN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRILaRGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGLS-DFVRPDERLND 308
Cdd:cd05570  80 GGDLMFHIQ-RARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAE---GHIKIADFGMCkEGIWGGNTTST 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 309 IVGSAYYVAPEVLHR-SYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLkadpsFDEPPWP-SLSFEAKDFVKRL 386
Cdd:cd05570 156 FCGTPDYIAPEILREqDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAIL-----NDEVLYPrWLSREAVSILKGL 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15230288 387 LYKDPRKRM----TASQALM-HPWiagYKKIDipFDILIFKQIK 425
Cdd:cd05570 231 LTKDPARRLgcgpKGEADIKaHPF---FRNID--WDKLEKKEVE 269
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
148-405 6.89e-38

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 141.69  E-value: 6.89e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKFKK-GELkdqeVAVKvipksKMTSAISIEDVR----REVKILRALSgHQNLVQFYDAFEDNANVY 222
Cdd:cd07833   7 GVVGEGAYGVVLKCRNKAtGEI----VAIK-----KFKESEDDEDVKktalREVKVLRQLR-HENIVNLKEAFRRKGRLY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 223 IVMELCGGgELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFV-- 300
Cdd:cd07833  77 LVFEYVER-TLLELLEASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVS---ESGVLKLCDFGFARALta 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 301 RPDERLNDIVGSAYYVAPEVL--HRSYTTEADVWSIGVIAYILLCGsRPFWARTES-----GIFRA----------VLKA 363
Cdd:cd07833 153 RPASPLTDYVATRWYRAPELLvgDTNYGKPVDVWAIGCIMAELLDG-EPLFPGDSDidqlyLIQKClgplppshqeLFSS 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15230288 364 DPSFDEPPWPSLS--------FEAK------DFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd07833 232 NPRFAGVAFPEPSqpeslerrYPGKvsspalDFLKACLRMDPKERLTCDELLQHPY 287
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
143-405 1.31e-37

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


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 141.17  E-value: 1.31e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMT--------SAIsiedvrREVKILRALSgHQNLVQFYDA 214
Cdd:cd07841   1 RYEKGKKLGEGTYAVVYKARDKE---TGRIVAIKKIKLGERKeakdginfTAL------REIKLLQELK-HPNIIGLLDV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 215 FEDNANVYIVMELCGGG-ELL--DRILarggKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsmLKV 291
Cdd:cd07841  71 FGHKSNINLVFEFMETDlEKVikDKSI----VLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGV---LKL 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 292 IDFGLS-DFVRPDERLNDIVGSAYYVAPEVLH--RSYTTEADVWSIGVI-AYILLcgSRPFWARTE-----SGIFRA--- 359
Cdd:cd07841 144 ADFGLArSFGSPNRKMTHQVVTRWYRAPELLFgaRHYGVGVDMWSVGCIfAELLL--RVPFLPGDSdidqlGKIFEAlgt 221
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15230288 360 -------VLKADPS------FDEPPW----PSLSFEAKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd07841 222 pteenwpGVTSLPDyvefkpFPPTPLkqifPAASDDALDLLQRLLTLNPNKRITARQALEHPY 284
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
144-349 2.31e-37

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: 139.22  E-value: 2.31e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288    144 IELGEEIGRGHFGYTCSAKFK-KGELKDQEVAVKVIPKSKMTSAIsiEDVRREVKILRALSgHQNLVQFYDAFEDNANVY 222
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKgKGDGKEVEVAVKTLKEDASEQQI--EEFLREARIMRKLD-HPNIVKLLGVCTEEEPLM 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288    223 IVMELCGGGELLDRILARGGKY-SEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFVR 301
Cdd:smart00221  78 IVMEYMPGGDLLDYLRKNRPKElSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVG---ENLVVKISDFGLSRDLY 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15230288    302 PDErlndivgsaYYV-----------APEVL-HRSYTTEADVWSIGVIAY-ILLCGSRPFW 349
Cdd:smart00221 155 DDD---------YYKvkggklpirwmAPESLkEGKFTSKSDVWSFGVLLWeIFTLGEEPYP 206
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
148-406 2.95e-37

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: 139.21  E-value: 2.95e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKFKKgelkDQEV-AVKVIPKSKMTSAISIEDVRrEVKILRALSgHQNLVQFYDAFEDNAN--VYIV 224
Cdd:cd08217   6 ETIGKGSFGTVRKVRRKS----DGKIlVWKEIDYGKMSEKEKQQLVS-EVNILRELK-HPNIVRYYDRIVDRANttLYIV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGEL---LDRILARGGKYSEDDAKAVLIQILNVVAFCHL-----QGVVHRDLKPEN-FLytskEENSMLKVIDFG 295
Cdd:cd08217  80 MEYCEGGDLaqlIKKCKKENQYIPEEFIWKIFTQLLLALYECHNrsvggGKILHRDLKPANiFL----DSDNNVKLGDFG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 296 LSDFVRPDERL-NDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTE--------SGIFravlkadp 365
Cdd:cd08217 156 LARVLSHDSSFaKTYVGTPYYMSPELLnEQSYDEKSDIWSLGCLIYELCALHPPFQAANQlelakkikEGKF-------- 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 15230288 366 sfdePPWPS-LSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd08217 228 ----PRIPSrYSSELNEVIKSMLNVDPDKRPSVEELLQLPLI 265
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
150-408 3.42e-37

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: 140.83  E-value: 3.42e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKK-GELkdqeVAVKVIPKSKMTSAISIEDVRREVKILrALSGHQNLVQFYDAFEDNANVYIVMELC 228
Cdd:cd05599   9 IGRGAFGEVRLVRKKDtGHV----YAMKKLRKSEMLEKEQVAHVRAERDIL-AEADNPWVVKLYYSFQDEENLYLIMEFL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 229 GGGELLDrILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGLSDFVRPDERLND 308
Cdd:cd05599  84 PGGDMMT-LLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDAR---GHIKLSDFGLCTGLKKSHLAYS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 309 IVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDFVKRLL 387
Cdd:cd05599 160 TVGTPDYIAPEVFLQKgYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMNWRETLVFPPEVPISPEAKDLIERLL 239
                       250       260
                ....*....|....*....|....
gi 15230288 388 yKDPRKRMTASQA---LMHPWIAG 408
Cdd:cd05599 240 -CDAEHRLGANGVeeiKSHPFFKG 262
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
148-405 4.61e-37

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: 138.97  E-value: 4.61e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGhfgyTCSAKFK---KGELkdQEVAVKVIPKSKMTsaisieDVRREVKILRALSgHQNLVQFYDAFEDNANVYIV 224
Cdd:cd14010   6 DEIGRG----KHSVVYKgrrKGTI--EFVAIKCVDKSKRP------EVLNEVRLTHELK-HPNVLKFYEWYETSNHLWLV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGELLDrILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLS------- 297
Cdd:cd14010  73 VEYCTGGDLET-LLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILL---DGNGTLKLSDFGLArregeil 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 298 ----------DFVRPDERLNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPs 366
Cdd:cd14010 149 kelfgqfsdeGNVNKVSKKQAKRGTPYYMAPELFQGGvHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDP- 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15230288 367 fdEPPWPSLSFEA----KDFVKRLLYKDPRKRMTASQALMHP-W 405
Cdd:cd14010 228 --PPPPPKVSSKPspdfKSLLKGLLEKDPAKRLSWDELVKHPfW 269
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
150-401 1.41e-36

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: 137.42  E-value: 1.41e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKGelkDQEVAVKVIPKSKmtSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd13996  14 LGSGGFGSVYKVRNKVD---GVTYAIKKIRLTE--KSSASEKVLREVKALAKLN-HPNIVRYYTAWVEEPPLYIQMELCE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRILARGGKYSEDDAKAVLI--QILNVVAFCHLQGVVHRDLKPEN-FLytsKEENSMLKVIDFGLSDFVRPDERL 306
Cdd:cd13996  88 GGTLRDWIDRRNSSSKNDRKLALELfkQILKGVSYIHSKGIVHRDLKPSNiFL---DNDDLQVKIGDFGLATSIGNQKRE 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 307 NDI---------------VGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCgsrPFWARTE-SGIFRAV--LKADPSF 367
Cdd:cd13996 165 LNNlnnnnngntsnnsvgIGTPLYASPEQLDGEnYNEKADIYSLGIILFEMLH---PFKTAMErSTILTDLrnGILPESF 241
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15230288 368 DE--PPWpslsfeaKDFVKRLLYKDPRKRMTASQAL 401
Cdd:cd13996 242 KAkhPKE-------ADLIQSLLSKNPEERPSAEQLL 270
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
149-406 4.76e-36

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: 135.87  E-value: 4.76e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 149 EIGRGHFGYT--CSAKFKKgelkdQEVAVKVIPKSKMTSaisiEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVME 226
Cdd:cd14113  14 ELGRGRFSVVkkCDQRGTK-----RAVATKFVNKKLMKR----DQVTHELGVLQSLQ-HPQLVGLLDTFETPTSYILVLE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 227 LCGGGELLDRILaRGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLSDFVRPDERL 306
Cdd:cd14113  84 MADQGRLLDYVV-RWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSKPTIKLADFGDAVQLNTTYYI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 307 NDIVGSAYYVAPE-VLHRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDFVKR 385
Cdd:cd14113 163 HQLLGSPEFAAPEiILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPDDYFKGVSQKAKDFVCF 242
                       250       260
                ....*....|....*....|.
gi 15230288 386 LLYKDPRKRMTASQALMHPWI 406
Cdd:cd14113 243 LLQMDPAKRPSAALCLQEQWL 263
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
145-407 5.08e-36

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: 136.41  E-value: 5.08e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIpksKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIV 224
Cdd:cd06611   8 EIIGELGDGAFGKVYKAQHKE---TGLFAAAKII---QIESEEELEDFMVEIDILSECK-HPNIVGLYEAYFYENKLWIL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsmLKVIDFGLS-DFVRPD 303
Cdd:cd06611  81 IEFCDGGALDSIMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGD---VKLADFGVSaKNKSTL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ERLNDIVGSAYYVAPEVL------HRSYTTEADVWSIGvIAYILLCGSRPfwARTESGIFRAVLKA----DPSFDEPPWP 373
Cdd:cd06611 158 QKRDTFIGTPYWMAPEVVacetfkDNPYDYKADIWSLG-ITLIELAQMEP--PHHELNPMRVLLKIlksePPTLDQPSKW 234
                       250       260       270
                ....*....|....*....|....*....|....
gi 15230288 374 SLSFeaKDFVKRLLYKDPRKRMTASQALMHPWIA 407
Cdd:cd06611 235 SSSF--NDFLKSCLVKDPDDRPTAAELLKHPFVS 266
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
150-405 6.18e-36

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


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 135.91  E-value: 6.18e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFgytcSAKFKKGELKDQ-EVAVKV---IPK-SKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFE-DNANVYI 223
Cdd:cd13990   8 LGKGGF----SEVYKAFDLVEQrYVACKIhqlNKDwSEEKKQNYIKHALREYEIHKSLD-HPRIVKLYDVFEiDTDSFCT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELlDRILARGGKYSEDDAKAVLIQILNVVAFC--HLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLSDFVr 301
Cdd:cd13990  83 VLEYCDGNDL-DFYLKQHKSIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHSGNVSGEIKITDFGLSKIM- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 302 PDERLNDI--------VGSAYYVAPEVLHR-----SYTTEADVWSIGVIAYILLCGSRPFWAR-TESGIFRA--VLKA-D 364
Cdd:cd13990 161 DDESYNSDgmeltsqgAGTYWYLPPECFVVgktppKISSKVDVWSVGVIFYQMLYGRKPFGHNqSQEAILEEntILKAtE 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15230288 365 PSFdePPWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd13990 241 VEF--PSKPVVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
150-406 9.43e-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: 135.14  E-value: 9.43e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKGelKDQEVAVKVIPKSKMTSAISIedVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd14201  14 VGHGAFAVVFKGRHRKK--TDWEVAIKSINKKNLSKSQIL--LGKEIKILKELQ-HENIVALYDVQEMPNSVFLVMEYCN 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRILARgGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFL--YTSKEENSM----LKVIDFGLSDFVRPD 303
Cdd:cd14201  89 GGDLADYLQAK-GTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILlsYASRKKSSVsgirIKIADFGFARYLQSN 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ERLNDIVGSAYYVAPEV-LHRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIfRAVLKADPSFdEPPWPS-LSFEAKD 381
Cdd:cd14201 168 MMAATLCGSPMYMAPEViMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDL-RMFYEKNKNL-QPSIPReTSPYLAD 245
                       250       260
                ....*....|....*....|....*
gi 15230288 382 FVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14201 246 LLLGLLQRNQKDRMDFEAFFSHPFL 270
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
143-406 1.80e-35

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: 134.09  E-value: 1.80e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFG--YTCSAKFKK--GELKdqevAVKVIPKSKMTSAISIeDVRREVKILRALSgHQNLVQFYDAFEDN 218
Cdd:cd08222   1 RYRVVRKLGSGNFGtvYLVSDLKATadEELK----VLKEISVGELQPDETV-DANREAKLLSKLD-HPAIVKFHDSFVEK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 219 ANVYIVMELCGGGELLDRILA---RGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPEN-FLytskeENSMLKVIDF 294
Cdd:cd08222  75 ESFCIVTEYCEGGDLDDKISEykkSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNiFL-----KNNVIKVGDF 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 295 GLSDFVRPDERL-NDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKAD-PSFDEpp 371
Cdd:cd08222 150 GISRILMGTSDLaTTFTGTPYYMSPEVLkHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGEtPSLPD-- 227
                       250       260       270
                ....*....|....*....|....*....|....*
gi 15230288 372 wpSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd08222 228 --KYSKELNAIYSRMLNKDPALRPSAAEILKIPFI 260
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
148-408 2.18e-35

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: 135.44  E-value: 2.18e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFG--YTCsakfkkgELKDQEV--AVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYI 223
Cdd:cd05574   7 KLLGKGDVGrvYLV-------RLKGTGKlfAMKVLDKEEMIKRNKVKRVLTEREILATLD-HPFLPTLYASFQTSTHLCF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLdRILAR--GGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLS---- 297
Cdd:cd05574  79 VMDYCPGGELF-RLLQKqpGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLH---ESGHIMLTDFDLSkqss 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 298 ------------------------DFV--RPDERLNDIVGSAYYVAPEVLHRSYTTEA-DVWSIGVIAYILLCGSRPFWA 350
Cdd:cd05574 155 vtpppvrkslrkgsrrssvksiekETFvaEPSARSNSFVGTEEYIAPEVIKGDGHGSAvDWWTLGILLYEMLYGTTPFKG 234
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15230288 351 RTESGIFRAVLKADPSFdePPWPSLSFEAKDFVKRLLYKDPRKRM----TASQALMHPWIAG 408
Cdd:cd05574 235 SNRDETFSNILKKELTF--PESPPVSSEAKDLIRKLLVKDPSKRLgskrGASEIKRHPFFRG 294
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
143-413 8.74e-35

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: 134.45  E-value: 8.74e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFGYTCSAKFKkgELKDQE-VAVKVIPKSkMTSAISIEDVRREVKILRALSGHQNLVQFYD---AFEDN 218
Cdd:cd07857   1 RYELIKELGQGAYGIVCSARNA--ETSEEEtVAIKKITNV-FSKKILAKRALRELKLLRHFRGHKNITCLYDmdiVFPGN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 219 AN-VYIVMELCGGGelLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLS 297
Cdd:cd07857  78 FNeLYLYEELMEAD--LHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNA---DCELKICDFGLA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 298 -----DFVRPDERLNDIVGSAYYVAPEVL--HRSYTTEADVWSIGVIAYILLcGSRPFW--------------------- 349
Cdd:cd07857 153 rgfseNPGENAGFMTEYVATRWYRAPEIMlsFQSYTKAIDVWSVGCILAELL-GRKPVFkgkdyvdqlnqilqvlgtpde 231
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15230288 350 ---ARTESGIFRAVLKADPSFDEPPWPSL----SFEAKDFVKRLLYKDPRKRMTASQALMHPWIAGYKKID 413
Cdd:cd07857 232 etlSRIGSPKAQNYIRSLPNIPKKPFESIfpnaNPLALDLLEKLLAFDPTKRISVEEALEHPYLAIWHDPD 302
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
144-409 1.52e-34

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: 131.70  E-value: 1.52e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 144 IELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVI---PKSKMTSAISiedvrREVKILRAlSGHQNLVQFYDAFEDNAN 220
Cdd:cd06605   3 LEYLGELGEGNGGVVSKVRHRP---SGQIMAVKVIrleIDEALQKQIL-----RELDVLHK-CNSPYIVGFYGAFYSEGD 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 VYIVMELCGGGElLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQ-GVVHRDLKPENFLYTSKEEnsmLKVIDFGLSDf 299
Cdd:cd06605  74 ISICMEYMDGGS-LDKILKEVGRIPERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRGQ---VKLCDFGVSG- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 300 VRPDERLNDIVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPF---WARTESGIF---RAVLKADPsfdePPW 372
Cdd:cd06605 149 QLVDSLAKTFVGTRSYMAPERISgGKYTVKSDIWSLGLSLVELATGRFPYpppNAKPSMMIFellSYIVDEPP----PLL 224
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 15230288 373 PSLSF--EAKDFVKRLLYKDPRKRMTASQALMHPWIAGY 409
Cdd:cd06605 225 PSGKFspDFQDFVSQCLQKDPTERPSYKELMEHPFIKRY 263
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
148-411 2.46e-34

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: 131.44  E-value: 2.46e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGytcsAKFKKGELKDQE-VAVKVIPKSkmTSAISIEDVRREVKILRALSGHQ--NLVQFYDAFEDNANVYIV 224
Cdd:cd06917   7 ELVGRGSYG----AVYRGYHVKTGRvVALKVLNLD--TDDDDVSDIQKEVALLSQLKLGQpkNIIKYYGSYLKGPSLWII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGELldRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsmLKVIDFGL-SDFVRPD 303
Cdd:cd06917  81 MDYCEGGSI--RTLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGN---VKLCDFGVaASLNQNS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ERLNDIVGSAYYVAPEVLH--RSYTTEADVWSIGVIAYILLCGSRPFwarTESGIFRAVL----KADPSFDEPPWpslSF 377
Cdd:cd06917 156 SKRSTFVGTPYWMAPEVITegKYYDTKADIWSLGITTYEMATGNPPY---SDVDALRAVMlipkSKPPRLEGNGY---SP 229
                       250       260       270
                ....*....|....*....|....*....|....
gi 15230288 378 EAKDFVKRLLYKDPRKRMTASQALMHPWIAGYKK 411
Cdd:cd06917 230 LLKEFVAACLDEEPKDRLSADELLKSKWIKQHSK 263
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
144-349 2.57e-34

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: 130.69  E-value: 2.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288   144 IELGEEIGRGHFG--YTCSAKFKKGElKDQEVAVKVIPKSkmTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANV 221
Cdd:pfam07714   1 LTLGEKLGEGAFGevYKGTLKGEGEN-TKIKVAVKTLKEG--ADEEEREDFLEEASIMKKLD-HPNIVKLLGVCTQGEPL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288   222 YIVMELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFVR 301
Cdd:pfam07714  77 YIVTEYMPGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVS---ENLVVKISDFGLSRDIY 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15230288   302 PDErlndivgsaYYV------------APEVL-HRSYTTEADVWSIGVIAY-ILLCGSRPFW 349
Cdd:pfam07714 154 DDD---------YYRkrgggklpikwmAPESLkDGKFTSKSDVWSFGVLLWeIFTLGEQPYP 206
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
171-405 2.98e-34

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: 130.45  E-value: 2.98e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 171 QEVAVKVIPKSKMTSAISIED-VRREVKILRALSgHQNLVQFYDAFEDNAN--VYIVMELCGGG--ELLDRilARGGKYS 245
Cdd:cd14119  19 CRRAVKILKKRKLRRIPNGEAnVKREIQILRRLN-HRNVIKLVDVLYNEEKqkLYMVMEYCVGGlqEMLDS--APDKRLP 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 246 EDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEensMLKVIDFGLSDFV---RPDERLNDIVGSAYYVAPEV-- 320
Cdd:cd14119  96 IWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDG---TLKISDFGVAEALdlfAEDDTCTTSQGSPAFQPPEIan 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 321 -LHRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADpsFDEPPWpsLSFEAKDFVKRLLYKDPRKRMTASQ 399
Cdd:cd14119 173 gQDSFSGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGE--YTIPDD--VDPDLQDLLRGMLEKDPEKRFTIEQ 248

                ....*.
gi 15230288 400 ALMHPW 405
Cdd:cd14119 249 IRQHPW 254
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
146-406 3.15e-34

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: 131.07  E-value: 3.15e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 146 LGEEIGRGHFGytcsaKFKKGELKDQ-------EVAVKVIPKSKMTSAISIEDVRREVKILRALsGHQNLVQFYDAFEDN 218
Cdd:cd14076   5 LGRTLGEGEFG-----KVKLGWPLPKanhrsgvQVAIKLIRRDTQQENCQTSKIMREINILKGL-THPNIVRLLDVLKTK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 219 ANVYIVMELCGGGELLDRILARggKYSEDD-AKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLS 297
Cdd:cd14076  79 KYIGIVLEFVSGGELFDYILAR--RRLKDSvACRLFAQLISGVAYLHKKGVVHRDLKLENLLL---DKNRNLVITDFGFA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 298 DFVRPDErlNDIV----GSAYYVAPE--VLHRSYT-TEADVWSIGVIAYILLCGSRPF---WARTESG----IFRAVLKA 363
Cdd:cd14076 154 NTFDHFN--GDLMstscGSPCYAAPElvVSDSMYAgRKADIWSCGVILYAMLAGYLPFdddPHNPNGDnvprLYRYICNT 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 15230288 364 DPSFDEPPWPslsfEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14076 232 PLIFPEYVTP----KARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
146-406 3.19e-34

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: 130.55  E-value: 3.19e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 146 LGEEIGRGHFG--YTCSAKfkkgelkD--QEVAVKVIPKSKMTSAIS--IEDVRREVKILRALSgHQNLVQFYDAFEDNA 219
Cdd:cd06625   4 QGKLLGQGAFGqvYLCYDA-------DtgRELAVKQVEIDPINTEASkeVKALECEIQLLKNLQ-HERIVQYYGCLQDEK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 220 NVYIVMELCGGGELLDRILARGGkYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSdf 299
Cdd:cd06625  76 SLSIFMEYMPGGSVKDEIKAYGA-LTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDS---NGNVKLGDFGAS-- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 300 vrpdERLNDI---------VGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCgSRPFWARTES--GIFRAVLKaDPSF 367
Cdd:cd06625 150 ----KRLQTIcsstgmksvTGTPYWMSPEVINgEGYGRKADIWSVGCTVVEMLT-TKPPWAEFEPmaAIFKIATQ-PTNP 223
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 15230288 368 DEPpwPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd06625 224 QLP--PHVSEDARDFLSLIFVRNKKQRPSAEELLSHSFV 260
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
149-406 4.55e-34

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: 130.56  E-value: 4.55e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 149 EIGRGHFGYTcsaKFKKGELKDQEVAVKVIPKSKMTSAI--------------------SIEDVRREVKILRALSgHQNL 208
Cdd:cd14118   1 EIGKGSYGIV---KLAYNEEDNTLYAMKILSKKKLLKQAgffrrppprrkpgalgkpldPLDRVYREIAILKKLD-HPNV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 209 VQFYDAFEDNA--NVYIVMELCGGGELLDRILARggKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeEN 286
Cdd:cd14118  77 VKLVEVLDDPNedNLYMVFELVDKGAVMEVPTDN--PLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLG---DD 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 287 SMLKVIDFGLSD-FVRPDERLNDIVGSAYYVAPEVL---HRSYTTEA-DVWSIGVIAYILLCGSRPFWARTESGIFRAVL 361
Cdd:cd14118 152 GHVKIADFGVSNeFEGDDALLSSTAGTPAFMAPEALsesRKKFSGKAlDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIK 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 15230288 362 KADPSFdePPWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14118 232 TDPVVF--PDDPVVSEQLKDLILRMLDKNPSERITLPEIKEHPWV 274
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
148-406 6.81e-34

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: 129.55  E-value: 6.81e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAiSIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMEL 227
Cdd:cd08218   6 KKIGEGSFGKALLVKSKE---DGKQYVIKEINISKMSPK-EREESRKEVAVLSKMK-HPNIVQYQESFEENGNLYIVMDY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 228 CGGGELLDRILA-RGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFVRPDERL 306
Cdd:cd08218  81 CDGGDLYKRINAqRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLT---KDGIIKLGDFGIARVLNSTVEL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 307 -NDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKAdpSFdePPWPS-LSFEAKDFV 383
Cdd:cd08218 158 aRTCIGTPYYLSPEICeNKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRG--SY--PPVPSrYSYDLRSLV 233
                       250       260
                ....*....|....*....|...
gi 15230288 384 KRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd08218 234 SQLFKRNPRDRPSINSILEKPFI 256
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
150-421 7.27e-34

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 131.37  E-value: 7.27e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKGELKDQEVAVKVIPKSKM-TSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELC 228
Cdd:cd05584   4 LGKGGYGKVFQVRKTTGSDKGKIFAMKVLKKASIvRNQKDTAHTKAERNILEAVK-HPFIVDLHYAFQTGGKLYLILEYL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 229 GGGELLDRiLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGLS-DFVRPDERLN 307
Cdd:cd05584  83 SGGELFMH-LEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQ---GHVKLTDFGLCkESIHDGTVTH 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 308 DIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFdePPWpsLSFEAKDFVKRL 386
Cdd:cd05584 159 TFCGTIEYMAPEILTRSgHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNL--PPY--LTNEARDLLKKL 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 15230288 387 LYKDPRKRM-----TASQALMHPWIAGY-------KKIDIPFDILIF 421
Cdd:cd05584 235 LKRNVSSRLgsgpgDAEEIKAHPFFRHInwddllaKKVEPPFKPLLQ 281
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
150-408 9.34e-34

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: 131.28  E-value: 9.34e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKK-GELkdqeVAVKVIPKSKMTSAISIEDVRREVKILrALSGHQNLVQFYDAFEDNANVYIVMELC 228
Cdd:cd05601   9 IGRGHFGEVQVVKEKAtGDI----YAMKVLKKSETLAQEEVSFFEEERDIM-AKANSPWITKLQYAFQDSENLYLVMEYH 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 229 GGGELLDRILARGGKYSEDDAK---AVLIQILNVVafcHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGLSDFVRPDER 305
Cdd:cd05601  84 PGGDLLSLLSRYDDIFEESMARfylAELVLAIHSL---HSMGYVHRDIKPENILIDRT---GHIKLADFGSAAKLSSDKT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 306 LNDI--VGSAYYVAPEVLHR-------SYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLS 376
Cdd:cd05601 158 VTSKmpVGTPDYIAPEVLTSmnggskgTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMNFKKFLKFPEDPKVS 237
                       250       260       270
                ....*....|....*....|....*....|..
gi 15230288 377 FEAKDFVKRLLyKDPRKRMTASQALMHPWIAG 408
Cdd:cd05601 238 ESAVDLIKGLL-TDAKERLGYEGLCCHPFFSG 268
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
142-395 1.25e-33

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 131.09  E-value: 1.25e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  142 SRIELGEEIGRGHFGYTCSAKFKKGElkdQEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANV 221
Cdd:PTZ00263  18 SDFEMGETLGTGSFGRVRIAKHKGTG---EYYAIKCLKKREILKMKQVQHVAQEKSILMELS-HPFIVNMMCSFQDENRV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  222 YIVMELCGGGELLDRiLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGLSDFVR 301
Cdd:PTZ00263  94 YFLLEFVVGGELFTH-LRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNK---GHVKVTDFGFAKKVP 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  302 pdERLNDIVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFdePPWpsLSFEAK 380
Cdd:PTZ00263 170 --DRTFTLCGTPEYLAPEVIQsKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKF--PNW--FDGRAR 243
                        250
                 ....*....|....*
gi 15230288  381 DFVKRLLYKDPRKRM 395
Cdd:PTZ00263 244 DLVKGLLQTDHTKRL 258
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
145-401 1.54e-33

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: 128.93  E-value: 1.54e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFgytcSAKFKKGELKDQE-VAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYI 223
Cdd:cd08224   3 EIEKKIGKGQF----SVVYRARCLLDGRlVALKKVQIFEMMDAKARQDCLKEIDLLQQLN-HPNIIKYLASFIENNELNI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGEL--LDRILARGGKY-SEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSDFV 300
Cdd:cd08224  78 VLELADAGDLsrLIKHFKKQKRLiPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITA---NGVVKLGDLGLGRFF 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 301 RPDE-RLNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTES--GIFRAVLKAdpsfDEPPWPSLS 376
Cdd:cd08224 155 SSKTtAAHSLVGTPYYMSPERIREQgYDFKSDIWSLGCLLYEMAALQSPFYGEKMNlySLCKKIEKC----EYPPLPADL 230
                       250       260
                ....*....|....*....|....*..
gi 15230288 377 F--EAKDFVKRLLYKDPRKRMTASQAL 401
Cdd:cd08224 231 YsqELRDLVAACIQPDPEKRPDISYVL 257
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
147-403 2.03e-33

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


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 128.21  E-value: 2.03e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 147 GEEIGRGHFGyTCsakFKKGELKDQEV-AVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVM 225
Cdd:cd14188   6 GKVLGKGGFA-KC---YEMTDLTTNKVyAAKIIPHSRVSKPHQREKIDKEIELHRILH-HKHVVQFYHYFEDKENIYILL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 226 ELCGGGELLDRILARgGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFVRP-DE 304
Cdd:cd14188  81 EYCSRRSMAHILKAR-KVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFIN---ENMELKVGDFGLAARLEPlEH 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 305 RLNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEppwpSLSFEAKDFV 383
Cdd:cd14188 157 RRRTICGTPNYLSPEVLNKQgHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPS----SLLAPAKHLI 232
                       250       260
                ....*....|....*....|
gi 15230288 384 KRLLYKDPRKRMTASQALMH 403
Cdd:cd14188 233 ASMLSKNPEDRPSLDEIIRH 252
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
150-405 2.52e-33

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: 127.77  E-value: 2.52e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYT--CSAKFKKgelkdQEVAVKVIPKsKMTSAisiEDVRREVKILRALSGHQnLVQFYDAFEDNANVYIVMEL 227
Cdd:cd14115   1 IGRGRFSIVkkCLHKATR-----KDVAVKFVSK-KMKKK---EQAAHEAALLQHLQHPQ-YITLHDTYESPTSYILVLEL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 228 CGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLSDFVRPDERLN 307
Cdd:cd14115  71 MDDGRLLDYLMNHD-ELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHRHVH 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 308 DIVGSAYYVAPEVLHRSYTTEA-DVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDFVKRL 386
Cdd:cd14115 150 HLLGNPEFAAPEVIQGTPVSLAtDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDEYFGDVSQAARDFINVI 229
                       250
                ....*....|....*....
gi 15230288 387 LYKDPRKRMTASQALMHPW 405
Cdd:cd14115 230 LQEDPRRRPTAATCLQHPW 248
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
145-404 2.68e-33

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: 127.91  E-value: 2.68e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKKgelkDQEV-AVKVIPKSKMTSAISiEDVRREVKILRALSgHQNLVQFYDAFEDNANVYI 223
Cdd:cd08529   3 EILNKLGKGSFGVVYKVVRKV----DGRVyALKQIDISRMSRKMR-EEAIDEARVLSKLN-SPYVIKYYDSFVDKGKLNI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDRILARGGK-YSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENfLYTSKEENsmLKVIDFGLSDFVRP 302
Cdd:cd08529  77 VMEYAENGDLHSLIKSQRGRpLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMN-IFLDKGDN--VKIGDLGVAKILSD 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 303 DERL-NDIVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKAdpsfDEPPWP-SLSFEA 379
Cdd:cd08529 154 TTNFaQTIVGTPYYLSPELCEdKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRG----KYPPISaSYSQDL 229
                       250       260
                ....*....|....*....|....*
gi 15230288 380 KDFVKRLLYKDPRKRMTASQALMHP 404
Cdd:cd08529 230 SQLIDSCLTKDYRQRPDTTELLRNP 254
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
149-407 3.37e-33

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: 127.94  E-value: 3.37e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 149 EIGRGHFGYTCSAKFKKgelKDQEVAVKvipKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELC 228
Cdd:cd06648  14 KIGEGSTGIVCIATDKS---TGRQVAVK---KMDLRKQQRRELLFNEVVIMRDYQ-HPNIVEMYSSYLVGDELWVVMEFL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 229 GGGELLDRILArgGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSDFVRPD-ERLN 307
Cdd:cd06648  87 EGGALTDIVTH--TRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTS---DGRVKLSDFGFCAQVSKEvPRRK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 308 DIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPwPSLSFEAKDFVKRL 386
Cdd:cd06648 162 SLVGTPYWMAPEVISRLpYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNEPPKLKNL-HKVSPRLRSFLDRM 240
                       250       260
                ....*....|....*....|.
gi 15230288 387 LYKDPRKRMTASQALMHPWIA 407
Cdd:cd06648 241 LVRDPAQRATAAELLNHPFLA 261
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
174-408 3.60e-33

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: 127.89  E-value: 3.60e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 174 AVKVIPK-SKMTSAISIEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIVMELCGGGELLDRILARGgKYSEDDAKAV 252
Cdd:cd05583  26 AMKVLKKaTIVQKAKTAEHTMTERQVLEAVRQSPFLVTLHYAFQTDAKLHLILDYVNGGELFTHLYQRE-HFTESEVRIY 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 253 LIQIlnVVAFCHLQ--GVVHRDLKPENFLYtskEENSMLKVIDFGLSDFVRP--DERLNDIVGSAYYVAPEVL---HRSY 325
Cdd:cd05583 105 IGEI--VLALEHLHklGIIYRDIKLENILL---DSEGHVVLTDFGLSKEFLPgeNDRAYSFCGTIEYMAPEVVrggSDGH 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 326 TTEADVWSIGVIAYILLCGSRPFW----ARTESGIFRAVLKAdpsfdEPPWP-SLSFEAKDFVKRLLYKDPRKRM----- 395
Cdd:cd05583 180 DKAVDWWSLGVLTYELLTGASPFTvdgeRNSQSEISKRILKS-----HPPIPkTFSAEAKDFILKLLEKDPKKRLgagpr 254
                       250
                ....*....|...
gi 15230288 396 TASQALMHPWIAG 408
Cdd:cd05583 255 GAHEIKEHPFFKG 267
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
150-401 3.81e-33

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: 127.40  E-value: 3.81e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGytcSAKFKKGELKDQEVAVKVIPKSKMTSAIsiEDVRREVkILRALSGHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd08219   8 VGEGSFG---RALLVQHVNSDQKYAMKEIRLPKSSSAV--EDSRKEA-VLLAKMKHPNIVAFKESFEADGHLYIVMEYCD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRI-LARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFV-RPDERLN 307
Cdd:cd08219  82 GGDLMQKIkLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLT---QNGKVKLGDFGSARLLtSPGAYAC 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 308 DIVGSAYYVAPEVLHR-SYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSfdepPWPS-LSFEAKDFVKR 385
Cdd:cd08219 159 TYVGTPYYVPPEIWENmPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYK----PLPShYSYELRSLIKQ 234
                       250
                ....*....|....*.
gi 15230288 386 LLYKDPRKRMTASQAL 401
Cdd:cd08219 235 MFKRNPRSRPSATTIL 250
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
134-409 1.06e-32

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: 128.46  E-value: 1.06e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 134 FGFSKELQSRIELGEEIGRGHFGYTCSAKfkkGELKDQEVAVKVIPKSKMTSAISiEDVRREVKILRALSgHQNLVQFYD 213
Cdd:cd07856   2 FGTVFEITTRYSDLQPVGMGAFGLVCSAR---DQLTGQNVAVKKIMKPFSTPVLA-KRTYRELKLLKHLR-HENIISLSD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 214 AF----EDnanVYIVMELCGGGelLDRILArgGKYSEDD-AKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSM 288
Cdd:cd07856  77 IFisplED---IYFVTELLGTD--LHRLLT--SRPLEKQfIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVN---ENCD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 289 LKVIDFGLSDFvrPDERLNDIVGSAYYVAPEVL--HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAV------ 360
Cdd:cd07856 147 LKICDFGLARI--QDPQMTGYVSTRYYRAPEIMltWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIItellgt 224
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 361 -----------------LKADPSFDEPP----WPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWIAGY 409
Cdd:cd07856 225 ppddvinticsentlrfVQSLPKRERVPfsekFKNADPDAIDLLEKMLVFDPKKRISAAEALAHPYLAPY 294
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
150-404 1.18e-32

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: 125.97  E-value: 1.18e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGytcsAKFKKGELKD-QEVAVKVIPKSKMTSAiSIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELC 228
Cdd:cd08530   8 LGKGSYG----SVYKVKRLSDnQVYALKEVNLGSLSQK-EREDSVNEIRLLASVN-HPNIIRYKEAFLDGNRLCIVMEYA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 229 GGGELLDRILARGGK---YSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSDfVRPDER 305
Cdd:cd08530  82 PFGDLSKLISKRKKKrrlFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSA---GDLVKIGDLGISK-VLKKNL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 306 LNDIVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKAdpSFDEPPwPSLSFEAKDFVK 384
Cdd:cd08530 158 AKTQIGTPLYAAPEVWKgRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRG--KFPPIP-PVYSQDLQQIIR 234
                       250       260
                ....*....|....*....|
gi 15230288 385 RLLYKDPRKRMTASQALMHP 404
Cdd:cd08530 235 SLLQVNPKKRPSCDKLLQSP 254
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
149-406 1.28e-32

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: 126.19  E-value: 1.28e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 149 EIGRGHFGYTCSAKFKKgelKDQEVAVKVIP-KSKMTSAisiedVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMEL 227
Cdd:cd14110  10 EINRGRFSVVRQCEEKR---SGQMLAAKIIPyKPEDKQL-----VLREYQVLRRLS-HPRIAQLHSAYLSPRHLVLIEEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 228 CGGGELLDRiLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFVRPDERL- 306
Cdd:cd14110  81 CSGPELLYN-LAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIIT---EKNLLKIVDLGNAQPFNQGKVLm 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 307 NDIVGsaYYV---APEVLH-RSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEpPWPSLSFEAKDF 382
Cdd:cd14110 157 TDKKG--DYVetmAPELLEgQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQLSR-CYAGLSGGAVNF 233
                       250       260
                ....*....|....*....|....
gi 15230288 383 VKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14110 234 LKSTLCAKPWGRPTASECLQNPWL 257
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
146-406 1.69e-32

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: 125.73  E-value: 1.69e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 146 LGEEIGRGHFGYTcsakFKKGELKD-QEVAVKVIPKSKMTSAISIEDVR---REVKILRAL---SGHQNLVQFYDAFEDN 218
Cdd:cd14101   4 MGNLLGKGGFGTV----YAGHRISDgLQVAIKQISRNRVQQWSKLPGVNpvpNEVALLQSVgggPGHRGVIRLLDWFEIP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 219 ANVYIVMEL---CGggELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENsmLKVIDFG 295
Cdd:cd14101  80 EGFLLVLERpqhCQ--DLFDYITERG-ALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLRTGD--IKLIDFG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 296 lSDFVRPDERLNDIVGSAYYVAPEVL--HRSYTTEADVWSIGVIAYILLCGSRPFWARTEsgifraVLKADPSFDEPpwp 373
Cdd:cd14101 155 -SGATLKDSMYTDFDGTRVYSPPEWIlyHQYHALPATVWSLGILLYDMVCGDIPFERDTD------ILKAKPSFNKR--- 224
                       250       260       270
                ....*....|....*....|....*....|...
gi 15230288 374 sLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14101 225 -VSNDCRSLIRSCLAYNPSDRPSLEQILLHPWM 256
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
148-362 2.09e-32

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: 125.73  E-value: 2.09e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKFKKGELKDQEVAVKVIPKSKMTSAIsiEDVRREVKILRALsGHQNLVQFYDAFEDNANVYIVMEL 227
Cdd:cd00192   1 KKLGEGAFGEVYKGKLKGGDGKTVDVAVKTLKEDASESER--KDFLKEARVMKKL-GHPNVVRLLGVCTEEEPLYLVMEY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 228 CGGGELLDRILARGGKYSEDDAKAVLIQILnvVAFC--------HL--QGVVHRDLKPENFLYTSKEEnsmLKVIDFGLS 297
Cdd:cd00192  78 MEGGDLLDFLRKSRPVFPSPEPSTLSLKDL--LSFAiqiakgmeYLasKKFVHRDLAARNCLVGEDLV---VKISDFGLS 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15230288 298 DFVRPDErlndivgsaYYV------------APEVL-HRSYTTEADVWSIGVIAY-ILLCGSRPFWARTESGIFRAVLK 362
Cdd:cd00192 153 RDIYDDD---------YYRkktggklpirwmAPESLkDGIFTSKSDVWSFGVLLWeIFTLGATPYPGLSNEEVLEYLRK 222
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
145-407 2.71e-32

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 125.91  E-value: 2.71e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGytcsaKFKKGELKDQEV--AVKVIpksKMTSAISIEDVRREVKILrALSGHQNLVQFYDAFEDNANVY 222
Cdd:cd06643   8 EIVGELGDGAFG-----KVYKAQNKETGIlaAAKVI---DTKSEEELEDYMVEIDIL-ASCDHPNIVKLLDAFYYENNLW 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 223 IVMELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsmLKVIDFGLS-DFVR 301
Cdd:cd06643  79 ILIEFCAGGAVDAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGD---IKLADFGVSaKNTR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 302 PDERLNDIVGSAYYVAPEVL------HRSYTTEADVWSIGViAYILLCGSRPfwARTESGIFRAVLKADPSfdEPP---W 372
Cdd:cd06643 156 TLQRRDSFIGTPYWMAPEVVmcetskDRPYDYKADVWSLGV-TLIEMAQIEP--PHHELNPMRVLLKIAKS--EPPtlaQ 230
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15230288 373 PS-LSFEAKDFVKRLLYKDPRKRMTASQALMHPWIA 407
Cdd:cd06643 231 PSrWSPEFKDFLRKCLEKNVDARWTTSQLLQHPFVS 266
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
147-406 3.60e-32

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: 125.19  E-value: 3.60e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 147 GEEIGRGHFG--YTCsAKFKKGELkdqeVAVK--VIPKSKMTSAIS-----IEDVRREVKILRALSgHQNLVQfYDAFED 217
Cdd:cd06629   6 GELIGKGTYGrvYLA-MNATTGEM----LAVKqvELPKTSSDRADSrqktvVDALKSEIDTLKDLD-HPNIVQ-YLGFEE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 218 NANVY-IVMELCGGGELlDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGL 296
Cdd:cd06629  79 TEDYFsIFLEYVPGGSI-GSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILV---DLEGICKISDFGI 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 297 S---DFVRPDERLNDIVGSAYYVAPEVLH---RSYTTEADVWSIGVIAYILLCGSRPfWARTEsgIFRAVLKADPSFDEP 370
Cdd:cd06629 155 SkksDDIYGNNGATSMQGSVFWMAPEVIHsqgQGYSAKVDIWSLGCVVLEMLAGRRP-WSDDE--AIAAMFKLGNKRSAP 231
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 15230288 371 PWPS---LSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd06629 232 PVPEdvnLSPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
145-405 3.96e-32

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: 125.47  E-value: 3.96e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTcsakFKKGELKDQE-VAVK--VIPKSKMTSAISiedVRREVKILRAL--SGHQNLVQFYDAF---- 215
Cdd:cd07838   2 EEVAEIGEGAYGTV----YKARDLQDGRfVALKkvRVPLSEEGIPLS---TIREIALLKQLesFEHPNVVRLLDVChgpr 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 216 -EDNANVYIVMELCGG--GELLDRILARGgkYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsmLKVI 292
Cdd:cd07838  75 tDRELKLTLVFEHVDQdlATYLDKCPKPG--LPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQ---VKLA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 293 DFGLSDFVRPDERLNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLcGSRP-FWARTESG----IFRAVLKadPS 366
Cdd:cd07838 150 DFGLARIYSFEMALTSVVVTLWYRAPEVLLQSsYATPVDMWSVGCIFAELF-NRRPlFRGSSEADqlgkIFDVIGL--PS 226
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15230288 367 FDEppWP-----------------------SLSFEAKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd07838 227 EEE--WPrnsalprssfpsytprpfksfvpEIDEEGLDLLKKMLTFNPHKRISAFEALQHPY 286
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
150-429 4.11e-32

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: 126.56  E-value: 4.11e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd05590   3 LGKGSFGKVMLARLKE---SGRLYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLYCCFQTPDRLFFVMEFVN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRIlARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGL-SDFVRPDERLND 308
Cdd:cd05590  80 GGDLMFHI-QKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLL---DHEGHCKLADFGMcKEGIFNGKTTST 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 309 IVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKadpsfDEPPWPS-LSFEAKDFVKRL 386
Cdd:cd05590 156 FCGTPDYIAPEILQEMlYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILN-----DEVVYPTwLSQDAVDILKAF 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 15230288 387 LYKDPRKRMTA------SQALMHPWiagYKKIDipFDILIFKQIKAYLR 429
Cdd:cd05590 231 MTKNPTMRLGSltlggeEAILRHPF---FKELD--WEKLNRRQIEPPFR 274
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
150-416 4.67e-32

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: 125.59  E-value: 4.67e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKGElkdQEVAVKVIPKSKMTSAISIEDVRREVKILRALsGHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd14209   9 LGTGSFGRVMLVRHKETG---NYYAMKILDKQKVVKLKQVEHTLNEKRILQAI-NFPFLVKLEYSFKDNSNLYMVMEYVP 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRiLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLSDFVRpdERLNDI 309
Cdd:cd14209  85 GGEMFSH-LRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLI---DQQGYIKVTDFGFAKRVK--GRTWTL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 310 VGSAYYVAPE-VLHRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFdeppwPS-LSFEAKDFVKRLL 387
Cdd:cd14209 159 CGTPEYLAPEiILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRF-----PShFSSDLKDLLRNLL 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15230288 388 YKDPRKRM-----TASQALMHPWIAGY-------KKIDIPF 416
Cdd:cd14209 234 QVDLTKRFgnlknGVNDIKNHKWFATTdwiaiyqRKVEAPF 274
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
143-406 6.14e-32

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: 124.30  E-value: 6.14e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFGytcSAKFKKGELKDQEVAVKVIPKSKMTSAiSIEDVRREVkILRALSGHQNLVQFYDAFEDNANVY 222
Cdd:cd08225   1 RYEIIKKIGEGSFG---KIYLAKAKSDSEHCVIKEIDLTKMPVK-EKEASKKEV-ILLAKMKHPNIVTFFASFQENGRLF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 223 IVMELCGGGELLDRI-LARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSML-KVIDFGLSdfv 300
Cdd:cd08225  76 IVMEYCDGGDLMKRInRQRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSK---NGMVaKLGDFGIA--- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 301 rpdERLND-------IVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFwarTESGIFRAVLKADPSFDEPPW 372
Cdd:cd08225 150 ---RQLNDsmelaytCVGTPYYLSPEICqNRPYNNKTDIWSLGCVLYELCTLKHPF---EGNNLHQLVLKICQGYFAPIS 223
                       250       260       270
                ....*....|....*....|....*....|....
gi 15230288 373 PSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd08225 224 PNFSRDLRSLISQLFKVSPRDRPSITSILKRPFL 257
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
150-409 7.16e-32

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: 126.25  E-value: 7.16e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKGElkdQEVAVKvipksKMT----SAISIEDVRREVKILRALSgHQNLVQFYDAF------EDNA 219
Cdd:cd07851  23 VGSGAYGQVCSAFDTKTG---RKVAIK-----KLSrpfqSAIHAKRTYRELRLLKHMK-HENVIGLLDVFtpasslEDFQ 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 220 NVYIVMELCGGGelLDRILaRGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSdf 299
Cdd:cd07851  94 DVYLVTHLMGAD--LNNIV-KCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVN---EDCELKILDFGLA-- 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 300 vRP-DERLNDIVGSAYYVAPEVLH--RSYTTEADVWSIGVIAYILLCG-----------------------SRPFWARTE 353
Cdd:cd07851 166 -RHtDDEMTGYVATRWYRAPEIMLnwMHYNQTVDIWSVGCIMAELLTGktlfpgsdhidqlkrimnlvgtpDEELLKKIS 244
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 354 SGIFRAVLKADPSFDEPPWPSL----SFEAKDFVKRLLYKDPRKRMTASQALMHPWIAGY 409
Cdd:cd07851 245 SESARNYIQSLPQMPKKDFKEVfsgaNPLAIDLLEKMLVLDPDKRITAAEALAHPYLAEY 304
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
139-413 9.65e-32

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: 125.94  E-value: 9.65e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 139 ELQSRIELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSkMTSAISIEDVRREVKILRALSgHQNLVQFYDAF--- 215
Cdd:cd07855   2 DVGDRYEPIETIGSGAYGVVCSAIDTK---SGQKVAIKKIPNA-FDVVTTAKRTLRELKILRHFK-HDNIIAIRDILrpk 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 216 ---EDNANVYIVMELCGGGelLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVI 292
Cdd:cd07855  77 vpyADFKDVYVVLDLMESD--LHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVN---ENCELKIG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 293 DFGLSDFV--RPDER---LNDIVGSAYYVAPE---VLHRsYTTEADVWSIGVI---------------------AYILLC 343
Cdd:cd07855 152 DFGMARGLctSPEEHkyfMTEYVATRWYRAPElmlSLPE-YTQAIDMWSVGCIfaemlgrrqlfpgknyvhqlqLILTVL 230
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15230288 344 GSRP--FWARTESGIFRAVLKADPSFDEPPW----PSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWIAGYKKID 413
Cdd:cd07855 231 GTPSqaVINAIGADRVRRYIQNLPNKQPVPWetlyPKADQQALDLLSQMLRFDPSERITVAEALQHPFLAKYHDPD 306
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
145-406 1.31e-31

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


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 123.53  E-value: 1.31e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFG--YTCsakfkKGELKDQEVAVKVIPKSKMTSAISIEdvrrEVKILRALSGHQ-----NLVQFYDAFED 217
Cdd:cd14133   2 EVLEVLGKGTFGqvVKC-----YDLLTGEEVALKIIKNNKDYLDQSLD----EIRLLELLNKKDkadkyHIVRLKDVFYF 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 218 NANVYIVMELCGGG--ELLDRILARGgkYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnSMLKVIDFG 295
Cdd:cd14133  73 KNHLCIVFELLSQNlyEFLKQNKFQY--LSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSR-CQIKIIDFG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 296 LSDFVrpDERLNDIVGSAYYVAPEV-LHRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFdePPW-- 372
Cdd:cd14133 150 SSCFL--TQRLYSYIQSRYYRAPEViLGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIP--PAHml 225
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 15230288 373 ---PSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14133 226 dqgKADDELFVDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
149-406 1.43e-31

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: 124.33  E-value: 1.43e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 149 EIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAisiEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELC 228
Cdd:cd06659  28 KIGEGSTGVVCIAREKH---SGRQVAVKMMDLRKQQRR---ELLFNEVVIMRDYQ-HPNVVEMYKSYLVGEELWVLMEYL 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 229 GGGELLDriLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSDFVRPD-ERLN 307
Cdd:cd06659 101 QGGALTD--IVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTL---DGRVKLSDFGFCAQISKDvPKRK 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 308 DIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLkadpsfDEPPwPSLSFEAK------ 380
Cdd:cd06659 176 SLVGTPYWMAPEVISRCpYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLR------DSPP-PKLKNSHKaspvlr 248
                       250       260
                ....*....|....*....|....*.
gi 15230288 381 DFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd06659 249 DFLERMLVRDPQERATAQELLDHPFL 274
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
139-409 1.88e-31

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: 125.11  E-value: 1.88e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 139 ELQSRIELGEEIGRGHFGYTCSAKFKkgeLKDQEVAVKVI-PKSKMTSAIsiedvR--REVKILRALSgHQNLVQFYD-- 213
Cdd:cd07849   2 DVGPRYQNLSYIGEGAYGMVCSAVHK---PTGQKVAIKKIsPFEHQTYCL-----RtlREIKILLRFK-HENIIGILDiq 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 214 ---AFEDNANVYIVMELCGGGelLDRILaRGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLK 290
Cdd:cd07849  73 rppTFESFKDVYIVQELMETD--LYKLI-KTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNT---NCDLK 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 291 VIDFGLSDFVRPDER----LNDIVGSAYYVAPEVL--HRSYTTEADVWSIGVI-AYILLCgsRPFW-------------- 349
Cdd:cd07849 147 ICDFGLARIADPEHDhtgfLTEYVATRWYRAPEIMlnSKGYTKAIDIWSVGCIlAEMLSN--RPLFpgkdylhqlnlilg 224
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15230288 350 ----------ARTESGIFRAVLKADPSFDEPPWPSL----SFEAKDFVKRLLYKDPRKRMTASQALMHPWIAGY 409
Cdd:cd07849 225 ilgtpsqedlNCIISLKARNYIKSLPFKPKVPWNKLfpnaDPKALDLLDKMLTFNPHKRITVEEALAHPYLEQY 298
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
145-420 1.93e-31

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: 124.65  E-value: 1.93e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKKGELKDQEVAVKVIPKSKMTS-AISIEDVRREVKILRALSGHQNLVQFYDAFEDNANVYI 223
Cdd:cd05614   3 ELLKVLGTGAYGKVFLVRKVSGHDANKLYAMKVLRKAALVQkAKTVEHTRTERNVLEHVRQSPFLVTLHYAFQTDAKLHL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGLS-DFVRP 302
Cdd:cd05614  83 ILDYVSGGELFTHLYQRD-HFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSE---GHVVLTDFGLSkEFLTE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 303 D-ERLNDIVGSAYYVAPEVLhRSYTTEA---DVWSIGVIAYILLCGSRPFW----ARTESGIFRAVLKADPSFDeppwPS 374
Cdd:cd05614 159 EkERTYSFCGTIEYMAPEII-RGKSGHGkavDWWSLGILMFELLTGASPFTlegeKNTQSEVSRRILKCDPPFP----SF 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15230288 375 LSFEAKDFVKRLLYKDPRKRM-----TASQALMHPWIAGY-------KKIDIPFDILI 420
Cdd:cd05614 234 IGPVARDLLQKLLCKDPKKRLgagpqGAQEIKEHPFFKGLdwealalRKVNPPFRPSI 291
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
194-412 3.05e-31

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: 122.92  E-value: 3.05e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 194 REVKILRALSgHQNLVQFYDAFEDNA--NVYIVMELCGGGEL---LDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGV 268
Cdd:cd06621  48 RELEINKSCA-SPYIVKYYGAFLDEQdsSIGIAMEYCEGGSLdsiYKKVKKKGGRIGEKVLGKIAESVLKGLSYLHSRKI 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 269 VHRDLKPENFLYTSKEEnsmLKVIDFGLSDfvrpdERLNDI----VGSAYYVAPE-VLHRSYTTEADVWSIGVIAYILLC 343
Cdd:cd06621 127 IHRDIKPSNILLTRKGQ---VKLCDFGVSG-----ELVNSLagtfTGTSYYMAPErIQGGPYSITSDVWSLGLTLLEVAQ 198
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 344 GSRPFWARTE---------SGIFRA---VLKADPSfDEPPWpSLSFeaKDFVKRLLYKDPRKRMTASQALMHPWIAGYKK 411
Cdd:cd06621 199 NRFPFPPEGEpplgpiellSYIVNMpnpELKDEPE-NGIKW-SESF--KDFIEKCLEKDGTRRPGPWQMLAHPWIKAQEK 274

                .
gi 15230288 412 I 412
Cdd:cd06621 275 K 275
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
150-406 3.06e-31

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: 122.15  E-value: 3.06e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFG--YTCSAKFKKgelkdQEVAVKVIPKSKMTSAiSIEDVRREVKILRALSgHQNLVQFYDAF-EDNAnVYIVME 226
Cdd:cd08220   8 VGRGAYGtvYLCRRKDDN-----KLVIIKQIPVEQMTKE-ERQAALNEVKVLSMLH-HPNIIEYYESFlEDKA-LMIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 227 LCGGGELLDRILARGGKY-SEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsMLKVIDFGLSDFVRPDER 305
Cdd:cd08220  80 YAPGGTLFEYIQQRKGSLlSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRT--VVKIGDFGISKILSSKSK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 306 LNDIVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPFWARTESGIfraVLKADPSFDEPPWPSLSFEAKDFVK 384
Cdd:cd08220 158 AYTVVGTPCYISPELCEgKPYNQKSDIWALGCVLYELASLKRAFEAANLPAL---VLKIMRGTFAPISDRYSEELRHLIL 234
                       250       260
                ....*....|....*....|..
gi 15230288 385 RLLYKDPRKRMTASQALMHPWI 406
Cdd:cd08220 235 SMLHLDPNKRPTLSEIMAQPII 256
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
147-406 3.78e-31

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: 122.16  E-value: 3.78e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 147 GEEIGRGHFGYTCSAKFKKGELkdqeVAVKVI---PKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYI 223
Cdd:cd06631   6 GNVLGKGAYGTVYCGLTSTGQL----IAVKQVeldTSDKEKAEKEYEKLQEEVDLLKTLK-HVNIVGYLGTCLEDNVVSI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELlDRILARGGKYSEddakAVLI----QILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFG---- 295
Cdd:cd06631  81 FMEFVPGGSI-ASILARFGALEE----PVFCrytkQILEGVAYLHNNNVIHRDIKGNNIMLMP---NGVIKLIDFGcakr 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 296 ---LSDFVRPDERLNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGsRPFWARTE--SGIFR--AVLKADPSF 367
Cdd:cd06631 153 lciNLSSGSQSQLLKSMRGTPYWMAPEVINETgHGRKSDIWSIGCTVFEMATG-KPPWADMNpmAAIFAigSGRKPVPRL 231
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 15230288 368 DEppwpSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd06631 232 PD----KFSPEARDFVHACLTRDQDERPSAEQLLKHPFI 266
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
141-404 4.79e-31

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: 123.04  E-value: 4.79e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 141 QSRIELGEEIGRGHFgytcSAKFK--KGElKDQEVAVKV---IPKSKmtsaisiedVRREVKILRALSGHQNLVQFYDAF 215
Cdd:cd14132  17 QDDYEIIRKIGRGKY----SEVFEgiNIG-NNEKVVIKVlkpVKKKK---------IKREIKILQNLRGGPNIVKLLDVV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 216 ED-NANVY-IVMELCGGGELLDRIlargGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtsKEENSMLKVID 293
Cdd:cd14132  83 KDpQSKTPsLIFEYVNNTDFKTLY----PTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMI--DHEKRKLRLID 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 294 FGLSDFVRPDERLNDIVGSAYYVAPEVL--HRSYTTEADVWSIGVIAYILLCGSRPFW------------AR---TEsGI 356
Cdd:cd14132 157 WGLAEFYHPGQEYNVRVASRYYKGPELLvdYQYYDYSLDMWSLGCMLASMIFRKEPFFhghdnydqlvkiAKvlgTD-DL 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15230288 357 FRAV----LKADPSFDE-----PPWPSLSF-----------EAKDFVKRLLYKDPRKRMTASQALMHP 404
Cdd:cd14132 236 YAYLdkygIELPPRLNDilgrhSKKPWERFvnsenqhlvtpEALDLLDKLLRYDHQERITAKEAMQHP 303
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
143-406 5.75e-31

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


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 123.04  E-value: 5.75e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFGYTCSAK-FKKGELkdqeVAVKVIPKSKMTSAISIEdvrrEVKILRAL-----SGHQNLVQFYDAFE 216
Cdd:cd14210  14 RYEVLSVLGKGSFGQVVKCLdHKTGQL----VAIKIIRNKKRFHQQALV----EVKILKHLndndpDDKHNIVRYKDSFI 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 217 DNANVYIVMELCGGG--ELLDRILARGgkYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTsKEENSMLKVIDF 294
Cdd:cd14210  86 FRGHLCIVFELLSINlyELLKSNNFQG--LSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLK-QPSKSSIKVIDF 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 295 GLSDFVrpDERLNDIVGSAYYVAPEV-LHRSYTTEADVWSIGVIAYILLCGsRP-FWARTES---GIFRAVLKADPS--- 366
Cdd:cd14210 163 GSSCFE--GEKVYTYIQSRFYRAPEViLGLPYDTAIDMWSLGCILAELYTG-YPlFPGENEEeqlACIMEVLGVPPKsli 239
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15230288 367 ---------FDEPPWP--------------SLSFEAK---------DFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14210 240 dkasrrkkfFDSNGKPrpttnskgkkrrpgSKSLAQVlkcddpsflDFLKKCLRWDPSERMTPEEALQHPWI 311
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
148-404 7.84e-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: 121.55  E-value: 7.84e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKFKKGelkdQEVAVKVIPKSKMTSAIsIEDVRREVKILRALSGHQNLVQFYDA--FEDNANVYIVM 225
Cdd:cd14131   7 KQLGKGGSSKVYKVLNPKK----KIYALKRVDLEGADEQT-LQSYKNEIELLKKLKGSDRIIQLYDYevTDEDDYLYMVM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 226 ElCGGGELlDRILA--RGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeensMLKVIDFGLSDFVRPD 303
Cdd:cd14131  82 E-CGEIDL-ATILKkkRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVKG----RLKLIDFGIAKAIQND 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 E----RLNdIVGSAYYVAPEVLHRSYTTE-----------ADVWSIGVIAYILLCGSRPFwARTESGIFRAVLKADPSFd 368
Cdd:cd14131 156 TtsivRDS-QVGTLNYMSPEAIKDTSASGegkpkskigrpSDVWSLGCILYQMVYGKTPF-QHITNPIAKLQAIIDPNH- 232
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 15230288 369 EPPWPSLSF-EAKDFVKRLLYKDPRKRMTASQALMHP 404
Cdd:cd14131 233 EIEFPDIPNpDLIDVMKRCLQRDPKKRPSIPELLNHP 269
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
147-401 9.78e-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: 121.19  E-value: 9.78e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 147 GEEIGRGHFGyTCsakFKKGELKDQEV-AVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVM 225
Cdd:cd14187  12 GRFLGKGGFA-KC---YEITDADTKEVfAGKIVPKSLLLKPHQKEKMSMEIAIHRSLA-HQHVVGFHGFFEDNDFVYVVL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 226 ELCGGGELLDrILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsmLKVIDFGLSDFVRPD-E 304
Cdd:cd14187  87 ELCRRRSLLE-LHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDME---VKIGDFGLATKVEYDgE 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 305 RLNDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSlsfeAKDFV 383
Cdd:cd14187 163 RKKTLCGTPNYIAPEVLsKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPV----AASLI 238
                       250
                ....*....|....*...
gi 15230288 384 KRLLYKDPRKRMTASQAL 401
Cdd:cd14187 239 QKMLQTDPTARPTINELL 256
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
148-405 1.56e-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: 121.13  E-value: 1.56e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKFKK-GELkdqeVAVKVIPKSKMTSAISIEDVRrEVKILRALSgHQNLVQFYD------AFEDNAN 220
Cdd:cd07840   5 AQIGEGTYGQVYKARNKKtGEL----VALKKIRMENEKEGFPITAIR-EIKLLQKLD-HPNVVRLKEivtskgSAKYKGS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 VYIVME-----LCGggeLLDRilaRGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsmLKVIDFG 295
Cdd:cd07840  79 IYMVFEymdhdLTG---LLDN---PEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGV---LKLADFG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 296 LSDFVRPDE--RLNDIVGSAYYVAPEVL--HRSYTTEADVWSIGVIAYILLCGSRPFWARTESG----IFRAV----LKA 363
Cdd:cd07840 150 LARPYTKENnaDYTNRVITLWYRPPELLlgATRYGPEVDMWSVGCILAELFTGKPIFQGKTELEqlekIFELCgsptEEN 229
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15230288 364 DPSFDEPPW----------PSLSFE---------AKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd07840 230 WPGVSDLPWfenlkpkkpyKRRLREvfknvidpsALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
145-406 1.94e-30

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 120.89  E-value: 1.94e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVI-PKSKMTsaisiEDVRREVKILRALSGHQNLVQFYDAF--EDNAN- 220
Cdd:cd06638  21 EIIETIGKGTYGKVFKVLNKK---NGSKAAVKILdPIHDID-----EEIEAEYNILKALSDHPNVVKFYGMYykKDVKNg 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 --VYIVMELCGGGELLDRI---LARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFG 295
Cdd:cd06638  93 dqLWLVLELCNGGSVTDLVkgfLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTE---GGVKLVDFG 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 296 LS-DFVRPDERLNDIVGSAYYVAPEV------LHRSYTTEADVWSIGVIAYILLCGSRPFwarTESGIFRAVLK----AD 364
Cdd:cd06638 170 VSaQLTSTRLRRNTSVGTPFWMAPEViaceqqLDSTYDARCDVWSLGITAIELGDGDPPL---ADLHPMRALFKiprnPP 246
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 15230288 365 PSFDEPP-WpslSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd06638 247 PTLHQPElW---SNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
145-426 2.22e-30

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


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 120.88  E-value: 2.22e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKKGELKDQEVAVKVIPKSKMTS-AISIEDVRREVKILRALSGHQNLVQFYDAFEDNANVYI 223
Cdd:cd05613   3 ELLKVLGTGAYGKVFLVRKVSGHDAGKLYAMKVLKKATIVQkAKTAEHTRTERQVLEHIRQSPFLVTLHYAFQTDTKLHL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLS-DFVRP 302
Cdd:cd05613  83 ILDYINGGELFTHLSQRE-RFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDS---SGHVVLTDFGLSkEFLLD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 303 D-ERLNDIVGSAYYVAPEVLH---RSYTTEADVWSIGVIAYILLCGSRPFWA----RTESGIFRAVLKAdpsfdEPPWPS 374
Cdd:cd05613 159 EnERAYSFCGTIEYMAPEIVRggdSGHDKAVDWWSLGVLMYELLTGASPFTVdgekNSQAEISRRILKS-----EPPYPQ 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15230288 375 -LSFEAKDFVKRLLYKDPRKRM-----TASQALMHPWiagYKKIDipFDILIFKQIKA 426
Cdd:cd05613 234 eMSALAKDIIQRLLMKDPKKRLgcgpnGADEIKKHPF---FQKIN--WDDLAAKKVPA 286
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
148-404 2.63e-30

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


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 119.25  E-value: 2.63e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKFKKGEL----KDQEVAVK-VIPKSkmtSAISIEdvrREVKILRALSGHQNLVQFYDAFEDNANVY 222
Cdd:cd14019   7 EKIGEGTFSSVYKAEDKLHDLydrnKGRLVALKhIYPTS---SPSRIL---NELECLERLGGSNNVSGLITAFRNEDQVV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 223 IVMELCGGGELLDRIlargGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLkvIDFGLSDFV-- 300
Cdd:cd14019  81 AVLPYIEHDDFRDFY----RKMSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNRETGKGVL--VDFGLAQREed 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 301 RPDERLNDiVGSAYYVAPEVLHRSY--TTEADVWSIGVIAYILLCGSRPFWartesgifravlKADPSFDeppwpSL--- 375
Cdd:cd14019 155 RPEQRAPR-AGTRGFRAPEVLFKCPhqTTAIDIWSAGVILLSILSGRFPFF------------FSSDDID-----ALaei 216
                       250       260       270
                ....*....|....*....|....*....|....
gi 15230288 376 -----SFEAKDFVKRLLYKDPRKRMTASQALMHP 404
Cdd:cd14019 217 atifgSDEAYDLLDKLLELDPSKRITAEEALKHP 250
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
145-406 7.09e-30

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: 119.28  E-value: 7.09e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTcsaKFKKGELKDQEVAVKVIPKSKMTSA-----------------------ISIEDVRREVKILRA 201
Cdd:cd14200   3 KLQSEIGKGSYGVV---KLAYNESDDKYYAMKVLSKKKLLKQygfprrppprgskaaqgeqakplAPLERVYQEIAILKK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 202 LSgHQNLVQFYDAFEDNA--NVYIVMELCGGGELLDriLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFL 279
Cdd:cd14200  80 LD-HVNIVKLIEVLDDPAedNLYMVFDLLRKGPVME--VPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 280 YTskeENSMLKVIDFGLSD-FVRPDERLNDIVGSAYYVAPEVLH---RSYTTEA-DVWSIGVIAYILLCGSRPFWARTES 354
Cdd:cd14200 157 LG---DDGHVKIADFGVSNqFEGNDALLSSTAGTPAFMAPETLSdsgQSFSGKAlDVWAMGVTLYCFVYGKCPFIDEFIL 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 15230288 355 GIFRAVlKADPsFDEPPWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14200 234 ALHNKI-KNKP-VEFPEEPEISEELKDLILKMLDKNPETRITVPEIKVHPWV 283
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
194-417 7.76e-30

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: 120.36  E-value: 7.76e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 194 REVKILRALSGHQNLVQFYDAF--EDNANVYIVMElcgggelldrilarggkYSEDDAKAV--------------LIQIL 257
Cdd:cd07852  55 REIMFLQELNDHPNIIKLLNVIraENDKDIYLVFE-----------------YMETDLHAViraniledihkqyiMYQLL 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 258 NVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGLSDFVRPDE------RLNDIVGSAYYVAPEVL--HRSYTTEA 329
Cdd:cd07852 118 KALKYLHSGGVIHRDLKPSNILLNSD---CRVKLADFGLARSLSQLEeddenpVLTDYVATRWYRAPEILlgSTRYTKGV 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 330 DVWSIGVIAYILLCGsRPFWART-----------------------------ESGIFRAVLKADPSFDEPPwPSLSFEAK 380
Cdd:cd07852 195 DMWSVGCILGEMLLG-KPLFPGTstlnqlekiievigrpsaediesiqspfaATMLESLPPSRPKSLDELF-PKASPDAL 272
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 15230288 381 DFVKRLLYKDPRKRMTASQALMHPWIAGYKK----------IDIPFD 417
Cdd:cd07852 273 DLLKKLLVFNPNKRLTAEEALRHPYVAQFHNpadepslpgpIVIPLD 319
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
146-406 1.24e-29

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: 117.65  E-value: 1.24e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 146 LGEEIGRGHFGYTCSAKFKKGELKdqeVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFE-DNANVYIV 224
Cdd:cd14164   4 LGTTIGEGSFSKVKLATSQKYCCK---VAIKIVDRRRASPDFVQKFLPRELSILRRVN-HPNIVQMFECIEvANGRLYIV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MElCGGGELLDRIlARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENsmLKVIDFGLSDFVR-PD 303
Cdd:cd14164  80 ME-AAATDLLQKI-QEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDRK--IKIADFGFARFVEdYP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ERLNDIVGSAYYVAPEV-LHRSYTTEA-DVWSIGVIAYILLCGSRPFwarTESGIFRAVLKADPsFDEPPWPSLSFEAKD 381
Cdd:cd14164 156 ELSTTFCGSRAYTPPEViLGTPYDPKKyDVWSLGVVLYVMVTGTMPF---DETNVRRLRLQQRG-VLYPSGVALEEPCRA 231
                       250       260
                ....*....|....*....|....*
gi 15230288 382 FVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14164 232 LIRTLLQFNPSTRPSIQQVAGNSWL 256
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
141-404 1.64e-29

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: 118.37  E-value: 1.64e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 141 QSRIELGEEIGRGHFGYTCSAKFKKGElkdQEVAVKVIPKSKmtsaisiedvR---REVKILRALSgHQNLVQFYDAF-- 215
Cdd:cd14137   3 EISYTIEKVIGSGSFGVVYQAKLLETG---EVVAIKKVLQDK----------RyknRELQIMRRLK-HPNIVKLKYFFys 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 216 --EDNANVY--IVMElCGGGELLDRILarggKYSEDDAK--AVLI-----QILNVVAFCHLQGVVHRDLKPENFLYtsKE 284
Cdd:cd14137  69 sgEKKDEVYlnLVME-YMPETLYRVIR----HYSKNKQTipIIYVklysyQLFRGLAYLHSLGICHRDIKPQNLLV--DP 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 285 ENSMLKVIDFGLSDFVRPDERLNDIVGSAYYVAPEVLHRS--YTTEADVWSIG-VIAYILLcgSRP-FWARTESGIFRAV 360
Cdd:cd14137 142 ETGVLKLCDFGSAKRLVPGEPNVSYICSRYYRAPELIFGAtdYTTAIDIWSAGcVLAELLL--GQPlFPGESSVDQLVEI 219
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15230288 361 LKA--DPSFDE------------------PPW-----PSLSFEAKDFVKRLLYKDPRKRMTASQALMHP 404
Cdd:cd14137 220 IKVlgTPTREQikamnpnytefkfpqikpHPWekvfpKRTPPDAIDLLSKILVYNPSKRLTALEALAHP 288
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
147-406 1.94e-29

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: 117.25  E-value: 1.94e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 147 GEEIGRGHFG--YTCSAKFKkGELkdqeVAVKVI------PKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDN 218
Cdd:cd06628   5 GALIGSGSFGsvYLGMNASS-GEL----MAVKQVelpsvsAENKDRKKSMLDALQREIALLRELQ-HENIVQYLGSSSDA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 219 ANVYIVMELCGGGELlDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGLSD 298
Cdd:cd06628  79 NHLNIFLEYVPGGSV-ATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNK---GGIKISDFGISK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 299 FVRPDeRLN--------DIVGSAYYVAPEVLHR-SYTTEADVWSIGVIAYILLCGSRPFWARTE-SGIFRAVLKADPsfd 368
Cdd:cd06628 155 KLEAN-SLStknngarpSLQGSVFWMAPEVVKQtSYTRKADIWSLGCLVVEMLTGTHPFPDCTQmQAIFKIGENASP--- 230
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 15230288 369 EPPwPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd06628 231 TIP-SNISSEARDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
145-407 2.06e-29

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: 118.21  E-value: 2.06e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKK-GELkdqeVAVKVIpksKMTSAISIEDVRREVKILrALSGHQNLVQFYDAFEDNANVYI 223
Cdd:cd06644  15 EIIGELGDGAFGKVYKAKNKEtGAL----AAAKVI---ETKSEEELEDYMVEIEIL-ATCNHPYIVKLLGAFYWDGKLWI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsmLKVIDFGLS-DFVRP 302
Cdd:cd06644  87 MIEFCPGGAVDAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGD---IKLADFGVSaKNVKT 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 303 DERLNDIVGSAYYVAPEVL------HRSYTTEADVWSIGvIAYILLCGSRPfwARTESGIFRAVLKADPSfdEPP---WP 373
Cdd:cd06644 164 LQRRDSFIGTPYWMAPEVVmcetmkDTPYDYKADIWSLG-ITLIEMAQIEP--PHHELNPMRVLLKIAKS--EPPtlsQP 238
                       250       260       270
                ....*....|....*....|....*....|....*
gi 15230288 374 S-LSFEAKDFVKRLLYKDPRKRMTASQALMHPWIA 407
Cdd:cd06644 239 SkWSMEFRDFLKTALDKHPETRPSAAQLLEHPFVS 273
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
141-406 2.16e-29

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: 116.85  E-value: 2.16e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 141 QSRIELGEEIGRGHFGYTcsaKFKKGELKDQEVAVKVIPKSKMTSaisiEDVRREVKILRALSgHQNLVQFYDAFEDNAN 220
Cdd:cd14111   2 QKPYTFLDEKARGRFGVI---RRCRENATGKNFPAKIVPYQAEEK----QGVLQEYEILKSLH-HERIMALHEAYITPRY 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 VYIVMELCGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSDFV 300
Cdd:cd14111  74 LVLIAEFCSGKELLHSLIDRF-RYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTN---LNAIKIVDFGSAQSF 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 301 RPD--ERLNDIVGSAYYVAPEVLHRSYT-TEADVWSIGVIAYILLCGSRPFWAR----TESGIFRAvlKADPSfdePPWP 373
Cdd:cd14111 150 NPLslRQLGRRTGTLEYMAPEMVKGEPVgPPADIWSIGVLTYIMLSGRSPFEDQdpqeTEAKILVA--KFDAF---KLYP 224
                       250       260       270
                ....*....|....*....|....*....|...
gi 15230288 374 SLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14111 225 NVSQSASLFLKKVLSSYPWSRPTTKDCFAHAWL 257
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
188-399 2.47e-29

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: 117.05  E-value: 2.47e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 188 SIEDVRREVKILRALSGHQNLVQFYD-AFEDNAN---VYIVMELCgGGELLDRILARGGKY-SEDDAKAVLIQILNVVAF 262
Cdd:cd13985  40 QLRVAIKEIEIMKRLCGHPNIVQYYDsAILSSEGrkeVLLLMEYC-PGSLVDILEKSPPSPlSEEEVLRIFYQICQAVGH 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 263 CHLQG--VVHRDLKPENFLYTSKEEnsmLKVIDFG-LSDFVRPDERLNDIV---------GSAYYVAPEV--LHRSY--T 326
Cdd:cd13985 119 LHSQSppIIHRDIKIENILFSNTGR---FKLCDFGsATTEHYPLERAEEVNiieeeiqknTTPMYRAPEMidLYSKKpiG 195
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15230288 327 TEADVWSIGVIAYILLCGSRPFwarTESGIFRAVlkaDPSFDEPPWPSLSFEAKDFVKRLLYKDPRKRMTASQ 399
Cdd:cd13985 196 EKADIWALGCLLYKLCFFKLPF---DESSKLAIV---AGKYSIPEQPRYSPELHDLIRHMLTPDPAERPDIFQ 262
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
148-405 2.92e-29

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 117.47  E-value: 2.92e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFG--YTCSAKfKKGELkdqeVAVK---------VIPKSKMtsaisiedvrREVKILRALSgHQNLVQFYDAFE 216
Cdd:cd07847   7 SKIGEGSYGvvFKCRNR-ETGQI----VAIKkfveseddpVIKKIAL----------REIRMLKQLK-HPNLVNLIEVFR 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 217 DNANVYIVMELCGGgELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGL 296
Cdd:cd07847  71 RKRKLHLVFEYCDH-TVLNELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILIT---KQGQIKLCDFGF 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 297 SDFV-RPDERLNDIVGSAYYVAPEVL--HRSYTTEADVWSIGVIAYILLCGsRPFWA------------RT--------- 352
Cdd:cd07847 147 ARILtGPGDDYTDYVATRWYRAPELLvgDTQYGPPVDVWAIGCVFAELLTG-QPLWPgksdvdqlylirKTlgdliprhq 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 353 ----ESGIFRAVLKADPSFDEP---PWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd07847 226 qifsTNQFFKGLSIPEPETREPlesKFPNISSPALSFLKGCLQMDPTERLSCEELLEHPY 285
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
150-417 5.97e-29

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: 117.83  E-value: 5.97e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKGELKdqeVAVKVIPKSkMTSAISIEDVRREVKILRALSgHQNLVQFYDAF------EDNANVYI 223
Cdd:cd07877  25 VGSGAYGSVCAAFDTKTGLR---VAVKKLSRP-FQSIIHAKRTYRELRLLKHMK-HENVIGLLDVFtparslEEFNDVYL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGelLDRILaRGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFlytSKEENSMLKVIDFGLSDFVrpD 303
Cdd:cd07877 100 VTHLMGAD--LNNIV-KCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNL---AVNEDCELKILDFGLARHT--D 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ERLNDIVGSAYYVAPEVLHR--SYTTEADVWSIGVIAYILLCGsRPFWARTE-----SGIFRAVLKADPSFDE------- 369
Cdd:cd07877 172 DEMTGYVATRWYRAPEIMLNwmHYNQTVDIWSVGCIMAELLTG-RTLFPGTDhidqlKLILRLVGTPGAELLKkissesa 250
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15230288 370 -------PPWPSLSFE---------AKDFVKRLLYKDPRKRMTASQALMHPWIAGYKKIDI-----PFD 417
Cdd:cd07877 251 rnyiqslTQMPKMNFAnvfiganplAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPDDepvadPYD 319
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
150-413 8.96e-29

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: 116.00  E-value: 8.96e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKGElkdQEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd05612   9 IGTGTFGRVHLVRDRISE---HYYALKVMAIPEVIRLKQEQHVHNEKRVLKEVS-HPFIIRLFWTEHDQRFLYMLMEYVP 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLyTSKEENsmLKVIDFGLSDFVRpdERLNDI 309
Cdd:cd05612  85 GGELFSYLRNSG-RFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENIL-LDKEGH--IKLTDFGFAKKLR--DRTWTL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 310 VGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEppwpSLSFEAKDFVKRLLY 388
Cdd:cd05612 159 CGTPEYLAPEVIQSKgHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFPR----HLDLYAKDLIKKLLV 234
                       250       260       270
                ....*....|....*....|....*....|
gi 15230288 389 KDPRKRM-----TASQALMHPWiagYKKID 413
Cdd:cd05612 235 VDRTRRLgnmknGADDVKNHRW---FKSVD 261
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
145-394 1.06e-28

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: 115.29  E-value: 1.06e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGytCSAKFKKGELKDQEVAVKVI-------PKSKMTSAISIEDVRREVKILRALSGHQNLVQFYDAFED 217
Cdd:cd08528   3 AVLELLGSGAFG--CVYKVRKKSNGQTLLALKEInmtnpafGRTEQERDKSVGDIISEVNIIKEQLRHPNIVRYYKTFLE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 218 NANVYIVMELCGG---GELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQ-GVVHRDLKPENFLYTskeENSMLKVID 293
Cdd:cd08528  81 NDRLYIVMELIEGaplGEHFSSLKEKNEHFTEDRIWNIFVQMVLALRYLHKEkQIVHRDLKPNNIMLG---EDDKVTITD 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 294 FGLSDFVRPDE-RLNDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADpsFDEPP 371
Cdd:cd08528 158 FGLAKQKGPESsKMTSVVGTILYSCPEIVqNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAE--YEPLP 235
                       250       260
                ....*....|....*....|...
gi 15230288 372 WPSLSFEAKDFVKRLLYKDPRKR 394
Cdd:cd08528 236 EGMYSDDITFVIRSCLTPDPEAR 258
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
143-419 1.61e-28

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: 117.44  E-value: 1.61e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGE-----EIGRGHFGYTCSAKfKK--GELkdqeVAVKVIPKSKMTSAISIEDVRREVKILrALSGHQNLVQFYDAF 215
Cdd:cd05600   7 RLKLSDfqiltQVGQGGYGSVFLAR-KKdtGEI----CALKIMKKKVLFKLNEVNHVLTERDIL-TTTNSPWLVKLLYAF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 216 EDNANVYIVMELCGGGELldR-ILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDF 294
Cdd:cd05600  81 QDPENVYLAMEYVPGGDF--RtLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSS---GHIKLTDF 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 295 GLSD-----------FVRPDE---------------------------RLNDIVGSAYYVAPEVLH-RSYTTEADVWSIG 335
Cdd:cd05600 156 GLASgtlspkkiesmKIRLEEvkntafleltakerrniyramrkedqnYANSVVGSPDYMAPEVLRgEGYDLTVDYWSLG 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 336 VIAYILLCGSRPFWARTESGIF------RAVLKAdPSFDEPPW-PSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWiag 408
Cdd:cd05600 236 CILFECLVGFPPFSGSTPNETWanlyhwKKTLQR-PVYTDPDLeFNLSDEAWDLITKLITDPQDRLQSPEQIKNHPF--- 311
                       330
                ....*....|.
gi 15230288 409 YKKIDipFDIL 419
Cdd:cd05600 312 FKNID--WDRL 320
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
148-403 1.85e-28

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: 114.77  E-value: 1.85e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEI---GRGHFGYTCSAKFKkgeLKDQEVAVKVIPKSKMTSAISieDVRREVKILRALSgHQNLVQFYDAFEDNANVYIV 224
Cdd:cd14046   9 EELqvlGKGAFGQVVKVRNK---LDGRYYAIKKIKLRSESKNNS--RILREVMLLSRLN-HQHVVRYYQAWIERANLYIQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGELLDRIlaRGGKYSEDDAKAVLI-QILNVVAFCHLQGVVHRDLKPEN-FLytskEENSMLKVIDFGLSDFVR- 301
Cdd:cd14046  83 MEYCEKSTLRDLI--DSGLFQDTDRLWRLFrQILEGLAYIHSQGIIHRDLKPVNiFL----DSNGNVKIGDFGLATSNKl 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 302 ------------------PDERLNDIVGSAYYVAPEVL---HRSYTTEADVWSIGVIAYILlcgsrpfWARTESGIFRA- 359
Cdd:cd14046 157 nvelatqdinkstsaalgSSGDLTGNVGTALYVAPEVQsgtKSTYNEKVDMYSLGIIFFEM-------CYPFSTGMERVq 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 15230288 360 VLKA--DPSFDEPP-WP-SLSFEAKDFVKRLLYKDPRKRMTASQALMH 403
Cdd:cd14046 230 ILTAlrSVSIEFPPdFDdNKHSKQAKLIRWLLNHDPAKRPSAQELLKS 277
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
146-395 2.03e-28

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: 116.18  E-value: 2.03e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 146 LGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIVM 225
Cdd:cd05619   9 LHKMLGKGSFGKVFLAELKG---TNQFFAIKALKKDVVLMDDDVECTMVEKRVLSLAWEHPFLTHLFCTFQTKENLFFVM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 226 ELCGGGELLDRILArGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGL-SDFVRPDE 304
Cdd:cd05619  86 EYLNGGDLMFHIQS-CHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILL---DKDGHIKIADFGMcKENMLGDA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 305 RLNDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFdePPWpsLSFEAKDFV 383
Cdd:cd05619 162 KTSTFCGTPDYIAPEILlGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRMDNPFY--PRW--LEKEAKDIL 237
                       250
                ....*....|..
gi 15230288 384 KRLLYKDPRKRM 395
Cdd:cd05619 238 VKLFVREPERRL 249
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
170-417 2.25e-28

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: 116.42  E-value: 2.25e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 170 DQEVAVKvipKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAF--------EDNANVYIVMELCGGGELLDRILAR- 240
Cdd:cd07854  30 DKRVAVK---KIVLTDPQSVKHALREIKIIRRLD-HDNIVKVYEVLgpsgsdltEDVGSLTELNSVYIVQEYMETDLANv 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 241 --GGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeENSMLKVIDFGLSDFVRPDER----LNDIVGSAY 314
Cdd:cd07854 106 leQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINT--EDLVLKIGDFGLARIVDPHYShkgyLSEGLVTKW 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 315 YVAPEVL--HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPP--------------------- 371
Cdd:cd07854 184 YRSPRLLlsPNNYTKAIDMWAAGCIFAEMLTGKPLFAGAHELEQMQLILESVPVVREEDrnellnvipsfvrndggeprr 263
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 15230288 372 -----WPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWIAGYKkidIPFD 417
Cdd:cd07854 264 plrdlLPGVNPEALDFLEQILTFNPMDRLTAEEALMHPYMSCYS---CPFD 311
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
145-406 2.43e-28

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: 114.68  E-value: 2.43e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTcsaKFKKGELKDQEVAVKVIPKSKMTSAIS-----------------------IEDVRREVKILRA 201
Cdd:cd14199   5 KLKDEIGKGSYGVV---KLAYNEDDNTYYAMKVLSKKKLMRQAGfprrppprgaraapegctqprgpIERVYQEIAILKK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 202 LSgHQNLVQFYDAFEDNA--NVYIVMELCGGGELLDriLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFL 279
Cdd:cd14199  82 LD-HPNVVKLVEVLDDPSedHLYMVFELVKQGPVME--VPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 280 YTskeENSMLKVIDFGLSD-FVRPDERLNDIVGSAYYVAPEVL---HRSYTTEA-DVWSIGVIAYILLCGSRPFW-ARTE 353
Cdd:cd14199 159 VG---EDGHIKIADFGVSNeFEGSDALLTNTVGTPAFMAPETLsetRKIFSGKAlDVWAMGVTLYCFVFGQCPFMdERIL 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 15230288 354 SgiFRAVLKADPsFDEPPWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14199 236 S--LHSKIKTQP-LEFPDQPDISDDLKDLLFRMLDKNPESRISVPEIKLHPWV 285
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
150-406 2.52e-28

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: 114.06  E-value: 2.52e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYtcSAKFKKGElKDQEVAVKVIPKSKMTSAISiEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd08221   8 LGRGAFGE--AVLYRKTE-DNSLVVWKEVNLSRLSEKER-RDALNEIDILSLLN-HDNIITYYNHFLDGESLFIEMEYCN 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRILARGGK-YSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEensMLKVIDFGLSDFVRPDERLND 308
Cdd:cd08221  83 GGNLHDKIAQQKNQlFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKAD---LVKLGDFGISKVLDSESSMAE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 309 -IVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWpslSFEAKDFVKRL 386
Cdd:cd08221 160 sIVGTPYYMSPELVQgVKYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQGEYEDIDEQY---SEEIIQLVHDC 236
                       250       260
                ....*....|....*....|
gi 15230288 387 LYKDPRKRMTASQALMHPWI 406
Cdd:cd08221 237 LHQDPEDRPTAEELLERPLL 256
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
149-406 4.75e-28

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: 113.31  E-value: 4.75e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 149 EIGRGHFGYTCSAKFKKGElkdQEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELC 228
Cdd:cd06607   8 EIGHGSFGAVYYARNKRTS---EVVAIKKMSYSGKQSTEKWQDIIKEVKFLRQLR-HPNTIEYKGCYLREHTAWLVMEYC 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 229 GGG-----ELLDRILarggkySEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFVRPd 303
Cdd:cd06607  84 LGSasdivEVHKKPL------QEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLT---EPGTVKLADFGSASLVCP- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 erLNDIVGSAYYVAPEVL----HRSYTTEADVWSIGvIAYILLCGSRP--FWARTESGIFRAVLKADPSFDEPPWpSLSF 377
Cdd:cd06607 154 --ANSFVGTPYWMAPEVIlamdEGQYDGKVDVWSLG-ITCIELAERKPplFNMNAMSALYHIAQNDSPTLSSGEW-SDDF 229
                       250       260
                ....*....|....*....|....*....
gi 15230288 378 eaKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd06607 230 --RNFVDSCLQKIPQDRPSAEDLLKHPFV 256
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
145-406 7.36e-28

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: 112.89  E-value: 7.36e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEI--GRGHFGYTCSAKfkkgELKDQ-EVAVKVIPKSKMTSAISIEDvrrEVKILRALSgHQNLVQFYDAFEDNANV 221
Cdd:cd06624   9 ESGERVvlGKGTFGVVYAAR----DLSTQvRIAIKEIPERDSREVQPLHE---EIALHSRLS-HKNIVQYLGSVSEDGFF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 YIVMELCGGGELLDRILARGG--KYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeeNSMLKVIDFGLSdf 299
Cdd:cd06624  81 KIFMEQVPGGSLSALLRSKWGplKDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTY--SGVVKISDFGTS-- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 300 vrpdERLNDI-------VGSAYYVAPEVL---HRSYTTEADVWSIGVIAYILLCGSRPFW--ARTESGIFR-AVLKADPS 366
Cdd:cd06624 157 ----KRLAGInpctetfTGTLQYMAPEVIdkgQRGYGPPADIWSLGCTIIEMATGKPPFIelGEPQAAMFKvGMFKIHPE 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 15230288 367 FDEppwpSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd06624 233 IPE----SLSEEAKSFILRCFEPDPDKRATASDLLQDPFL 268
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
150-407 1.05e-27

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: 114.00  E-value: 1.05e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKfkkGELKDQEVAVKVIPKSkMTSAISIEDVRREVKILRALSgHQNLVQFYD--------AFEDnanV 221
Cdd:cd07858  13 IGRGAYGIVCSAK---NSETNEKVAIKKIANA-FDNRIDAKRTLREIKLLRHLD-HENVIAIKDimppphreAFND---V 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 YIVMELCGGGelLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSdfvR 301
Cdd:cd07858  85 YIVYELMDTD--LHQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNA---NCDLKICDFGLA---R 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 302 P----DERLNDIVGSAYYVAPEVLHRS--YTTEADVWSIGVIAYILLcGSRPFWARTES----GIFRAVLkADPSFDE-- 369
Cdd:cd07858 157 TtsekGDFMTEYVVTRWYRAPELLLNCseYTTAIDVWSVGCIFAELL-GRKPLFPGKDYvhqlKLITELL-GSPSEEDlg 234
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15230288 370 --------------PPWPSLSFEAK---------DFVKRLLYKDPRKRMTASQALMHPWIA 407
Cdd:cd07858 235 firnekarryirslPYTPRQSFARLfphanplaiDLLEKMLVFDPSKRITVEEALAHPYLA 295
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
150-425 1.14e-27

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: 113.74  E-value: 1.14e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd05591   3 LGKGSFGKVMLAERKG---TDEVYAIKVLKKDVILQDDDVDCTMTEKRILALAAKHPFLTALHSCFQTKDRLFFVMEYVN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRIlARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGL-SDFVRPDERLND 308
Cdd:cd05591  80 GGDLMFQI-QRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAE---GHCKLADFGMcKEGILNGKTTTT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 309 IVGSAYYVAPEVLHR-SYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFdePPWpsLSFEAKDFVKRLL 387
Cdd:cd05591 156 FCGTPDYIAPEILQElEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLY--PVW--LSKEAVSILKAFM 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 15230288 388 YKDPRKRM--TASQA-----LMHPWiagYKKIDipFDILIFKQIK 425
Cdd:cd05591 232 TKNPAKRLgcVASQGgedaiRQHPF---FREID--WEALEQRKVK 271
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
142-414 1.37e-27

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: 112.63  E-value: 1.37e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 142 SRIELGEEIGRGHFGYTCSAKFKKGELKdqeVAVKVIPKSKMTSAISieDVRREVKIL-RALSGHqnLVQFYDAFEDNAN 220
Cdd:cd06622   1 DEIEVLDELGKGNYGSVYKVLHRPTGVT---MAMKEIRLELDESKFN--QIIMELDILhKAVSPY--IVDFYGAFFIEGA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 VYIVMELCGGGELlDRILArGGKYSEDDAKAVLIQILNVVafchLQG---------VVHRDLKPENFLYTSKEEnsmLKV 291
Cdd:cd06622  74 VYMCMEYMDAGSL-DKLYA-GGVATEGIPEDVLRRITYAV----VKGlkflkeehnIIHRDVKPTNVLVNGNGQ---VKL 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 292 IDFGLS-DFVRPDERLNdiVGSAYYVAPEVLHR-------SYTTEADVWSIGVIAYILLCGSRPFWARTESGIFrAVLKA 363
Cdd:cd06622 145 CDFGVSgNLVASLAKTN--IGCQSYMAPERIKSggpnqnpTYTVQSDVWSLGLSILEMALGRYPYPPETYANIF-AQLSA 221
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 15230288 364 DPSFDEPPWPS-LSFEAKDFVKRLLYKDPRKRMTASQALMHPWIAGYKKIDI 414
Cdd:cd06622 222 IVDGDPPTLPSgYSDDAQDFVAKCLNKIPNRRPTYAQLLEHPWLVKYKNADV 273
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
143-404 1.63e-27

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: 112.13  E-value: 1.63e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFGYTCSAKFKKgeLKDQEVAVKVIpKSKMTSAISIEDVRREVKILRALS--GHQNLVQFYDAFEDNAN 220
Cdd:cd14052   1 RFANVELIGSGEFSQVYKVSERV--PTGKVYAVKKL-KPNYAGAKDRLRRLEEVSILRELTldGHDNIVQLIDSWEYHGH 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 VYIVMELCGGGELlDRILARGGKYSE-DDAKA--VLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLS 297
Cdd:cd14052  78 LYIQTELCENGSL-DVFLSELGLLGRlDEFRVwkILVELSLGLRFIHDHHFVHLDLKPANVLIT---FEGTLKIGDFGMA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 298 DfVRPDERLNDIVGSAYYVAPEVL-HRSYTTEADVWSIGVI-----AYILLCGSRPFWARTESG---------IFRAVLK 362
Cdd:cd14052 154 T-VWPLIRGIEREGDREYIAPEILsEHMYDKPADIFSLGLIlleaaANVVLPDNGDAWQKLRSGdlsdaprlsSTDLHSA 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 15230288 363 ADPSFDEPPWPSLSFEAKD----FVKRLLYKDPRKRMTASQALMHP 404
Cdd:cd14052 233 SSPSSNPPPDPPNMPILSGsldrVVRWMLSPEPDRRPTADDVLATP 278
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
145-406 1.87e-27

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: 112.02  E-value: 1.87e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAK-FKKGELkdqeVAVKVIPKSKMTSaisiEDVRREVKILRALSGHQNLVQFYDAFEDNA---- 219
Cdd:cd06636  19 ELVEVVGNGTYGQVYKGRhVKTGQL----AAIKVMDVTEDEE----EEIKLEINMLKKYSHHRNIATYYGAFIKKSppgh 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 220 --NVYIVMELCGGGELLDRIL-ARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGL 296
Cdd:cd06636  91 ddQLWLVMEFCGAGSVTDLVKnTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT---ENAEVKLVDFGV 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 297 S-DFVRPDERLNDIVGSAYYVAPEVL------HRSYTTEADVWSIGVIAYIL------LCGSRPFWArtesgIFRAVLKA 363
Cdd:cd06636 168 SaQLDRTVGRRNTFIGTPYWMAPEVIacdenpDATYDYRSDIWSLGITAIEMaegappLCDMHPMRA-----LFLIPRNP 242
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 15230288 364 DPSFDEPPWPSLSFeakDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd06636 243 PPKLKSKKWSKKFI---DFIEGCLVKNYLSRPSTEQLLKHPFI 282
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
145-406 2.53e-27

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: 112.01  E-value: 2.53e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFG--YTCSAKfKKGELkdqeVAVKVI-PKSKMTsaisiEDVRREVKILRALSGHQNLVQFYDAFED---- 217
Cdd:cd06639  25 DIIETIGKGTYGkvYKVTNK-KDGSL----AAVKILdPISDVD-----EEIEAEYNILRSLPNHPNVVKFYGMFYKadqy 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 218 -NANVYIVMELCGGG---ELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVID 293
Cdd:cd06639  95 vGGQLWLVLELCNGGsvtELVKGLLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTE---GGVKLVD 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 294 FGLS-DFVRPDERLNDIVGSAYYVAPEVL------HRSYTTEADVWSIGVIAYILLCGSRP-FWARTESGIFRAVLKADP 365
Cdd:cd06639 172 FGVSaQLTSARLRRNTSVGTPFWMAPEVIaceqqyDYSYDARCDVWSLGITAIELADGDPPlFDMHPVKALFKIPRNPPP 251
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15230288 366 SFDEPPWPSLSFeaKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd06639 252 TLLNPEKWCRGF--SHFISQCLIKDFEKRPSVTHLLEHPFI 290
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
148-405 2.84e-27

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: 111.83  E-value: 2.84e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKFKK-GELkdqeVAVKVIPKSKMTSAISIEDVRrEVKILRALSgHQNLVQFYDAFEDNANVYIVME 226
Cdd:cd07860   6 EKIGEGTYGVVYKARNKLtGEV----VALKKIRLDTETEGVPSTAIR-EISLLKELN-HPNIVKLLDVIHTENKLYLVFE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 227 LCGggELLDRIL--ARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLSD-FVRPD 303
Cdd:cd07860  80 FLH--QDLKKFMdaSALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLI---NTEGAIKLADFGLARaFGVPV 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ERLNDIVGSAYYVAPEVL--HRSYTTEADVWSIGVIAYILLCGSRPFWARTESG----IFRAVLKAD------------- 364
Cdd:cd07860 155 RTYTHEVVTLWYRAPEILlgCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDqlfrIFRTLGTPDevvwpgvtsmpdy 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 15230288 365 -PSFdePPW---------PSLSFEAKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd07860 235 kPSF--PKWarqdfskvvPPLDEDGRDLLSQMLHYDPNKRISAKAALAHPF 283
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
150-423 3.07e-27

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: 112.80  E-value: 3.07e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKfKKGelKDQEVAVKVIPKSKMTSAISIEDVRREVKILrALSGHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd05598   9 IGVGAFGEVSLVR-KKD--TNALYAMKTLRKKDVLKRNQVAHVKAERDIL-AEADNEWVVKLYYSFQDKENLYFVMDYIP 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDrILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLSDFVR--PDERL- 306
Cdd:cd05598  85 GGDLMS-LLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILI---DRDGHIKLTDFGLCTGFRwtHDSKYy 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 307 --NDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDFV 383
Cdd:cd05598 161 laHSLVGTPNYIAPEVLLRTgYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKVINWRTTLKIPHEANLSPEAKDLI 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 15230288 384 KRLLyKDPRKRM---TASQALMHPWIAGykkidIPFDILIFKQ 423
Cdd:cd05598 241 LRLC-CDAEDRLgrnGADEIKAHPFFAG-----IDWEKLRKQK 277
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
150-424 3.65e-27

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: 112.66  E-value: 3.65e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIEDVRREVKIL--RALSGHQNLVQFYDAFEDNANVYIVMEL 227
Cdd:cd05586   1 IGKGTFGQVYQVRKKD---TRRIYAMKVLSKKVIVAKKEVAHTIGERNILvrTALDESPFIVGLKFSFQTPTDLYLVTDY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 228 CGGGELLDRiLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLSDF-VRPDERL 306
Cdd:cd05586  78 MSGGELFWH-LQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILL---DANGHIALCDFGLSKAdLTDNKTT 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 307 NDIVGSAYYVAPEVL--HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFdepPWPSLSFEAKDFVK 384
Cdd:cd05586 154 NTFCGTTEYLAPEVLldEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRF---PKDVLSDEGRSFVK 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15230288 385 RLLYKDPRKRMTA----SQALMHPWIAgykkiDIPFDILIFKQI 424
Cdd:cd05586 231 GLLNRNPKHRLGAhddaVELKEHPFFA-----DIDWDLLSKKKI 269
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
150-416 3.87e-27

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: 112.06  E-value: 3.87e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKK-GELkdqeVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELC 228
Cdd:cd05571   3 LGKGTFGKVILCREKAtGEL----YAIKILKKEVIIAKDEVAHTLTENRVLQNTR-HPFLTSLKYSFQTNDRLCFVMEYV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 229 GGGELLDRiLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGL-SDFVRPDERLN 307
Cdd:cd05571  78 NGGELFFH-LSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLL---DKDGHIKITDFGLcKEEISYGATTK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 308 DIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFdePpwPSLSFEAKDFVKRL 386
Cdd:cd05571 154 TFCGTPEYLAPEVLEDNdYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRF--P--STLSPEAKSLLAGL 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 15230288 387 LYKDPRKRM-----TASQALMHPWIAGY-------KKIDIPF 416
Cdd:cd05571 230 LKKDPKKRLgggprDAKEIMEHPFFASInwddlyqKKIPPPF 271
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
150-425 4.46e-27

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: 112.01  E-value: 4.46e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKK-GELkdqeVAVKVIPKSKMTSAISIEDVRREVKILRALS--GHQNLVQFYDAFEDNANVYIVME 226
Cdd:cd05589   7 LGRGHFGKVLLAEYKPtGEL----FAIKALKKGDIIARDEVESLMCEKRIFETVNsaRHPFLVNLFACFQTPEHVCFVME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 227 LCGGGELLDRILA------RGGKYSeddAKAVL-IQilnvvaFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGL-SD 298
Cdd:cd05589  83 YAAGGDLMMHIHEdvfsepRAVFYA---ACVVLgLQ------FLHEHKIVYRDLKLDNLLLDTE---GYVKIADFGLcKE 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 299 FVRPDERLNDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKadpsfDEPPWPS-LS 376
Cdd:cd05589 151 GMGFGDRTSTFCGTPEFLAPEVLtDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVN-----DEVRYPRfLS 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 15230288 377 FEAKDFVKRLLYKDPRKRMTASQ-----ALMHPWiagYKKIDipFDILIFKQIK 425
Cdd:cd05589 226 TEAISIMRRLLRKNPERRLGASErdaedVKKQPF---FRNID--WEALLARKIK 274
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
150-416 4.78e-27

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: 112.02  E-value: 4.78e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIEDVRREVKILRAlSGHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd05595   3 LGKGTFGKVILVREKA---TGRYYAMKILRKEVIIAKDEVAHTVTESRVLQN-TRHPFLTALKYAFQTHDRLCFVMEYAN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRiLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGL-SDFVRPDERLND 308
Cdd:cd05595  79 GGELFFH-LSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLML---DKDGHIKITDFGLcKEGITDGATMKT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 309 IVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEppwpSLSFEAKDFVKRLL 387
Cdd:cd05595 155 FCGTPEYLAPEVLEdNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPR----TLSPEAKSLLAGLL 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15230288 388 YKDPRKRM-----TASQALMHPWIAGY-------KKIDIPF 416
Cdd:cd05595 231 KKDPKQRLgggpsDAKEVMEHRFFLSInwqdvvqKKLLPPF 271
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
150-426 5.21e-27

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: 111.71  E-value: 5.21e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd05592   3 LGKGSFGKVMLAELKG---TNQYFAIKALKKDVVLEDDDVECTMIERRVLALASQHPFLTHLFCTFQTESHLFFVMEYLN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRIlARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGL-SDFVRPDERLND 308
Cdd:cd05592  80 GGDLMFHI-QQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLL---DREGHIKIADFGMcKENIYGENKAST 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 309 IVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFdePPWpsLSFEAKDFVKRLL 387
Cdd:cd05592 156 FCGTPDYIAPEILKgQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPHY--PRW--LTKEAASCLSLLL 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15230288 388 YKDPRKRM-----TASQALMHPWiagYKKIDipFDILIFKQIKA 426
Cdd:cd05592 232 ERNPEKRLgvpecPAGDIRDHPF---FKTID--WDKLERREIDP 270
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
150-405 6.27e-27

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: 110.11  E-value: 6.27e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKmtsaISIEDVRREVKILRALSGHQNLVQFYD-AFEDNANVYIVMELC 228
Cdd:cd13987   1 LGEGTYGKVLLAVHKG---SGTKMALKFVPKPS----TKLKDFLREYNISLELSVHPHIIKTYDvAFETEDYYVFAQEYA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 229 GGGELLDRILARGGkYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPEN-FLYTSkeENSMLKVIDFGLSDfvRPDERLN 307
Cdd:cd13987  74 PYGDLFSIIPPQVG-LPEERVKRCAAQLASALDFMHSKNLVHRDIKPENvLLFDK--DCRRVKLCDFGLTR--RVGSTVK 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 308 DIVGSAYYVAPEVL----HRSYTTE--ADVWSIGVIAYILLCGSRPfWARTESgifravlkADPSFDE-----------P 370
Cdd:cd13987 149 RVSGTIPYTAPEVCeakkNEGFVVDpsIDVWAFGVLLFCCLTGNFP-WEKADS--------DDQFYEEfvrwqkrkntaV 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 15230288 371 P--WPSLSFEAKDFVKRLLYKDPRKRMTASQA---LMHPW 405
Cdd:cd13987 220 PsqWRRFTPKALRMFKKLLAPEPERRCSIKEVfkyLGDRW 259
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
194-405 6.93e-27

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: 110.65  E-value: 6.93e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 194 REVKILRALSgHQNLVQFYDAFEDNANVYIVMELCGGgELLDRILARG--GKYSEDDAKAVLIQILNVVAFCHLQGVVHR 271
Cdd:cd07836  47 REISLMKELK-HENIVRLHDVIHTENKLMLVFEYMDK-DLKKYMDTHGvrGALDPNTVKSFTYQLLKGIAFCHENRVLHR 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 272 DLKPENFLYTSKEEnsmLKVIDFGLS-DFVRPDERLNDIVGSAYYVAPEVL--HRSYTTEADVWSIGVIAYILLCGSRPF 348
Cdd:cd07836 125 DLKPQNLLINKRGE---LKLADFGLArAFGIPVNTFSNEVVTLWYRAPDVLlgSRTYSTSIDIWSVGCIMAEMITGRPLF 201
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 349 WARTESG----IFRAV----------LKADPSF--DEPPWPSLSFE---------AKDFVKRLLYKDPRKRMTASQALMH 403
Cdd:cd07836 202 PGTNNEDqllkIFRIMgtptestwpgISQLPEYkpTFPRYPPQDLQqlfphadplGIDLLHRLLQLNPELRISAHDALQH 281

                ..
gi 15230288 404 PW 405
Cdd:cd07836 282 PW 283
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
150-404 1.12e-26

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: 108.94  E-value: 1.12e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKgelKDQEVAVKVIP---KSKMTSAISIEDVRREVKIlralSGHQNLVQFYDAFEDNANVYIVME 226
Cdd:cd14050   9 LGEGSFGEVFKVRSRE---DGKLYAVKRSRsrfRGEKDRKRKLEEVERHEKL----GEHPNCVRFIKAWEEKGILYIQTE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 227 LCGGGelLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFVRPDERL 306
Cdd:cd14050  82 LCDTS--LQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLS---KDGVCKLGDFGLVVELDKEDIH 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 307 NDIVGSAYYVAPEVLHRSYTTEADVWSIG-----VIAYILLCGSRPFWARTESGIFravlkadpsfdepPWP---SLSFE 378
Cdd:cd14050 157 DAQEGDPRYMAPELLQGSFTKAADIFSLGitileLACNLELPSGGDGWHQLRQGYL-------------PEEftaGLSPE 223
                       250       260
                ....*....|....*....|....*.
gi 15230288 379 AKDFVKRLLYKDPRKRMTASQALMHP 404
Cdd:cd14050 224 LRSIIKLMMDPDPERRPTAEDLLALP 249
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
145-406 1.15e-26

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 109.27  E-value: 1.15e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGyTCSAKFKKGElkDQEVAVKVIPKSKMTSAISIEDVR--REVKILRAL-SGHQNLVQFYDAFEDNANV 221
Cdd:cd14102   3 QVGSVLGSGGFG-TVYAGSRIAD--GLPVAVKHVVKERVTEWGTLNGVMvpLEIVLLKKVgSGFRGVIKLLDWYERPDGF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 YIVMELCG-GGELLDRILARGGkYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeeNSMLKVIDFGlSDFV 300
Cdd:cd14102  80 LIVMERPEpVKDLFDFITEKGA-LDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLR--TGELKLIDFG-SGAL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 301 RPDERLNDIVGSAYYVAPEVL--HRSYTTEADVWSIGVIAYILLCGSRPFWARTEsgifraVLKADPSFDEppwpSLSFE 378
Cdd:cd14102 156 LKDTVYTDFDGTRVYSPPEWIryHRYHGRSATVWSLGVLLYDMVCGDIPFEQDEE------ILRGRLYFRR----RVSPE 225
                       250       260
                ....*....|....*....|....*...
gi 15230288 379 AKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14102 226 CQQLIKWCLSLRPSDRPTLEQIFDHPWM 253
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
173-418 1.39e-26

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: 109.84  E-value: 1.39e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 173 VAVKVIP---KSKMTSAISiedvrREVKILRALSgHQNLVQFYDAF-EDNANVYIVMELCGGGELlDRILARGGKYSEDd 248
Cdd:cd06620  33 MAKKVIHidaKSSVRKQIL-----RELQILHECH-SPYIVSFYGAFlNENNNIIICMEYMDCGSL-DKILKKKGPFPEE- 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 249 akavliqILNVVAFCHLQG---------VVHRDLKPENFLYTSKEEnsmLKVIDFGLSDfvrpdERLNDI----VGSAYY 315
Cdd:cd06620 105 -------VLGKIAVAVLEGltylynvhrIIHRDIKPSNILVNSKGQ---IKLCDFGVSG-----ELINSIadtfVGTSTY 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 316 VAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPFWARTES--------GIF----RAVlkadpsfDEPPwPSL------S 376
Cdd:cd06620 170 MSPERIQgGKYSVKSDVWSLGLSIIELALGEFPFAGSNDDddgyngpmGILdllqRIV-------NEPP-PRLpkdrifP 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 15230288 377 FEAKDFVKRLLYKDPRKRMTASQALMHPWIAGYKKIdIPFDI 418
Cdd:cd06620 242 KDLRDFVDRCLLKDPRERPSPQLLLDHDPFIQAVRA-SDVDL 282
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
148-405 1.56e-26

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: 109.30  E-value: 1.56e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKFKKGelkDQEVAVKVI---------PkskmTSAIsiedvrREVKILRALSgHQNLVQFYDAFEDN 218
Cdd:cd07835   5 EKIGEGTYGVVYKARDKLT---GEIVALKKIrletedegvP----STAI------REISLLKELN-HPNIVRLLDVVHSE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 219 ANVYIVMELcgggelLDRILArggKYSE---------DDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLyTSKEENsmL 289
Cdd:cd07835  71 NKLYLVFEF------LDLDLK---KYMDsspltgldpPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLL-IDTEGA--L 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 290 KVIDFGLSD-FVRPDERLNDIVGSAYYVAPEVL--HRSYTTEADVWSIGVIaYILLCGSRP-FWARTESG----IFRAVL 361
Cdd:cd07835 139 KLADFGLARaFGVPVRTYTHEVVTLWYRAPEILlgSKHYSTPVDIWSVGCI-FAEMVTRRPlFPGDSEIDqlfrIFRTLG 217
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15230288 362 KAD--------------PSFdePPW---------PSLSFEAKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd07835 218 TPDedvwpgvtslpdykPTF--PKWarqdlskvvPSLDEDGLDLLSQMLVYDPAKRISAKAALQHPY 282
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
140-405 1.83e-26

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: 110.35  E-value: 1.83e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 140 LQSRIELGEEIGRGHFG--YTCsakfkKGELKDQEVAVKVI---PKSKmtsaisiEDVRREVKILRAL-----SGHQNLV 209
Cdd:cd14134  10 LTNRYKILRLLGEGTFGkvLEC-----WDRKRKRYVAVKIIrnvEKYR-------EAAKIEIDVLETLaekdpNGKSHCV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 210 QFYDAFEDNANVYIVMELCGGgELLDRILA-RGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKE---- 284
Cdd:cd14134  78 QLRDWFDYRGHMCIVFELLGP-SLYDFLKKnNYGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDSDyvkv 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 285 ------------ENSMLKVIDFGLSDFVrpDERLNDIVGSAYYVAPEV---LHRSYTteADVWSIGVIAYILLCGSRPF- 348
Cdd:cd14134 157 ynpkkkrqirvpKSTDIKLIDFGSATFD--DEYHSSIVSTRHYRAPEVilgLGWSYP--CDVWSIGCILVELYTGELLFq 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 349 ---------------------WAR----TESGIFRAVLKADPSFDEP-------------PWPSLSFEAK----DFVKRL 386
Cdd:cd14134 233 thdnlehlammerilgplpkrMIRrakkGAKYFYFYHGRLDWPEGSSsgrsikrvckplkRLMLLVDPEHrllfDLIRKM 312
                       330
                ....*....|....*....
gi 15230288 387 LYKDPRKRMTASQALMHPW 405
Cdd:cd14134 313 LEYDPSKRITAKEALKHPF 331
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
148-406 2.29e-26

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: 108.48  E-value: 2.29e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKFKKGElkdQEVAVKVIPKSKMTSAisiEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMEL 227
Cdd:cd06647  13 EKIGQGASGTVYTAIDVATG---QEVAIKQMNLQQQPKK---ELIINEILVMRENK-NPNIVNYLDSYLVGDELWVVMEY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 228 CGGGELLDRILARggKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSDFVRPDER-L 306
Cdd:cd06647  86 LAGGSLTDVVTET--CMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGM---DGSVKLTDFGFCAQITPEQSkR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 307 NDIVGSAYYVAPEVLHR-SYTTEADVWSIGVIAYILLCGSRPFWARTE-SGIFRAVLKADPSFDEPPWPSLSFeaKDFVK 384
Cdd:cd06647 161 STMVGTPYWMAPEVVTRkAYGPKVDIWSLGIMAIEMVEGEPPYLNENPlRALYLIATNGTPELQNPEKLSAIF--RDFLN 238
                       250       260
                ....*....|....*....|..
gi 15230288 385 RLLYKDPRKRMTASQALMHPWI 406
Cdd:cd06647 239 RCLEMDVEKRGSAKELLQHPFL 260
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
150-406 2.55e-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: 109.24  E-value: 2.55e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKK-GELkdqeVAVKVIPKSKMTSAISIEDVRrEVKILRALSgHQNLVQFYD-AFEDNAN-VYIVME 226
Cdd:cd07843  13 IEEGTYGVVYRARDKKtGEI----VALKKLKMEKEKEGFPITSLR-EINILLKLQ-HPNIVTVKEvVVGSNLDkIYMVME 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 227 lCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsmLKVIDFGLS-DFVRPDER 305
Cdd:cd07843  87 -YVEHDLKSLMETMKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGI---LKICDFGLArEYGSPLKP 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 306 LNDIVGSAYYVAPEVL--HRSYTTEADVWSIGVIAYILLCGSRPFWARTE----SGIFRAVlkADPSfdEPPWP------ 373
Cdd:cd07843 163 YTQLVVTLWYRAPELLlgAKEYSTAIDMWSVGCIFAELLTKKPLFPGKSEidqlNKIFKLL--GTPT--EKIWPgfselp 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15230288 374 ----------------------SLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd07843 239 gakkktftkypynqlrkkfpalSLSDNGFDLLNRLLTYDPAKRISAEDALKHPYF 293
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
156-404 2.57e-26

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: 108.51  E-value: 2.57e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 156 GYTCSAKFK-KGELKDQEVAVKVIPKSKMTSAisiedvRREVKILRALSGHQNLVQFYDAFEDNANVYIVMELCGGG--E 232
Cdd:cd13982  10 GYGSEGTIVfRGTFDGRPVAVKRLLPEFFDFA------DREVQLLRESDEHPNVIRYFCTEKDRQFLYIALELCAASlqD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 233 LLDR-ILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFL--YTSKEENSMLKVIDFGLSDFVRPDE----R 305
Cdd:cd13982  84 LVESpRESKLFLRPGLEPVRLLRQIASGLAHLHSLNIVHRDLKPQNILisTPNAHGNVRAMISDFGLCKKLDVGRssfsR 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 306 LNDIVGSAYYVAPEVL----HRSYTTEADVWSIG-VIAYILLCGSRPFWAR--TESGIfravLKADPSFDEP-PWPSLSF 377
Cdd:cd13982 164 RSGVAGTSGWIAPEMLsgstKRRQTRAVDIFSLGcVFYYVLSGGSHPFGDKleREANI----LKGKYSLDKLlSLGEHGP 239
                       250       260
                ....*....|....*....|....*..
gi 15230288 378 EAKDFVKRLLYKDPRKRMTASQALMHP 404
Cdd:cd13982 240 EAQDLIERMIDFDPEKRPSAEEVLNHP 266
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
150-416 3.36e-26

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: 109.26  E-value: 3.36e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFK-KGELkdqeVAVKVIPKSKMTSAISIEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIVMELC 228
Cdd:cd05620   3 LGKGSFGKVLLAELKgKGEY----FAVKALKKDVVLIDDDVECTMVEKRVLALAWENPFLTHLYCTFQTKEHLFFVMEFL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 229 GGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGL-SDFVRPDERLN 307
Cdd:cd05620  79 NGGDLMFHIQDKG-RFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVML---DRDGHIKIADFGMcKENVFGDNRAS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 308 DIVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFdePPWpsLSFEAKDFVKRL 386
Cdd:cd05620 155 TFCGTPDYIAPEILQgLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHY--PRW--ITKESKDILEKL 230
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 15230288 387 LYKDPRKRMTASQAL-MHP------WIAGYKK-IDIPF 416
Cdd:cd05620 231 FERDPTRRLGVVGNIrGHPffktinWTALEKReLDPPF 268
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
139-409 3.87e-26

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: 109.75  E-value: 3.87e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 139 ELQSRIELGEEIGRGHFGYTCSAKFKKGElkdQEVAVKVIPKSkMTSAISIEDVRREVKILRALSgHQNLVQFYDAF--- 215
Cdd:cd07878  12 EVPERYQNLTPVGSGAYGSVCSAYDTRLR---QKVAVKKLSRP-FQSLIHARRTYRELRLLKHMK-HENVIGLLDVFtpa 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 216 ---EDNANVYIVMELCGGGelLDRILaRGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFlytSKEENSMLKVI 292
Cdd:cd07878  87 tsiENFNEVYLVTNLMGAD--LNNIV-KCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNV---AVNEDCELRIL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 293 DFGLSDfvRPDERLNDIVGSAYYVAPEVLHR--SYTTEADVWSIGVIAYILLCGSRPF----WARTESGIFRAVLKADPS 366
Cdd:cd07878 161 DFGLAR--QADDEMTGYVATRWYRAPEIMLNwmHYNQTVDIWSVGCIMAELLKGKALFpgndYIDQLKRIMEVVGTPSPE 238
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15230288 367 F--------------DEPPWPSLSFE---------AKDFVKRLLYKDPRKRMTASQALMHPWIAGY 409
Cdd:cd07878 239 VlkkisseharkyiqSLPHMPQQDLKkifrganplAIDLLEKMLVLDSDKRISASEALAHPYFSQY 304
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
150-416 4.41e-26

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 109.68  E-value: 4.41e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  150 IGRGHFGYTCSAKFKKGELKdqEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:PTZ00426  38 LGTGSFGRVILATYKNEDFP--PVAIKRFEKSKIIKQKQVDHVFSERKILNYIN-HPFCVNLYGSFKDESYLYLVLEFVI 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  230 GGELLDrILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLSDFVrpDERLNDI 309
Cdd:PTZ00426 115 GGEFFT-FLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLL---DKDGFIKMTDFGFAKVV--DTRTYTL 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  310 VGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFdePPWpsLSFEAKDFVKRLLY 388
Cdd:PTZ00426 189 CGTPEYIAPEILlNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGIIYF--PKF--LDNNCKHLMKKLLS 264
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 15230288  389 KDPRKRM-----TASQALMHPWIAG-------YKKIDIPF 416
Cdd:PTZ00426 265 HDLTKRYgnlkkGAQNVKEHPWFGNidwvsllHKNVEVPY 304
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
201-405 4.83e-26

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: 107.04  E-value: 4.83e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 201 ALSGHQNLVQFYDAFEDNANVYIVMELCGGGelLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLY 280
Cdd:cd14022  40 CLPAHSNINQITEIILGETKAYVFFERSYGD--MHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVF 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 281 TSkEENSMLKVIDFGLSDFVR-PDERLNDIVGSAYYVAPEVLHR--SYTTE-ADVWSIGVIAYILLCGSRPFWARTESGI 356
Cdd:cd14022 118 KD-EERTRVKLESLEDAYILRgHDDSLSDKHGCPAYVSPEILNTsgSYSGKaADVWSLGVMLYTMLVGRYPFHDIEPSSL 196
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15230288 357 FRAVLKAdpSFDEPpwPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd14022 197 FSKIRRG--QFNIP--ETLSPKAKCLIRSILRREPSERLTSQEILDHPW 241
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
171-408 6.01e-26

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


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 107.88  E-value: 6.01e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 171 QEVAVKVIPKSKMTSAISIEDVRREVKILrALSGHQNLVQFYDAFEDNANVYIVMELCGGGE---LLDRIlargGKYSED 247
Cdd:cd05609  26 QRFAMKKINKQNLILRNQIQQVFVERDIL-TFAENPFVVSMYCSFETKRHLCMVMEYVEGGDcatLLKNI----GPLPVD 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 248 DAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGLS-------------DFVRPDER-LND--IVG 311
Cdd:cd05609 101 MARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSM---GHIKLTDFGLSkiglmslttnlyeGHIEKDTReFLDkqVCG 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 312 SAYYVAPEV-LHRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKadpsfDEPPWPS----LSFEAKDFVKRL 386
Cdd:cd05609 178 TPEYIAPEViLRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVIS-----DEIEWPEgddaLPDDAQDLITRL 252
                       250       260
                ....*....|....*....|....*
gi 15230288 387 LYKDPRKRMTASQAL---MHPWIAG 408
Cdd:cd05609 253 LQQNPLERLGTGGAEevkQHPFFQD 277
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
148-411 8.24e-26

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: 107.45  E-value: 8.24e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTcsakFKKGELKDQEV-AVKVIPKSKMTSaiSIEDVRREVKILRALSGhQNLVQFYDAFEDNANVYIVME 226
Cdd:cd06642  10 ERIGKGSFGEV----YKGIDNRTKEVvAIKIIDLEEAED--EIEDIQQEITVLSQCDS-PYITRYYGSYLKGTKLWIIME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 227 LCGGGELLDriLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFVRPDE-R 305
Cdd:cd06642  83 YLGGGSALD--LLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLS---EQGDVKLADFGVAGQLTDTQiK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 306 LNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPsfdeppwPSL----SFEAK 380
Cdd:cd06642 158 RNTFVGTPFWMAPEVIKQSaYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKNSP-------PTLegqhSKPFK 230
                       250       260       270
                ....*....|....*....|....*....|.
gi 15230288 381 DFVKRLLYKDPRKRMTASQALMHPWIAGYKK 411
Cdd:cd06642 231 EFVEACLNKDPRFRPTAKELLKHKFITRYTK 261
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
145-406 9.71e-26

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: 107.50  E-value: 9.71e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAK-FKKGELkdqeVAVKVIPkskmTSAISIEDVRREVKILRALSGHQNLVQFYDAFED------ 217
Cdd:cd06637   9 ELVELVGNGTYGQVYKGRhVKTGQL----AAIKVMD----VTGDEEEEIKQEINMLKKYSHHRNIATYYGAFIKknppgm 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 218 NANVYIVMELCGGGELLDRIL-ARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGL 296
Cdd:cd06637  81 DDQLWLVMEFCGAGSVTDLIKnTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLT---ENAEVKLVDFGV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 297 S-DFVRPDERLNDIVGSAYYVAPEVL------HRSYTTEADVWSIGVIAYILLCGSRPFW-ARTESGIFRAVLKADPSFD 368
Cdd:cd06637 158 SaQLDRTVGRRNTFIGTPYWMAPEVIacdenpDATYDFKSDLWSLGITAIEMAEGAPPLCdMHPMRALFLIPRNPAPRLK 237
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 15230288 369 EPPWpslSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd06637 238 SKKW---SKKFQSFIESCLVKNHSQRPSTEQLMKHPFI 272
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
190-408 1.04e-25

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 108.76  E-value: 1.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  190 EDVR----REVKILRALSgHQNLVQFYDAFEDNANVYIVMELCGGGELLDRILARGGKYSEddakaVLIQILNVVAFCHL 265
Cdd:PLN00034 113 DTVRrqicREIEILRDVN-HPNVVKCHDMFDHNGEIQVLLEFMDGGSLEGTHIADEQFLAD-----VARQILSGIAYLHR 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  266 QGVVHRDLKPENFLYTSKEEnsmLKVIDFGLSDFV-RPDERLNDIVGSAYYVAPEVL-----HRSYTTEA-DVWSIGVIA 338
Cdd:PLN00034 187 RHIVHRDIKPSNLLINSAKN---VKIADFGVSRILaQTMDPCNSSVGTIAYMSPERIntdlnHGAYDGYAgDIWSLGVSI 263
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15230288  339 YILLCGSRPF-------WArtesGIFRAVLKADPSfdEPPwPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWIAG 408
Cdd:PLN00034 264 LEFYLGRFPFgvgrqgdWA----SLMCAICMSQPP--EAP-ATASREFRHFISCCLQREPAKRWSAMQLLQHPFILR 333
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
140-348 1.78e-25

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 110.66  E-value: 1.78e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  140 LQSRIELGEEIGRG-----HFGytcsakfkKGELKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDA 214
Cdd:NF033483   5 LGGRYEIGERIGRGgmaevYLA--------KDTRLDRDVAVKVLRPDLARDPEFVARFRREAQSAASLS-HPNIVSVYDV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  215 FEDNANVYIVMELCGGgELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDF 294
Cdd:NF033483  76 GEDGGIPYIVMEYVDG-RTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILIT---KDGRVKVTDF 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15230288  295 GLSdfvrpdeRL---------NDIVGSAYYVAPEVLHRSYTTE-ADVWSIGVIAYILLCGSRPF 348
Cdd:NF033483 152 GIA-------RAlssttmtqtNSVLGTVHYLSPEQARGGTVDArSDIYSLGIVLYEMLTGRPPF 208
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
150-395 1.84e-25

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: 107.09  E-value: 1.84e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGytcsaKFKKGELKDQE--VAVKVIPKSKMTSAISIEDVRREVKILrALSGHQN-LVQFYDAFEDNANVYIVME 226
Cdd:cd05587   4 LGKGSFG-----KVMLAERKGTDelYAIKILKKDVIIQDDDVECTMVEKRVL-ALSGKPPfLTQLHSCFQTMDRLYFVME 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 227 LCGGGELLDRIlARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGL-SDFVRPDER 305
Cdd:cd05587  78 YVNGGDLMYHI-QQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDA---EGHIKIADFGMcKEGIFGGKT 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 306 LNDIVGSAYYVAPE-VLHRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEppwpSLSFEAKDFVK 384
Cdd:cd05587 154 TRTFCGTPDYIAPEiIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPK----SLSKEAVSICK 229
                       250
                ....*....|.
gi 15230288 385 RLLYKDPRKRM 395
Cdd:cd05587 230 GLLTKHPAKRL 240
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
148-411 2.08e-25

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: 106.29  E-value: 2.08e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTcsakFKKGELKDQEV-AVKVIPKSKMTSaiSIEDVRREVKILRALSGhQNLVQFYDAFEDNANVYIVME 226
Cdd:cd06640  10 ERIGKGSFGEV----FKGIDNRTQQVvAIKIIDLEEAED--EIEDIQQEITVLSQCDS-PYVTKYYGSYLKGTKLWIIME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 227 LCGGGELLDriLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFVRPDE-R 305
Cdd:cd06640  83 YLGGGSALD--LLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLS---EQGDVKLADFGVAGQLTDTQiK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 306 LNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPfwaRTESGIFRaVLKADPSFDEPPWP-SLSFEAKDFV 383
Cdd:cd06640 158 RNTFVGTPFWMAPEVIQQSaYDSKADIWSLGITAIELAKGEPP---NSDMHPMR-VLFLIPKNNPPTLVgDFSKPFKEFI 233
                       250       260
                ....*....|....*....|....*...
gi 15230288 384 KRLLYKDPRKRMTASQALMHPWIAGYKK 411
Cdd:cd06640 234 DACLNKDPSFRPTAKELLKHKFIVKNAK 261
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
148-406 2.19e-25

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: 105.92  E-value: 2.19e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTcsakFKKGELKDQEV-AVKVIPKSKMTSaiSIEDVRREVKILRALSGhQNLVQFYDAFEDNANVYIVME 226
Cdd:cd06641  10 EKIGKGSFGEV----FKGIDNRTQKVvAIKIIDLEEAED--EIEDIQQEITVLSQCDS-PYVTKYYGSYLKDTKLWIIME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 227 LCGGGELLDriLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFVRPDE-R 305
Cdd:cd06641  83 YLGGGSALD--LLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLS---EHGEVKLADFGVAGQLTDTQiK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 306 LNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWpslSFEAKDFVK 384
Cdd:cd06641 158 RN*FVGTPFWMAPEVIKQSaYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLEGNY---SKPLKEFVE 234
                       250       260
                ....*....|....*....|..
gi 15230288 385 RLLYKDPRKRMTASQALMHPWI 406
Cdd:cd06641 235 ACLNKEPSFRPTAKELLKHKFI 256
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
142-354 2.43e-25

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: 105.42  E-value: 2.43e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 142 SRIELGEEIGRGHFGYTcsakFKKGELKDQEVAVKVIPKSKMtsaiSIEDVRREVKILRALSgHQNLVQFYDAFEDNANV 221
Cdd:cd05112   4 SELTFVQEIGSGQFGLV----HLGYWLNKDKVAIKTIREGAM----SEEDFIEEAEVMMKLS-HPKLVQLYGVCLEQAPI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 YIVMELCGGGELLDRILARGGKYSeddAKAVLIQILNV---VAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSD 298
Cdd:cd05112  75 CLVFEFMEHGCLSDYLRTQRGLFS---AETLLGMCLDVcegMAYLEEASVIHRDLAARNCLVG---ENQVVKVSDFGMTR 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15230288 299 FVRpDERLNDIVGSAYYV---APEVLHRS-YTTEADVWSIGVIAYILLC-GSRPFWARTES 354
Cdd:cd05112 149 FVL-DDQYTSSTGTKFPVkwsSPEVFSFSrYSSKSDVWSFGVLMWEVFSeGKIPYENRSNS 208
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
150-425 2.76e-25

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: 106.72  E-value: 2.76e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKGELKDQEVAVKVIPKSkmtsAISIEDVRR---EVKILrALSGHQNLVQFYDAFEDNANVYIVME 226
Cdd:cd05582   3 LGQGSFGKVFLVRKITGPDAGTLYAMKVLKKA----TLKVRDRVRtkmERDIL-ADVNHPFIVKLHYAFQTEGKLYLILD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 227 LCGGGELLDRiLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLS-DFVRPDER 305
Cdd:cd05582  78 FLRGGDLFTR-LSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL---DEDGHIKLTDFGLSkESIDHEKK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 306 LNDIVGSAYYVAPEVLHR-SYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKAD---PSFdeppwpsLSFEAKD 381
Cdd:cd05582 154 AYSFCGTVEYMAPEVVNRrGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKlgmPQF-------LSPEAQS 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 15230288 382 FVKRLLYKDPRKRMTAS-----QALMHPWiagYKKIDipFDILIFKQIK 425
Cdd:cd05582 227 LLRALFKRNPANRLGAGpdgveEIKRHPF---FATID--WNKLYRKEIK 270
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
142-361 4.41e-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: 104.45  E-value: 4.41e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 142 SRIELGEEIGRGHFGYTCSAKFKkGELKdqeVAVKVIPKSKMtsaiSIEDVRREVKILRALSgHQNLVQFYDAFEDNANV 221
Cdd:cd05059   4 SELTFLKELGSGQFGVVHLGKWR-GKID---VAIKMIKEGSM----SEDDFIEEAKVMMKLS-HPKLVQLYGVCTKQRPI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 YIVMELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFVR 301
Cdd:cd05059  75 FIVTEYMANGCLLNYLRERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVG---EQNVVKVSDFGLARYVL 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15230288 302 PDERLNDiVGSAYYV---APEVLHRS-YTTEADVWSIGVIAY-ILLCGSRPFWARTESGIFRAVL 361
Cdd:cd05059 152 DDEYTSS-VGTKFPVkwsPPEVFMYSkFSSKSDVWSFGVLMWeVFSEGKMPYERFSNSEVVEHIS 215
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
149-407 5.41e-25

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: 105.49  E-value: 5.41e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 149 EIGRGHFGYTCSAKFKK-GELkdqeVAVKvipKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMEL 227
Cdd:cd06657  27 KIGEGSTGIVCIATVKSsGKL----VAVK---KMDLRKQQRRELLFNEVVIMRDYQ-HENVVEMYNSYLVGDELWVVMEF 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 228 CGGGELLDriLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFVRPD-ERL 306
Cdd:cd06657  99 LEGGALTD--IVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLT---HDGRVKLSDFGFCAQVSKEvPRR 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 307 NDIVGSAYYVAPEVLHR-SYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPsfdePPWPSL---SFEAKDF 382
Cdd:cd06657 174 KSLVGTPYWMAPELISRlPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLP----PKLKNLhkvSPSLKGF 249
                       250       260
                ....*....|....*....|....*
gi 15230288 383 VKRLLYKDPRKRMTASQALMHPWIA 407
Cdd:cd06657 250 LDRLLVRDPAQRATAAELLKHPFLA 274
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
205-406 7.36e-25

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: 103.42  E-value: 7.36e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 205 HQNLVQFYDAFEDNANVYIVMELCGGGelLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKE 284
Cdd:cd14024  44 HEGVCSVLEVVIGQDRAYAFFSRHYGD--MHSHVRRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDEL 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 285 ENsmlKVIDFGLSD---FVRPDERLNDIVGSAYYVAPEVLH--RSYTTE-ADVWSIGVIAYILLCGSRPFWARTESGIFR 358
Cdd:cd14024 122 RT---KLVLVNLEDscpLNGDDDSLTDKHGCPAYVGPEILSsrRSYSGKaADVWSLGVCLYTMLLGRYPFQDTEPAALFA 198
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15230288 359 AVLKAdpSFDEPPWpsLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14024 199 KIRRG--AFSLPAW--LSPGARCLVSCMLRRSPAERLKASEILLHPWL 242
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
150-397 9.17e-25

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: 105.44  E-value: 9.17e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd05603   3 IGKGSFGKVLLAKRKC---DGKFYAVKVLQKKTILKKKEQNHIMAERNVLLKNLKHPFLVGLHYSFQTSEKLYFVLDYVN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRiLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGL-SDFVRPDERLND 308
Cdd:cd05603  80 GGELFFH-LQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQ---GHVVLTDFGLcKEGMEPEETTST 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 309 IVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKAdpSFDEPPWPSLSfeAKDFVKRLL 387
Cdd:cd05603 156 FCGTPEYLAPEVLRKEpYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHK--PLHLPGGKTVA--ACDLLQGLL 231
                       250
                ....*....|
gi 15230288 388 YKDPRKRMTA 397
Cdd:cd05603 232 HKDQRRRLGA 241
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
144-415 9.57e-25

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: 104.76  E-value: 9.57e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 144 IELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSkmtsaisieDVRREVK-ILRALS----GHQ--NLVQFYDAFE 216
Cdd:cd06618  17 LENLGEIGSGTCGQVYKMRHKK---TGHVMAVKQMRRS---------GNKEENKrILMDLDvvlkSHDcpYIVKCYGYFI 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 217 DNANVYIVMELCGggELLDRILAR-GGKYSEDDAKAVLIQILNvvAFCHL---QGVVHRDLKPENFLYtskEENSMLKVI 292
Cdd:cd06618  85 TDSDVFICMELMS--TCLDKLLKRiQGPIPEDILGKMTVSIVK--ALHYLkekHGVIHRDVKPSNILL---DESGNVKLC 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 293 DFGLSDFVRPDERLNDIVGSAYYVAPEVL----HRSYTTEADVWSIGVIAYILLCGSRPF-WARTESGIFRAVLKadpsf 367
Cdd:cd06618 158 DFGISGRLVDSKAKTRSAGCAAYMAPERIdppdNPKYDIRADVWSLGISLVELATGQFPYrNCKTEFEVLTKILN----- 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 15230288 368 DEPPWPSL----SFEAKDFVKRLLYKDPRKRMTASQALMHPWIAGY--KKIDIP 415
Cdd:cd06618 233 EEPPSLPPnegfSPDFCSFVDLCLTKDHRYRPKYRELLQHPFIRRYetAEVDVA 286
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
142-405 1.15e-24

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: 103.57  E-value: 1.15e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 142 SRIELGEEIGRGHFGYTCSAKFkkgELKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANV 221
Cdd:cd08228   2 ANFQIEKKIGRGQFSEVYRATC---LLDRKPVALKKVQIFEMMDAKARQDCVKEIDLLKQLN-HPNVIKYLDSFIEDNEL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 YIVMELCGGGELLDRIlarggKYSEDDAKAV--------LIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsmLKVID 293
Cdd:cd08228  78 NIVLELADAGDLSQMI-----KYFKKQKRLIpertvwkyFVQLCSAVEHMHSRRVMHRDIKPANVFITATGV---VKLGD 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 294 FGLSDFVRPDER-LNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWArTESGIFRAVLKADPSfDEPP 371
Cdd:cd08228 150 LGLGRFFSSKTTaAHSLVGTPYYMSPERIHENgYNFKSDIWSLGCLLYEMAALQSPFYG-DKMNLFSLCQKIEQC-DYPP 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15230288 372 WPSLSFEAK--DFVKRLLYKDPRKRMTASQAL-----MHPW 405
Cdd:cd08228 228 LPTEHYSEKlrELVSMCIYPDPDQRPDIGYVHqiakqMHVW 268
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
150-405 1.36e-24

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: 104.37  E-value: 1.36e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIEDVRrEVKILRALSgHQNLVQFYDAFEDNA--NVYIVMEL 227
Cdd:cd07845  15 IGEGTYGIVYRARDTT---SGEIVALKKVRMDNERDGIPISSLR-EITLLLNLR-HPNIVELKEVVVGKHldSIFLVMEY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 228 CGG--GELLDRILArggKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGLS-DFVRPDE 304
Cdd:cd07845  90 CEQdlASLLDNMPT---PFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDK---GCLKIADFGLArTYGLPAK 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 305 RLNDIVGSAYYVAPEVL--HRSYTTEADVWSIGVIAYILLCGSRPFWARTE-------------------------SGIF 357
Cdd:cd07845 164 PMTPKVVTLWYRAPELLlgCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEieqldliiqllgtpnesiwpgfsdlPLVG 243
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 15230288 358 RAVLKADP-SFDEPPWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd07845 244 KFTLPKQPyNNLKHKFPWLSEAGLRLLNFLLMYDPKKRATAEEALESSY 292
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
148-406 1.40e-24

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: 104.04  E-value: 1.40e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKfkkGELKDQEVAVKVIPKSKMTSAisiEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMEL 227
Cdd:cd06655  25 EKIGQGASGTVFTAI---DVATGQEVAIKQINLQKQPKK---ELIINEILVMKELK-NPNIVNFLDSFLVGDELFVVMEY 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 228 CGGGELLDRILarggKYSEDDAK--AVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGLSDFVRPDE- 304
Cdd:cd06655  98 LAGGSLTDVVT----ETCMDEAQiaAVCRECLQALEFLHANQVIHRDIKSDNVLLGMD---GSVKLTDFGFCAQITPEQs 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 305 RLNDIVGSAYYVAPEVLHR-SYTTEADVWSIGVIAYILLCGSRPFWARTE-SGIFRAVLKADPSFDEPPWPSLSFeaKDF 382
Cdd:cd06655 171 KRSTMVGTPYWMAPEVVTRkAYGPKVDIWSLGIMAIEMVEGEPPYLNENPlRALYLIATNGTPELQNPEKLSPIF--RDF 248
                       250       260
                ....*....|....*....|....
gi 15230288 383 VKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd06655 249 LNRCLEMDVEKRGSAKELLQHPFL 272
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
150-402 1.68e-24

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: 105.10  E-value: 1.68e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKGElkdQEVAVKVIPKSKMTSAISIEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd05602  15 IGKGSFGKVLLARHKSDE---KFYAVKVLQKKAILKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTTDKLYFVLDYIN 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRiLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGL-SDFVRPDERLND 308
Cdd:cd05602  92 GGELFYH-LQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQ---GHIVLTDFGLcKENIEPNGTTST 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 309 IVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDeppwPSLSFEAKDFVKRLL 387
Cdd:cd05602 168 FCGTPEYLAPEVLHKQpYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLK----PNITNSARHLLEGLL 243
                       250
                ....*....|....*
gi 15230288 388 YKDPRKRMTASQALM 402
Cdd:cd05602 244 QKDRTKRLGAKDDFT 258
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
150-395 1.74e-24

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: 104.70  E-value: 1.74e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKfKKGelKDQEVAVKVIPKSKMTSAISIEDVRREVKILrALSGHQN-LVQFYDAFEDNANVYIVMELC 228
Cdd:cd05616   8 LGKGSFGKVMLAE-RKG--TDELYAVKILKKDVVIQDDDVECTMVEKRVL-ALSGKPPfLTQLHSCFQTMDRLYFVMEYV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 229 GGGELLDRIlARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGLSDfvrpdERLND 308
Cdd:cd05616  84 NGGDLMYHI-QQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSE---GHIKIADFGMCK-----ENIWD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 309 IV------GSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEppwpSLSFEAKD 381
Cdd:cd05616 155 GVttktfcGTPDYIAPEIIaYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPK----SMSKEAVA 230
                       250
                ....*....|....
gi 15230288 382 FVKRLLYKDPRKRM 395
Cdd:cd05616 231 ICKGLMTKHPGKRL 244
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
139-413 1.89e-24

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: 104.65  E-value: 1.89e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 139 ELQSRIELGEEIGRGHFGYTCSAKFKKGELKdqeVAVKVIPKSkMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDN 218
Cdd:cd07880  12 EVPDRYRDLKQVGSGAYGTVCSALDRRTGAK---VAIKKLYRP-FQSELFAKRAYRELRLLKHMK-HENVIGLLDVFTPD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 219 ANV------YIVMELCGG--GELLdrilaRGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFlytSKEENSMLK 290
Cdd:cd07880  87 LSLdrfhdfYLVMPFMGTdlGKLM-----KHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNL---AVNEDCELK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 291 VIDFGLSDfvRPDERLNDIVGSAYYVAPEVLHR--SYTTEADVWSIGVIAYILLCG-----------------------S 345
Cdd:cd07880 159 ILDFGLAR--QTDSEMTGYVVTRWYRAPEVILNwmHYTQTVDIWSVGCIMAEMLTGkplfkghdhldqlmeimkvtgtpS 236
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15230288 346 RPFWARTESGIFRAVLKADPSFDEPPWPSL----SFEAKDFVKRLLYKDPRKRMTASQALMHPWIAGYKKID 413
Cdd:cd07880 237 KEFVQKLQSEDAKNYVKKLPRFRKKDFRSLlpnaNPLAVNVLEKMLVLDAESRITAAEALAHPYFEEFHDPE 308
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
150-348 2.07e-24

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: 102.52  E-value: 2.07e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKkgelkDQEVAVKVIpkskmTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd14058   1 VGRGSFGVVCKARWR-----NQIVAVKII-----ESESEKKAFEVEVRQLSRVD-HPNIIKLYGACSNQKPVCLVMEYAE 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRILARGGK--YSEDDAKAVLIQILNVVAFCHL---QGVVHRDLKPENFLYTSKEENsmLKVIDFGLS-DFvrpD 303
Cdd:cd14058  70 GGSLYNVLHGKEPKpiYTAAHAMSWALQCAKGVAYLHSmkpKALIHRDLKPPNLLLTNGGTV--LKICDFGTAcDI---S 144
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15230288 304 ERLNDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPF 348
Cdd:cd14058 145 THMTNNKGSAAWMAPEVFeGSKYSEKCDVFSWGIILWEVITRRKPF 190
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
144-406 2.18e-24

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: 105.21  E-value: 2.18e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 144 IELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSkMTSAISIEDVRREVKILRALSgHQNLVQFYDA--------F 215
Cdd:cd07853   2 VEPDRPIGYGAFGVVWSVTDPR---DGKRVALKKMPNV-FQNLVSCKRVFRELKMLCFFK-HDNVLSALDIlqpphidpF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 216 EDnanVYIVMELCGGGelLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFG 295
Cdd:cd07853  77 EE---IYVVTELMQSD--LHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNS---NCVLKICDFG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 296 LSDFVRPDERLNDI--VGSAYYVAPEVL--HRSYTTEADVWSIGVIAYILLCGSRPFWARTE------------------ 353
Cdd:cd07853 149 LARVEEPDESKHMTqeVVTQYYRAPEILmgSRHYTSAVDIWSVGCIFAELLGRRILFQAQSPiqqldlitdllgtpslea 228
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15230288 354 -----SGIFRAVLKADPSfdePPWPSLSF--------EAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd07853 229 mrsacEGARAHILRGPHK---PPSLPVLYtlssqathEAVHLLCRMLVFDPDKRISAADALAHPYL 291
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
146-406 2.37e-24

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: 102.80  E-value: 2.37e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 146 LGEEIGRGHFG--YTCSAKFKKGELKDQEVAVKviPKSKMTSAiSIEDVRREVKILRALSgHQNLVQFYDAFED--NANV 221
Cdd:cd06653   6 LGKLLGRGAFGevYLCYDADTGRELAVKQVPFD--PDSQETSK-EVNALECEIQLLKNLR-HDRIVQYYGCLRDpeEKKL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 YIVMELCGGGELLDRILARGGkYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLytsKEENSMLKVIDFGLSDFV- 300
Cdd:cd06653  82 SIFVEYMPGGSVKDQLKAYGA-LTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANIL---RDSAGNVKLGDFGASKRIq 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 301 ---RPDERLNDIVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCgSRPFWARTESgiFRAVLKADPSFDEPPWP-SL 375
Cdd:cd06653 158 ticMSGTGIKSVTGTPYWMSPEVISgEGYGRKADVWSVACTVVEMLT-EKPPWAEYEA--MAAIFKIATQPTKPQLPdGV 234
                       250       260       270
                ....*....|....*....|....*....|.
gi 15230288 376 SFEAKDFVKRLLYKDPRkRMTASQALMHPWI 406
Cdd:cd06653 235 SDACRDFLRQIFVEEKR-RPTAEFLLRHPFV 264
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
148-405 2.72e-24

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: 102.90  E-value: 2.72e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKFKK-GELkdqeVAVKvipkskmtsAISIED--------VRREVKILRALSgHQNLVQFYDAFEDN 218
Cdd:cd07839   6 EKIGEGTYGTVFKAKNREtHEI----VALK---------RVRLDDddegvpssALREICLLKELK-HKNIVRLYDVLHSD 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 219 ANVYIVMELCgggellDRILAR-----GGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVID 293
Cdd:cd07839  72 KKLTLVFEYC------DQDLKKyfdscNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLIN---KNGELKLAD 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 294 FGLS-DFVRPDERLNDIVGSAYYVAPEVL--HRSYTTEADVWSIGVIAYILLCGSRPFWARTE-----SGIFRAV----- 360
Cdd:cd07839 143 FGLArAFGIPVRCYSAEVVTLWYRPPDVLfgAKLYSTSIDMWSAGCIFAELANAGRPLFPGNDvddqlKRIFRLLgtpte 222
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15230288 361 -----------LKADPSFD-----EPPWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd07839 223 eswpgvsklpdYKPYPMYPattslVNVVPKLNSTGRDLLQNLLVCNPVQRISAEEALQHPY 283
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
143-401 2.88e-24

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 102.46  E-value: 2.88e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFGytcsaKFKKGELKDQEVAVKVIPKSKMTSAiSIEDVRREVKILRAlsGHQNLVQFYDA---FEDNA 219
Cdd:cd13979   4 PLRLQEPLGSGGFG-----SVYKATYKGETVAVKIVRRRRKNRA-SRQSFWAELNAARL--RHENIVRVLAAetgTDFAS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 220 NVYIVMELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFG---- 295
Cdd:cd13979  76 LGLIIMEYCGNGTLQQLIYEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILIS---EQGVCKLCDFGcsvk 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 296 LSDFVRPDERLNDIVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPS 374
Cdd:cd13979 153 LGEGNEVGTPRSHIGGTYTYRAPELLKgERVTPKADIYSFGITLWQMLTRELPYAGLRQHVLYAVVAKDLRPDLSGLEDS 232
                       250       260
                ....*....|....*....|....*...
gi 15230288 375 LSFEA-KDFVKRLLYKDPRKRMTASQAL 401
Cdd:cd13979 233 EFGQRlRSLISRCWSAQPAERPNADESL 260
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
150-414 3.19e-24

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: 104.39  E-value: 3.19e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIEDVRREVKILRAlSGHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd05593  23 LGKGTFGKVILVREKA---SGKYYAMKILKKEVIIAKDEVAHTLTESRVLKN-TRHPFLTSLKYSFQTKDRLCFVMEYVN 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRiLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGL-SDFVRPDERLND 308
Cdd:cd05593  99 GGELFFH-LSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML---DKDGHIKITDFGLcKEGITDAATMKT 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 309 IVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEppwpSLSFEAKDFVKRLL 387
Cdd:cd05593 175 FCGTPEYLAPEVLEdNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPR----TLSADAKSLLSGLL 250
                       250       260       270
                ....*....|....*....|....*....|..
gi 15230288 388 YKDPRKRM-----TASQALMHPWIAGYKKIDI 414
Cdd:cd05593 251 IKDPNKRLgggpdDAKEIMRHSFFTGVNWQDV 282
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
141-412 3.34e-24

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 107.90  E-value: 3.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288   141 QSRI---ELGEEIGRGHFGYTCSAKFKKGElkdQEVAVKVIP----KSKMTSAISIE-DVRREVKilralsgHQNLVQFY 212
Cdd:PTZ00266    9 ESRLneyEVIKKIGNGRFGEVFLVKHKRTQ---EFFCWKAISyrglKEREKSQLVIEvNVMRELK-------HKNIVRYI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288   213 DAFEDNAN--VYIVMELCGGGEL---LDRILARGGKYSEDDAKAVLIQILNVVAFCHL-------QGVVHRDLKPEN-FL 279
Cdd:PTZ00266   79 DRFLNKANqkLYILMEFCDAGDLsrnIQKCYKMFGKIEEHAIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNiFL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288   280 YT--------SKEENSM-----LKVIDFGLSDFVRPDERLNDIVGSAYYVAPEVL---HRSYTTEADVWSIGVIAYILLC 343
Cdd:PTZ00266  159 STgirhigkiTAQANNLngrpiAKIGDFGLSKNIGIESMAHSCVGTPYYWSPELLlheTKSYDDKSDMWALGCIIYELCS 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15230288   344 GSRPFWARTESGIFRAVLKADPsfdEPPWPSLSFEAKDFVKRLLYKDPRKRMTASQALmhpwiaGYKKI 412
Cdd:PTZ00266  239 GKTPFHKANNFSQLISELKRGP---DLPIKGKSKELNILIKNLLNLSAKERPSALQCL------GYQII 298
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
150-405 3.62e-24

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: 102.89  E-value: 3.62e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKgelKDQEVAVKVI---PKSKMTSAISIedvrREVKILRALSgHQNLVQFYDAFEDNANVYIVME 226
Cdd:cd07846   9 VGEGSYGMVMKCRHKE---TGQIVAIKKFlesEDDKMVKKIAM----REIKMLKQLR-HENLVNLIEVFRRKKRWYLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 227 LCGGgELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFVR-PDER 305
Cdd:cd07846  81 FVDH-TVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVS---QSGVVKLCDFGFARTLAaPGEV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 306 LNDIVGSAYYVAPEVL--HRSYTTEADVWSIGVIAYILLCGSRPFWARTE------------------------SGIFRA 359
Cdd:cd07846 157 YTDYVATRWYRAPELLvgDTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDidqlyhiikclgnliprhqelfqkNPLFAG 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 15230288 360 VLKADPSFDEP---PWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd07846 237 VRLPEVKEVEPlerRYPKLSGVVIDLAKKCLHIDPDKRPSCSELLHHEF 285
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
149-406 4.08e-24

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: 102.81  E-value: 4.08e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 149 EIGRGHFGYTCSAKFKKgelKDQEVAVKvipKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELC 228
Cdd:cd06658  29 KIGEGSTGIVCIATEKH---TGKQVAVK---KMDLRKQQRRELLFNEVVIMRDYH-HENVVDMYNSYLVGDELWVVMEFL 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 229 GGGELLDriLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSDFVRPD-ERLN 307
Cdd:cd06658 102 EGGALTD--IVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTS---DGRIKLSDFGFCAQVSKEvPKRK 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 308 DIVGSAYYVAPEVLHR-SYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPwPSLSFEAKDFVKRL 386
Cdd:cd06658 177 SLVGTPYWMAPEVISRlPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDNLPPRVKDS-HKVSSVLRGFLDLM 255
                       250       260
                ....*....|....*....|
gi 15230288 387 LYKDPRKRMTASQALMHPWI 406
Cdd:cd06658 256 LVREPSQRATAQELLQHPFL 275
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
136-420 4.57e-24

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: 103.19  E-value: 4.57e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 136 FSKELQSRIELG-EEIGRGHFGytcSAKFKKGELKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDA 214
Cdd:cd06633  14 FYKDDPEEIFVDlHEIGHGSFG---AVYFATNSHTNEVVAIKKMSYSGKQTNEKWQDIIKEVKFLQQLK-HPNTIEYKGC 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 215 FEDNANVYIVMELCGGGELlDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDF 294
Cdd:cd06633  90 YLKDHTAWLVMEYCLGSAS-DLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLT---EPGQVKLADF 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 295 GLSDFVRPderLNDIVGSAYYVAPEVL----HRSYTTEADVWSIGvIAYILLCGSRP--FWARTESGIFRAVLKADPSFD 368
Cdd:cd06633 166 GSASIASP---ANSFVGTPYWMAPEVIlamdEGQYDGKVDIWSLG-ITCIELAERKPplFNMNAMSALYHIAQNDSPTLQ 241
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 15230288 369 EPPWpSLSFeaKDFVKRLLYKDPRKRMTASQALMHPWIagykKIDIPFDILI 420
Cdd:cd06633 242 SNEW-TDSF--RGFVDYCLQKIPQERPSSAELLRHDFV----RRERPPRVLI 286
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
150-408 4.63e-24

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: 103.81  E-value: 4.63e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSA-KFKKGELkdqeVAVKVIPKSKMTSAISIEDVRREVKILrALSGHQNLVQFYDAFEDNANVYIVMELC 228
Cdd:cd05610  12 ISRGAFGKVYLGrKKNNSKL----YAVKVVKKADMINKNMVHQVQAERDAL-ALSKSPFIVHLYYSLQSANNVYLVMEYL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 229 GGGELlDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGLS----------- 297
Cdd:cd05610  87 IGGDV-KSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNE---GHIKLTDFGLSkvtlnrelnmm 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 298 -------------DFVR-PDERLN-----------------------------DIVGSAYYVAPE-VLHRSYTTEADVWS 333
Cdd:cd05610 163 dilttpsmakpknDYSRtPGQVLSlisslgfntptpyrtpksvrrgaarvegeRILGTPDYLAPElLLGKPHGPAVDWWA 242
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15230288 334 IGVIAYILLCGSRPFWARTESGIFRAVLKADpsfdePPWP----SLSFEAKDFVKRLLYKDPRKRMTASQALMHPWIAG 408
Cdd:cd05610 243 LGVCLFEFLTGIPPFNDETPQQVFQNILNRD-----IPWPegeeELSVNAQNAIEILLTMDPTKRAGLKELKQHPLFHG 316
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
150-416 6.68e-24

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: 103.57  E-value: 6.68e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIEDVRREVKILRAlSGHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd05594  33 LGKGTFGKVILVKEKA---TGRYYAMKILKKEVIVAKDEVAHTLTENRVLQN-SRHPFLTALKYSFQTHDRLCFVMEYAN 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRiLARGGKYSEDDAKAVLIQILNVVAFCHLQ-GVVHRDLKPENFLYtskEENSMLKVIDFGL-SDFVRPDERLN 307
Cdd:cd05594 109 GGELFFH-LSRERVFSEDRARFYGAEIVSALDYLHSEkNVVYRDLKLENLML---DKDGHIKITDFGLcKEGIKDGATMK 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 308 DIVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEppwpSLSFEAKDFVKRL 386
Cdd:cd05594 185 TFCGTPEYLAPEVLEdNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPR----TLSPEAKSLLSGL 260
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 15230288 387 LYKDPRKRM-----TASQALMHPWIAGY-------KKIDIPF 416
Cdd:cd05594 261 LKKDPKQRLgggpdDAKEIMQHKFFAGIvwqdvyeKKLVPPF 302
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
138-393 6.80e-24

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


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 104.32  E-value: 6.80e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 138 KELQ---SRIELGEEIGRGHFGYTCSAKFKKGElkdQEVAVKVIPKSKMTSAISIEDVRREVKILraLSGH-QNLVQFYD 213
Cdd:cd05624  65 KEMQlhrDDFEIIKVIGRGAFGEVAVVKMKNTE---RIYAMKILNKWEMLKRAETACFREERNVL--VNGDcQWITTLHY 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 214 AFEDNANVYIVMELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVID 293
Cdd:cd05624 140 AFQDENYLYLVMDYYVGGDLLTLLSKFEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLL---DMNGHIRLAD 216
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 294 FGLSDFVRPDERLND--IVGSAYYVAPEVLHR------SYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADP 365
Cdd:cd05624 217 FGSCLKMNDDGTVQSsvAVGTPDYISPEILQAmedgmgKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEE 296
                       250       260
                ....*....|....*....|....*....
gi 15230288 366 SFDEPPWPS-LSFEAKDFVKRLLYKDPRK 393
Cdd:cd05624 297 RFQFPSHVTdVSEEAKDLIQRLICSRERR 325
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
150-408 8.28e-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: 102.81  E-value: 8.28e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKGElkdQEVAVKVIPKSKMTSAISIEDVRREVKILrALSGHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd05597   9 IGRGAFGEVAVVKLKSTE---KVYAMKILNKWEMLKRAETACFREERDVL-VNGDRRWITKLHYAFQDENYLYLVMDYYC 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLSDFVRPDERL--N 307
Cdd:cd05597  85 GGDLLTLLSKFEDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLL---DRNGHIRLADFGSCLKLREDGTVqsS 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 308 DIVGSAYYVAPEVL------HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPW-PSLSFEAK 380
Cdd:cd05597 162 VAVGTPDYISPEILqamedgKGRYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKEHFSFPDDeDDVSEEAK 241
                       250       260       270
                ....*....|....*....|....*....|.
gi 15230288 381 DFVKRLLyKDPRKRMTAS--QALM-HPWIAG 408
Cdd:cd05597 242 DLIRRLI-CSRERRLGQNgiDDFKkHPFFEG 271
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
143-406 1.05e-23

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


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 100.68  E-value: 1.05e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFGYTCSAKFKKGELkDQEVAVKVIPKSKMTSAISiedvrREVKILRALSgHQNLVQFYDAFEDNANVY 222
Cdd:cd14112   4 RFSFGSEIFRGRFSVIVKAVDSTTET-DAHCAVKIFEVSDEASEAV-----REFESLRTLQ-HENVQRLIAAFKPSNFAY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 223 IVMElcgggELLDRILAR---GGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeENSMLKVIDFGLSDF 299
Cdd:cd14112  77 LVME-----KLQEDVFTRfssNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSV-RSWQVKLVDFGRAQK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 300 VRPdERLNDIVGSAYYVAPEVLH--RSYTTEADVWSIGVIAYILLCGSRPFwarTESGIFRAVLKADPSFdEPPWPSLSF 377
Cdd:cd14112 151 VSK-LGKVPVDGDTDWASPEFHNpeTPITVQSDIWGLGVLTFCLLSGFHPF---TSEYDDEEETKENVIF-VKCRPNLIF 225
                       250       260       270
                ....*....|....*....|....*....|....
gi 15230288 378 -----EAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14112 226 veatqEALRFATWALKKSPTRRMRTDEALEHRWL 259
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
148-405 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: 100.96  E-value: 1.31e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIEDVRrEVKILRALSgHQNLVQFYDAFEDNANVYIVMEL 227
Cdd:cd07861   6 EKIGEGTYGVVYKGRNKK---TGQIVAMKKIRLESEEEGVPSTAIR-EISLLKELQ-HPNIVCLEDVLMQENRLYLVFEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 228 --CGGGELLDRIlaRGGKYSEDD-AKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGLS-DFVRPD 303
Cdd:cd07861  81 lsMDLKKYLDSL--PKGKYMDAElVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNK---GVIKLADFGLArAFGIPV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ERLNDIVGSAYYVAPEVLHRS--YTTEADVWSIGVIaYILLCGSRP-FWARTESG----IFRAVLKAD------------ 364
Cdd:cd07861 156 RVYTHEVVTLWYRAPEVLLGSprYSTPVDIWSIGTI-FAEMATKKPlFHGDSEIDqlfrIFRILGTPTediwpgvtslpd 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 15230288 365 --PSFdePPW---------PSLSFEAKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd07861 235 ykNTF--PKWkkgslrtavKNLDEDGLDLLEKMLIYDPAKRISAKKALVHPY 284
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
150-418 1.49e-23

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: 102.82  E-value: 1.49e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKfkKGELKdQEVAVKVIPKSKMTSAISIEDVRREVKILrALSGHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd05625   9 LGIGAFGEVCLAR--KVDTK-ALYATKTLRKKDVLLRNQVAHVKAERDIL-AEADNEWVVRLYYSFQDKDNLYFVMDYIP 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDrILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGL------------- 296
Cdd:cd05625  85 GGDMMS-LLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILI---DRDGHIKLTDFGLctgfrwthdskyy 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 297 -------------------------SDFVRPDER----------LNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYI 340
Cdd:cd05625 161 qsgdhlrqdsmdfsnewgdpencrcGDRLKPLERraarqhqrclAHSLVGTPNYIAPEVLLRTgYTQLCDWWSVGVILFE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 341 LLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDFVKRLLyKDPRKRM---TASQALMHPWiagYKKIDIPFD 417
Cdd:cd05625 241 MLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLC-RGPEDRLgknGADEIKAHPF---FKTIDFSSD 316

                .
gi 15230288 418 I 418
Cdd:cd05625 317 L 317
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
150-425 1.54e-23

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: 101.49  E-value: 1.54e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKfKKGELKdqEVAVKVIPKSKMTSAISIEDVRREVKILrALSGHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd05585   2 IGKGSFGKVMQVR-KKDTSR--IYALKTIRKAHIVSRSEVTHTLAERTVL-AQVDCPFIVPLKFSFQSPEKLYLVLAFIN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRiLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFL--YTSKeensmLKVIDFGLSDF-VRPDERL 306
Cdd:cd05585  78 GGELFHH-LQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILldYTGH-----IALCDFGLCKLnMKDDDKT 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 307 NDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKaDPSFDEPPWPSlsfEAKDFVKR 385
Cdd:cd05585 152 NTFCGTPEYLAPELLlGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQ-EPLRFPDGFDR---DAKDLLIG 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 15230288 386 LLYKDPRKRM---TASQALMHPWIAgykkiDIPFDILIFKQIK 425
Cdd:cd05585 228 LLNRDPTKRLgynGAQEIKNHPFFD-----QIDWKRLLMKKIQ 265
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
149-405 2.48e-23

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: 100.82  E-value: 2.48e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 149 EIGRGHFGYTCSAKFKKGELKdQEVAVKVI--PKSKMT----SAIsiedvrREVKILRALSgHQNLVQFYDAFEDNAN-- 220
Cdd:cd07842   7 CIGRGTYGRVYKAKRKNGKDG-KEYAIKKFkgDKEQYTgisqSAC------REIALLRELK-HENVVSLVEVFLEHADks 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 VYIVMELCgggE--LLDRI----LARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSK-EENSMLKVID 293
Cdd:cd07842  79 VYLLFDYA---EhdLWQIIkfhrQAKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVMGEgPERGVVKIGD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 294 FGLSDFV----RPDERLNDIVGSAYYVAPEVL--HRSYTTEADVWSIGVIAYILLCGSRPFWARTES------------- 354
Cdd:cd07842 156 LGLARLFnaplKPLADLDPVVVTIWYRAPELLlgARHYTKAIDIWAIGCIFAELLTLEPIFKGREAKikksnpfqrdqle 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 355 GIFRavLKADPSFDE-------PPWPSL--SFEAKDFVKRLLYK----------------------DPRKRMTASQALMH 403
Cdd:cd07842 236 RIFE--VLGTPTEKDwpdikkmPEYDTLksDTKASTYPNSLLAKwmhkhkkpdsqgfdllrklleyDPTKRITAEEALEH 313

                ..
gi 15230288 404 PW 405
Cdd:cd07842 314 PY 315
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
143-315 3.69e-23

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: 99.07  E-value: 3.69e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAIsiedvRREVKILRALSGHQNLVQFYDAFEDNANVY 222
Cdd:cd14016   1 RYKLVKKIGSGSFGEVYLGIDLK---TGEEVAIKIEKKDSKHPQL-----EYEAKVYKLLQGGPGIPRLYWFGQEGDYNV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 223 IVMELCGggELLDRILAR-GGKYSEddaKAVL---IQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLSD 298
Cdd:cd14016  73 MVMDLLG--PSLEDLFNKcGRKFSL---KTVLmlaDQMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNKVYLIDFGLAK 147
                       170       180
                ....*....|....*....|....*
gi 15230288 299 FVRPDERLNDI--------VGSAYY 315
Cdd:cd14016 148 KYRDPRTGKHIpyregkslTGTARY 172
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
148-405 3.69e-23

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 99.89  E-value: 3.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  148 EEIGRGHFGYTCSAKFKkgeLKDQEVAVKVIPKSKMTSAISIEDVRrEVKILRALSgHQNLVQFYDAFEDNANVYIVMEL 227
Cdd:PLN00009   8 EKIGEGTYGVVYKARDR---VTNETIALKKIRLEQEDEGVPSTAIR-EISLLKEMQ-HGNIVRLQDVVHSEKRLYLVFEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  228 cgggelLDRILARGGKYSEDDA------KAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeeNSMLKVIDFGLSD-FV 300
Cdd:PLN00009  83 ------LDLDLKKHMDSSPDFAknprliKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRR--TNALKLADFGLARaFG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  301 RPDERLNDIVGSAYYVAPEVL--HRSYTTEADVWSIGVIaYILLCGSRP-FWARTE----SGIFRAV----------LKA 363
Cdd:PLN00009 155 IPVRTFTHEVVTLWYRAPEILlgSRHYSTPVDIWSVGCI-FAEMVNQKPlFPGDSEidelFKIFRILgtpneetwpgVTS 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15230288  364 DPSFDE--PPW---------PSLSFEAKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:PLN00009 234 LPDYKSafPKWppkdlatvvPTLEPAGVDLLSKMLRLDPSKRITARAALEHEY 286
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
150-387 3.83e-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: 101.30  E-value: 3.83e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKGElkdQEVAVKVIPKSKMT----SAISIEDvrREVkilRALSGHQNLVQFYDAFEDNANVYIVM 225
Cdd:cd05596  34 IGRGAFGEVQLVRHKSTK---KVYAMKLLSKFEMIkrsdSAFFWEE--RDI---MAHANSEWIVQLHYAFQDDKYLYMVM 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 226 ELCGGGELLDriLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSdfVRPDE- 304
Cdd:cd05596 106 DYMPGGDLVN--LMSNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDA---SGHLKLADFGTC--MKMDKd 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 305 ---RLNDIVGSAYYVAPEVL-----HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLS 376
Cdd:cd05596 179 glvRSDTAVGTPDYISPEVLksqggDGVYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIMNHKNSLQFPDDVEIS 258
                       250
                ....*....|.
gi 15230288 377 FEAKDFVKRLL 387
Cdd:cd05596 259 KDAKSLICAFL 269
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
145-406 4.15e-23

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: 99.05  E-value: 4.15e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKKGELKdqevavKVIPKSKMTSAISIED--VRREVKILRALSgHQNLVQFYDAFED-NANV 221
Cdd:cd08223   3 QFLRVIGKGSYGEVWLVRHKRDRKQ------YVIKKLNLKNASKRERkaAEQEAKLLSKLK-HPNIVSYKESFEGeDGFL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 YIVMELCGGGELLDRILARGGK-YSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPEN-FLYTSKeensMLKVIDFGLSdf 299
Cdd:cd08223  76 YIVMGFCEGGDLYTRLKEQKGVlLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNiFLTKSN----IIKVGDLGIA-- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 300 vRPDERLND----IVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKAdpsfDEPPWPS 374
Cdd:cd08223 150 -RVLESSSDmattLIGTPYYMSPELFsNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEG----KLPPMPK 224
                       250       260       270
                ....*....|....*....|....*....|...
gi 15230288 375 -LSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd08223 225 qYSPELGELIKAMLHQDPEKRPSVKRILRQPYI 257
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
150-416 4.45e-23

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: 101.46  E-value: 4.45e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYT-CSAKFKKGELkdqeVAVKVIPKSKMTSAISIEDVRREVKILrALSGHQNLVQFYDAFEDNANVYIVMELC 228
Cdd:cd05629   9 IGKGAFGEVrLVQKKDTGKI----YAMKTLLKSEMFKKDQLAHVKAERDVL-AESDSPWVVSLYYSFQDAQYLYLIMEFL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 229 GGGELLDrILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLSD---------- 298
Cdd:cd05629  84 PGGDLMT-MLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILI---DRGGHIKLSDFGLSTgfhkqhdsay 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 299 FVRPDER--------------LNDI------------------------VGSAYYVAPEV-LHRSYTTEADVWSIGVIAY 339
Cdd:cd05629 160 YQKLLQGksnknridnrnsvaVDSInltmsskdqiatwkknrrlmaystVGTPDYIAPEIfLQQGYGQECDWWSLGAIMF 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 340 ILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDFVKRLLyKDPRKRM---TASQALMHPWIAGY-----KK 411
Cdd:cd05629 240 ECLIGWPPFCSENSHETYRKIINWRETLYFPDDIHLSVEAEDLIRRLI-TNAENRLgrgGAHEIKSHPFFRGVdwdtiRQ 318

                ....*
gi 15230288 412 IDIPF 416
Cdd:cd05629 319 IRAPF 323
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
148-406 4.49e-23

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: 99.80  E-value: 4.49e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSA-KFKKGelkdQEVAVKvipKSKMTSAISIEDVRREVKILRAlSGHQNLVQFYDAFEDNANVYIVME 226
Cdd:cd06656  25 EKIGQGASGTVYTAiDIATG----QEVAIK---QMNLQQQPKKELIINEILVMRE-NKNPNIVNYLDSYLVGDELWVVME 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 227 LCGGGELLDRILARGgkYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSDFVRPDE-R 305
Cdd:cd06656  97 YLAGGSLTDVVTETC--MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGM---DGSVKLTDFGFCAQITPEQsK 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 306 LNDIVGSAYYVAPEVLHR-SYTTEADVWSIGVIAYILLCGSRPFWARTE-SGIFRAVLKADPSFDEPPWPSLSFeaKDFV 383
Cdd:cd06656 172 RSTMVGTPYWMAPEVVTRkAYGPKVDIWSLGIMAIEMVEGEPPYLNENPlRALYLIATNGTPELQNPERLSAVF--RDFL 249
                       250       260
                ....*....|....*....|...
gi 15230288 384 KRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd06656 250 NRCLEMDVDRRGSAKELLQHPFL 272
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
202-405 4.98e-23

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: 98.20  E-value: 4.98e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 202 LSGHQNLVQFYDAFEDNANVYIVMELcGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYt 281
Cdd:cd14023  41 LPSHRNITGIVEVILGDTKAYVFFEK-DFGDMHSYVRSCK-RLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVF- 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 282 SKEENSMLKVIDFGLSDFVR-PDERLNDIVGSAYYVAPEVLHRSYT---TEADVWSIGVIAYILLCGSRPFWARTESGIF 357
Cdd:cd14023 118 SDEERTQLRLESLEDTHIMKgEDDALSDKHGCPAYVSPEILNTTGTysgKSADVWSLGVMLYTLLVGRYPFHDSDPSALF 197
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15230288 358 RAVLKADPSFDEppwpSLSFEAKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd14023 198 SKIRRGQFCIPD----HVSPKARCLIRSLLRREPSERLTAPEILLHPW 241
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
150-417 5.43e-23

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 100.36  E-value: 5.43e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSkMTSAISIEDVRREVKILRALSgHQNLVQFYDAF------EDNANVYI 223
Cdd:cd07879  23 VGSGAYGSVCSAIDKR---TGEKVAIKKLSRP-FQSEIFAKRAYRELTLLKHMQ-HENVIGLLDVFtsavsgDEFQDFYL 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCgggeLLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFlytSKEENSMLKVIDFGLSDfvRPD 303
Cdd:cd07879  98 VMPYM----QTDLQKIMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNL---AVNEDCELKILDFGLAR--HAD 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ERLNDIVGSAYYVAPEV----LHrsYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKAD----PSFDE------ 369
Cdd:cd07879 169 AEMTGYVVTRWYRAPEVilnwMH--YNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILKVTgvpgPEFVQkledka 246
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 370 --------PPWPSLSF---------EAKDFVKRLLYKDPRKRMTASQALMHPWIAGYKKID-----IPFD 417
Cdd:cd07879 247 aksyikslPKYPRKDFstlfpkaspQAVDLLEKMLELDVDKRLTATEALEHPYFDSFRDADeeteqQPYD 316
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
137-419 5.91e-23

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 100.22  E-value: 5.91e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  137 SKELQSR-IELGEEIGRGHFGytcsaKFKKGE--LKDQEVAVKVIPKSKMTSAISIED-----------VRREVKILRAL 202
Cdd:PTZ00024   3 SFSISERyIQKGAHLGEGTYG-----KVEKAYdtLTGKIVAIKKVKIIEISNDVTKDRqlvgmcgihftTLRELKIMNEI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  203 SgHQNLVQFYDAFEDNANVYIVMELCGGGelLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTS 282
Cdd:PTZ00024  78 K-HENIMGLVDVYVEGDFINLVMDIMASD--LKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  283 KEEnsmLKVIDFGLS---------------DFVRPDERLNDIVGSAYYVAPEVLHRS--YTTEADVWSIGVIAYILLCGS 345
Cdd:PTZ00024 155 KGI---CKIADFGLArrygyppysdtlskdETMQRREEMTSKVVTLWYRAPELLMGAekYHFAVDMWSVGCIFAELLTGK 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  346 RPFWARTE----SGIFRavLKADPSfdEPPWPS-----LSFE-------------------AKDFVKRLLYKDPRKRMTA 397
Cdd:PTZ00024 232 PLFPGENEidqlGRIFE--LLGTPN--EDNWPQakklpLYTEftprkpkdlktifpnasddAIDLLQSLLKLNPLERISA 307
                        330       340
                 ....*....|....*....|....*.
gi 15230288  398 SQALMHPWIAGY----KKIDIPFDIL 419
Cdd:PTZ00024 308 KEALKHEYFKSDplpcDPSQLPFNFL 333
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
134-405 5.93e-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: 99.75  E-value: 5.93e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 134 FGFSKELqSRIELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIEDVRrEVKILRALSgHQNLVQFYD 213
Cdd:cd07865   5 FPFCDEV-SKYEKLAKIGQGTFGEVFKARHRK---TGQIVALKKVLMENEKEGFPITALR-EIKILQLLK-HENVVNLIE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 214 -----AFEDN---ANVYIVMELCgggellDRILAR-----GGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLY 280
Cdd:cd07865  79 icrtkATPYNrykGSIYLVFEFC------EHDLAGllsnkNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILI 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 281 TskeENSMLKVIDFGLS-DFVRPDE----RLNDIVGSAYYVAPEVL--HRSYTTEADVWSIGVIA--------------- 338
Cdd:cd07865 153 T---KDGVLKLADFGLArAFSLAKNsqpnRYTNRVVTLWYRPPELLlgERDYGPPIDMWGAGCIMaemwtrspimqgnte 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 339 ------YILLCGS-----------RPFWARTE--SGIFRAV-LKADPSFDEPpwpslsfEAKDFVKRLLYKDPRKRMTAS 398
Cdd:cd07865 230 qhqltlISQLCGSitpevwpgvdkLELFKKMElpQGQKRKVkERLKPYVKDP-------YALDLIDKLLVLDPAKRIDAD 302

                ....*..
gi 15230288 399 QALMHPW 405
Cdd:cd07865 303 TALNHDF 309
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
145-395 5.97e-23

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: 100.87  E-value: 5.97e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIV 224
Cdd:cd05617  18 DLIRVIGRGSYAKVLLVRLKK---NDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGELLDRiLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGL-SDFVRPD 303
Cdd:cd05617  95 IEYVNGGDLMFH-MQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLL---DADGHIKLTDYGMcKEGLGPG 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ERLNDIVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPF-------WARTESGIFRAVLKADPSFDEppwpSL 375
Cdd:cd05617 171 DTTSTFCGTPNYIAPEILRgEEYGFSVDWWALGVLMFEMMAGRSPFdiitdnpDMNTEDYLFQVILEKPIRIPR----FL 246
                       250       260
                ....*....|....*....|
gi 15230288 376 SFEAKDFVKRLLYKDPRKRM 395
Cdd:cd05617 247 SVKASHVLKGFLNKDPKERL 266
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
144-401 6.30e-23

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: 98.58  E-value: 6.30e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 144 IELGEEIGRGHFGYTCSAKFKKgelkdqEVAVKVIPKSKMTSAiSIEDVRREVKILRAlSGHQNLVQFYDAFEDNANVYI 223
Cdd:cd14063   2 LEIKEVIGKGRFGRVHRGRWHG------DVAIKLLNIDYLNEE-QLEAFKEEVAAYKN-TRHDNLVLFMGACMDPPHLAI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDRIlaRGGKYSEDDAKAVLI--QILNVVAFCHLQGVVHRDLKPENFLYtskeENSMLKVIDFGL---SD 298
Cdd:cd14063  74 VTSLCKGRTLYSLI--HERKEKFDFNKTVQIaqQICQGMGYLHAKGIIHKDLKSKNIFL----ENGRVVITDFGLfslSG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 299 FVRPDERLNDIV---GSAYYVAPEVLHR-----------SYTTEADVWSIGVIAYILLCGSRPFWART-ESGIFRAVLKA 363
Cdd:cd14063 148 LLQPGRREDTLVipnGWLCYLAPEIIRAlspdldfeeslPFTKASDVYAFGTVWYELLAGRWPFKEQPaESIIWQVGCGK 227
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 15230288 364 DPSFDEppwPSLSFEAKDFVKRLLYKDPRKRMTASQAL 401
Cdd:cd14063 228 KQSLSQ---LDIGREVKDILMQCWAYDPEKRPTFSDLL 262
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
141-406 7.83e-23

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: 98.58  E-value: 7.83e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 141 QSRIELGEEIGRGHFGYTCSAK-FKKGELkdqeVAVKVIpksKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNA 219
Cdd:cd06645  10 QEDFELIQRIGSGTYGDVYKARnVNTGEL----AAIKVI---KLEPGEDFAVVQQEIIMMKDCK-HSNIVAYFGSYLRRD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 220 NVYIVMELCGGGELLDrILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDF 299
Cdd:cd06645  82 KLWICMEFCGGGSLQD-IYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLT---DNGHVKLADFGVSAQ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 300 VRPD-ERLNDIVGSAYYVAPEV--LHRS--YTTEADVWSIGVIAYILLCGSRPFWartESGIFRAVLKADPSFDEPP--- 371
Cdd:cd06645 158 ITATiAKRKSFIGTPYWMAPEVaaVERKggYNQLCDIWAVGITAIELAELQPPMF---DLHPMRALFLMTKSNFQPPklk 234
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 15230288 372 ----WPSlSFEakDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd06645 235 dkmkWSN-SFH--HFVKMALTKNPKKRPTAEKLLQHPFV 270
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
150-399 7.93e-23

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: 100.07  E-value: 7.93e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd05615  18 LGKGSFGKVMLAERKG---SDELYAIKILKKDVVIQDDDVECTMVEKRVLALQDKPPFLTQLHSCFQTVDRLYFVMEYVN 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRIlARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGL-SDFVRPDERLND 308
Cdd:cd05615  95 GGDLMYHI-QQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSE---GHIKIADFGMcKEHMVEGVTTRT 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 309 IVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEppwpSLSFEAKDFVKRLL 387
Cdd:cd05615 171 FCGTPDYIAPEIIaYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPK----SLSKEAVSICKGLM 246
                       250
                ....*....|..
gi 15230288 388 YKDPRKRMTASQ 399
Cdd:cd05615 247 TKHPAKRLGCGP 258
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
148-404 7.94e-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: 98.63  E-value: 7.94e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFG--YTCsakfkkgeLKDQEVAVKVIPKSKMTSAISIEDVR--REVKILRALSGHQNLVQFYDAFEDNANVYI 223
Cdd:cd14051   6 EKIGSGEFGsvYKC--------INRLDGCVYAIKKSKKPVAGSVDEQNalNEVYAHAVLGKHPHVVRYYSAWAEDDHMII 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDRILAR---GGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENfLYTSKEENSMLKVIDFGLSDFV 300
Cdd:cd14051  78 QNEYCNGGSLADAISENekaGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGN-IFISRTPNPVSSEEEEEDFEGE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 301 RPDERLNDIV-------------------GSAYYVAPEVLHRSYT--TEADVWSIGVIAYILLCGSR-----PFWARTES 354
Cdd:cd14051 157 EDNPESNEVTykigdlghvtsisnpqveeGDCRFLANEILQENYShlPKADIFALALTVYEAAGGGPlpkngDEWHEIRQ 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 15230288 355 GIFravlkadpsfdePPWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHP 404
Cdd:cd14051 237 GNL------------PPLPQCSPEFNELLRSMIHPDPEKRPSAAALLQHP 274
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
146-406 9.08e-23

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: 98.19  E-value: 9.08e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 146 LGEEIGRGHFG--YTCSAKFKKGELKDQEVAVKviPKSKMTSAiSIEDVRREVKILRALSgHQNLVQFYDAFED--NANV 221
Cdd:cd06652   6 LGKLLGQGAFGrvYLCYDADTGRELAVKQVQFD--PESPETSK-EVNALECEIQLLKNLL-HERIVQYYGCLRDpqERTL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 YIVMELCGGGELLDRILARGGkYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLytsKEENSMLKVIDFGLSDFVR 301
Cdd:cd06652  82 SIFMEYMPGGSIKDQLKSYGA-LTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANIL---RDSVGNVKLGDFGASKRLQ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 302 ----PDERLNDIVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCgSRPFWARTE--SGIFRavLKADPSFDEPPwPS 374
Cdd:cd06652 158 ticlSGTGMKSVTGTPYWMSPEVISgEGYGRKADIWSVGCTVVEMLT-EKPPWAEFEamAAIFK--IATQPTNPQLP-AH 233
                       250       260       270
                ....*....|....*....|....*....|..
gi 15230288 375 LSFEAKDFVKRlLYKDPRKRMTASQALMHPWI 406
Cdd:cd06652 234 VSDHCRDFLKR-IFVEAKLRPSADELLRHTFV 264
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
145-387 1.01e-22

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: 100.86  E-value: 1.01e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKKGelkDQEVAVKVIPKSKMTSAISIEDVRREVKILraLSGH-QNLVQFYDAFEDNANVYI 223
Cdd:cd05623  75 EILKVIGRGAFGEVAVVKLKNA---DKVFAMKILNKWEMLKRAETACFREERDVL--VNGDsQWITTLHYAFQDDNNLYL 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLSDFVRPD 303
Cdd:cd05623 150 VMDYYVGGDLLTLLSKFEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILM---DMNGHIRLADFGSCLKLMED 226
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ERLND--IVGSAYYVAPEVLHR------SYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPS- 374
Cdd:cd05623 227 GTVQSsvAVGTPDYISPEILQAmedgkgKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKERFQFPTQVTd 306
                       250
                ....*....|...
gi 15230288 375 LSFEAKDFVKRLL 387
Cdd:cd05623 307 VSENAKDLIRRLI 319
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
150-348 1.19e-22

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: 98.29  E-value: 1.19e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKgelKDQEVAVKvipKSKMTSAISIEDVRR---EVKILRALSgHQNLVQFYD------AFEDNAN 220
Cdd:cd13989   1 LGSGGFGYVTLWKHQD---TGEYVAIK---KCRQELSPSDKNRERwclEVQIMKKLN-HPNVVSARDvppeleKLSPNDL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 VYIVMELCGGGELlDRILARGGKYS---EDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLS 297
Cdd:cd13989  74 PLLAMEYCSGGDL-RKVLNQPENCCglkESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGRVIYKLIDLGYA 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15230288 298 DFVRPDERLNDIVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPF 348
Cdd:cd13989 153 KELDQGSLCTSFVGTLQYLAPELFEsKKYTCTVDYWSFGTLAFECITGYRPF 204
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
197-406 1.31e-22

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: 97.11  E-value: 1.31e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 197 KILRA---LSGHQNLVQFYDAFEDNANVYIVMELcGGGELLDRILARGgKYSEDDAKAVLIQILNVVAFCHLQGVVHRDL 273
Cdd:cd13976  33 AVLRAyfrLPSHPNISGVHEVIAGETKAYVFFER-DHGDLHSYVRSRK-RLREPEAARLFRQIASAVAHCHRNGIVLRDL 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 274 KPENFLYtSKEENSMLKVIDFGLSDFVR-PDERLNDIVGSAYYVAPEVLH--RSYTTE-ADVWSIGVIAYILLCGSRPFW 349
Cdd:cd13976 111 KLRKFVF-ADEERTKLRLESLEDAVILEgEDDSLSDKHGCPAYVSPEILNsgATYSGKaADVWSLGVILYTMLVGRYPFH 189
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15230288 350 ARTESGIFRAVLKADPSFDEppwpSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd13976 190 DSEPASLFAKIRRGQFAIPE----TLSPRARCLIRSLLRREPSERLTAEDILLHPWL 242
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
150-426 2.29e-22

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: 98.16  E-value: 2.29e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKgelkDQEV-AVKVIPKSKMTSAISIEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIVMELC 228
Cdd:cd05575   3 IGKGSFGKVLLARHKA----EGKLyAVKVLQKKAILKRNEVKHIMAERNVLLKNVKHPFLVGLHYSFQTKDKLYFVLDYV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 229 GGGELLDRiLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGL-SDFVRPDERLN 307
Cdd:cd05575  79 NGGELFFH-LQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQ---GHVVLTDFGLcKEGIEPSDTTS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 308 DIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDeppwPSLSFEAKDFVKRL 386
Cdd:cd05575 155 TFCGTPEYLAPEVLRKQpYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLR----TNVSPSARDLLEGL 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15230288 387 LYKDPRKRMTASQALM----HPWIAgykkiDIPFDILIFKQIKA 426
Cdd:cd05575 231 LQKDRTKRLGSGNDFLeiknHSFFR-----PINWDDLEAKKIPP 269
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
145-403 2.41e-22

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: 97.25  E-value: 2.41e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKkgeLKDQEVAVKVIPKSKMTSAIsiEDVRREVKILRALSgHQNLVQFYDAF--------- 215
Cdd:cd14048   9 EPIQCLGRGGFGVVFEAKNK---VDDCNYAVKRIRLPNNELAR--EKVLREVRALAKLD-HPGIVRYFNAWlerppegwq 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 216 --EDNANVYIVMELCGGGELLDRILARGGKYSED--DAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKV 291
Cdd:cd14048  83 ekMDEVYLYIQMQLCRKENLKDWMNRRCTMESRElfVCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSL---DDVVKV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 292 IDFGLSDFVRPDERLNDI-------------VGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLcgsRPFWARTES-GI 356
Cdd:cd14048 160 GDFGLVTAMDQGEPEQTVltpmpayakhtgqVGTRLYMSPEQIHgNQYSEKVDIFALGLILFELI---YSFSTQMERiRT 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 15230288 357 FRAV--LKADPSFDEpPWPslsfEAKDFVKRLLYKDPRKRMTASQALMH 403
Cdd:cd14048 237 LTDVrkLKFPALFTN-KYP----EERDMVQQMLSPSPSERPEAHEVIEH 280
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
150-417 2.54e-22

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: 98.11  E-value: 2.54e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKfkkGELKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd05604   4 IGKGSFGKVLLAK---RKRDGKYYAVKVLQKKVILNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRiLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGL-SDFVRPDERLND 308
Cdd:cd05604  81 GGELFFH-LQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQ---GHIVLTDFGLcKEGISNSDTTTT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 309 IVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDeppwPSLSFEAKDFVKRLL 387
Cdd:cd05604 157 FCGTPEYLAPEVIRKQpYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLR----PGISLTAWSILEELL 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15230288 388 YKDPRKRMTASQALM----HPWIAGY-------KKIDIPFD 417
Cdd:cd05604 233 EKDRQLRLGAKEDFLeiknHPFFESInwtdlvqKKIPPPFN 273
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
141-406 3.17e-22

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: 96.64  E-value: 3.17e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 141 QSRIELGEEIGRGHFGYTCSA-KFKKGELkdqeVAVKVIpksKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNA 219
Cdd:cd06646   8 QHDYELIQRVGSGTYGDVYKArNLHTGEL----AAVKII---KLEPGDDFSLIQQEIFMVKECK-HCNIVAYFGSYLSRE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 220 NVYIVMELCGGGELLDrILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDF 299
Cdd:cd06646  80 KLWICMEYCGGGSLQD-IYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLT---DNGDVKLADFGVAAK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 300 VRPD-ERLNDIVGSAYYVAPEVL----HRSYTTEADVWSIGVIAYILLCGSRPFWartESGIFRAVLKADPSFDEPP--- 371
Cdd:cd06646 156 ITATiAKRKSFIGTPYWMAPEVAavekNGGYNQLCDIWAVGITAIELAELQPPMF---DLHPMRALFLMSKSNFQPPklk 232
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 15230288 372 ----WpSLSFEakDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd06646 233 dktkW-SSTFH--NFVKISLTKNPKKRPTAERLLTHLFV 268
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
145-406 3.21e-22

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: 96.19  E-value: 3.21e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKfkkgELKDQ-EVAVKVIPKSKMTSAISIEDVRR---EVKILRAL-SGHQNLVQFYDAFEDNA 219
Cdd:cd14100   3 QVGPLLGSGGFGSVYSGI----RVADGaPVAIKHVEKDRVSEWGELPNGTRvpmEIVLLKKVgSGFRGVIRLLDWFERPD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 220 NVYIVMELCGG-GELLDRILARGGkYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENsmLKVIDFGLSD 298
Cdd:cd14100  79 SFVLVLERPEPvQDLFDFITERGA-LPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDLNTGE--LKLIDFGSGA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 299 FVRpDERLNDIVGSAYYVAPEVL--HRSYTTEADVWSIGVIAYILLCGSRPFWARTEsgifraVLKADPSFDEppwpSLS 376
Cdd:cd14100 156 LLK-DTVYTDFDGTRVYSPPEWIrfHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEE------IIRGQVFFRQ----RVS 224
                       250       260       270
                ....*....|....*....|....*....|
gi 15230288 377 FEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14100 225 SECQHLIKWCLALRPSDRPSFEDIQNHPWM 254
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
150-406 3.45e-22

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: 97.87  E-value: 3.45e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKfkkGELKDQEVAVKVI--PKSKMTSAisiEDVRREVKILRALSgHQNLVQFYDAF------EDNANV 221
Cdd:cd07850   8 IGSGAQGIVCAAY---DTVTGQNVAIKKLsrPFQNVTHA---KRAYRELVLMKLVN-HKNIIGLLNVFtpqkslEEFQDV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 YIVME-----LCgggELLDRILarggkySEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGL 296
Cdd:cd07850  81 YLVMElmdanLC---QVIQMDL------DHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKS---DCTLKILDFGL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 297 SDFVRPDERLNDIVGSAYYVAPEV-LHRSYTTEADVWSIGVIAYILLCGSRPF--------WAR------TESGIFRAVL 361
Cdd:cd07850 149 ARTAGTSFMMTPYVVTRYYRAPEViLGMGYKENVDIWSVGCIMGEMIRGTVLFpgtdhidqWNKiieqlgTPSDEFMSRL 228
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15230288 362 KadPSF-----DEPPWPSLSFE----------------------AKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd07850 229 Q--PTVrnyveNRPKYAGYSFEelfpdvlfppdseehnklkasqARDLLSKMLVIDPEKRISVDDALQHPYI 298
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
147-405 3.81e-22

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: 96.69  E-value: 3.81e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 147 GEEIGRGHFG--YTCSAKFKKGELKDQEVAVKviPKSKMTSAiSIEDVRREVKILRALSgHQNLVQFYDAFEDNA--NVY 222
Cdd:cd06651  12 GKLLGQGAFGrvYLCYDVDTGRELAAKQVQFD--PESPETSK-EVSALECEIQLLKNLQ-HERIVQYYGCLRDRAekTLT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 223 IVMELCGGGELLDRILARGGkYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLytsKEENSMLKVIDFGLSDFVR- 301
Cdd:cd06651  88 IFMEYMPGGSVKDQLKAYGA-LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL---RDSAGNVKLGDFGASKRLQt 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 302 ---PDERLNDIVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCgSRPFWARTESgiFRAVLKADPSFDEPPWPS-LS 376
Cdd:cd06651 164 icmSGTGIRSVTGTPYWMSPEVISgEGYGRKADVWSLGCTVVEMLT-EKPPWAEYEA--MAAIFKIATQPTNPQLPShIS 240
                       250       260
                ....*....|....*....|....*....
gi 15230288 377 FEAKDFVKRlLYKDPRKRMTASQALMHPW 405
Cdd:cd06651 241 EHARDFLGC-IFVEARHRPSAEELLRHPF 268
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
148-406 4.11e-22

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: 97.10  E-value: 4.11e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKfkkGELKDQEVAVKvipKSKMTSAISIEDVRREVKILRAlSGHQNLVQFYDAFEDNANVYIVMEL 227
Cdd:cd06654  26 EKIGQGASGTVYTAM---DVATGQEVAIR---QMNLQQQPKKELIINEILVMRE-NKNPNIVNYLDSYLVGDELWVVMEY 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 228 CGGGELLDRILARGgkYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSDFVRPDE-RL 306
Cdd:cd06654  99 LAGGSLTDVVTETC--MDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGM---DGSVKLTDFGFCAQITPEQsKR 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 307 NDIVGSAYYVAPEVLHR-SYTTEADVWSIGVIAYILLCGSRPFWARTE-SGIFRAVLKADPSFDEPPWPSLSFeaKDFVK 384
Cdd:cd06654 174 STMVGTPYWMAPEVVTRkAYGPKVDIWSLGIMAIEMIEGEPPYLNENPlRALYLIATNGTPELQNPEKLSAIF--RDFLN 251
                       250       260
                ....*....|....*....|..
gi 15230288 385 RLLYKDPRKRMTASQALMHPWI 406
Cdd:cd06654 252 RCLEMDVEKRGSAKELLQHQFL 273
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
150-418 4.29e-22

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: 98.55  E-value: 4.29e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSA-KFKKGELkdqeVAVKVIPKSKMTSAISIEDVRREVKILrALSGHQNLVQFYDAFEDNANVYIVMELC 228
Cdd:cd05626   9 LGIGAFGEVCLAcKVDTHAL----YAMKTLRKKDVLNRNQVAHVKAERDIL-AEADNEWVVKLYYSFQDKDNLYFVMDYI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 229 GGGELLDrILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGL------------ 296
Cdd:cd05626  84 PGGDMMS-LLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILI---DLDGHIKLTDFGLctgfrwthnsky 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 297 --------SDFVRPDERLNDI----------------------------VGSAYYVAPEVLHRS-YTTEADVWSIGVIAY 339
Cdd:cd05626 160 yqkgshirQDSMEPSDLWDDVsncrcgdrlktleqratkqhqrclahslVGTPNYIAPEVLLRKgYTQLCDWWSVGVILF 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 340 ILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDFVKRLL--YKDPRKRMTASQALMHPWiagYKKIDIPFD 417
Cdd:cd05626 240 EMLVGQPPFLAPTPTETQLKVINWENTLHIPPQVKLSPEAVDLITKLCcsAEERLGRNGADDIKAHPF---FSEVDFSSD 316

                .
gi 15230288 418 I 418
Cdd:cd05626 317 I 317
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
150-395 4.48e-22

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: 98.18  E-value: 4.48e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd05618  28 IGRGSYAKVLLVRLKK---TERIYAMKVVKKELVNDDEDIDWVQTEKHVFEQASNHPFLVGLHSCFQTESRLFFVIEYVN 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRiLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGL-SDFVRPDERLND 308
Cdd:cd05618 105 GGDLMFH-MQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSE---GHIKLTDYGMcKEGLRPGDTTST 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 309 IVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPF---------WARTESGIFRAVLKADPSFDEppwpSLSFE 378
Cdd:cd05618 181 FCGTPNYIAPEILRgEDYGFSVDWWALGVLMFEMMAGRSPFdivgssdnpDQNTEDYLFQVILEKQIRIPR----SLSVK 256
                       250
                ....*....|....*..
gi 15230288 379 AKDFVKRLLYKDPRKRM 395
Cdd:cd05618 257 AASVLKSFLNKDPKERL 273
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
147-404 6.31e-22

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: 95.57  E-value: 6.31e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 147 GEEIGRGHFGYTCSAK-FKKGELkdqeVAVKVIP---KSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVY 222
Cdd:cd06630   5 GPLLGTGAFSSCYQARdVKTGTL----MAVKQVSfcrNSSSEQEEVVEAIREEIRMMARLN-HPNIVRMLGATQHKSHFN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 223 IVMELCGGGELlDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENsmLKVIDFGL-----S 297
Cdd:cd06630  80 IFVEWMAGGSV-ASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGQR--LRIADFGAaarlaS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 298 DFVRPDERLNDIVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWP-SL 375
Cdd:cd06630 157 KGTGAGEFQGQLLGTIAFMAPEVLRgEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIFKIASATTPPPIPeHL 236
                       250       260
                ....*....|....*....|....*....
gi 15230288 376 SFEAKDFVKRLLYKDPRKRMTASQALMHP 404
Cdd:cd06630 237 SPGLRDVTLRCLELQPEDRPPARELLKHP 265
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
189-404 6.69e-22

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 95.50  E-value: 6.69e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 189 IEDVRREVKILRALSgHQNLVQFYdAF-----EDNAN--VYIVMELCGGGELLDrILARGGKYSEDDAKAVLIQILNVVA 261
Cdd:cd14012  42 IQLLEKELESLKKLR-HPNLVSYL-AFsierrGRSDGwkVYLLTEYAPGGSLSE-LLDSVGSVPLDTARRWTLQLLEALE 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 262 FCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLSdfvrpdERLNDIVG--------SAYYVAPEVL--HRSYTTEADV 331
Cdd:cd14012 119 YLHRNGVVHKSLHAGNVLLDRDAGTGIVKLTDYSLG------KTLLDMCSrgsldefkQTYWLPPELAqgSKSPTRKTDV 192
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15230288 332 WSIGVIAYILLCGSRPF-WARTESGiFRAVLKADPSFDeppwpslsfeakDFVKRLLYKDPRKRMTASQALMHP 404
Cdd:cd14012 193 WDLGLLFLQMLFGLDVLeKYTSPNP-VLVSLDLSASLQ------------DFLSKCLSLDPKKRPTALELLPHE 253
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
188-394 7.39e-22

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: 95.81  E-value: 7.39e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 188 SIEDVRREVKILRALSGHQNLVQFYDAF-----EDNANVYIVMELCGGGELLDRILAR-GGKYSEDDAKAVLIQILNVVA 261
Cdd:cd14037  43 DLNVCKREIEIMKRLSGHKNIVGYIDSSanrsgNGVYEVLLLMEYCKGGGVIDLMNQRlQTGLTESEILKIFCDVCEAVA 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 262 FCHL--QGVVHRDLKPENFLYTSKEEnsmLKVIDFGLSDFVRPDERLNDIVG----------SAYYVAPEV--LHR--SY 325
Cdd:cd14037 123 AMHYlkPPLIHRDLKVENVLISDSGN---YKLCDFGSATTKILPPQTKQGVTyveedikkytTLQYRAPEMidLYRgkPI 199
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15230288 326 TTEADVWSIGVIAYILLCGSRPFwarTESGIFrAVLKADPSFdePPWPSLSFEAKDFVKRLLYKDPRKR 394
Cdd:cd14037 200 TEKSDIWALGCLLYKLCFYTTPF---EESGQL-AILNGNFTF--PDNSRYSKRLHKLIRYMLEEDPEKR 262
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
150-348 7.64e-22

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: 95.15  E-value: 7.64e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGytcsaKFKKGELKDQEVAVKVI---PKSKMtsAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVME 226
Cdd:cd14061   2 IGVGGFG-----KVYRGIWRGEEVAVKAArqdPDEDI--SVTLENVRQEARLFWMLR-HPNIIALRGVCLQPPNLCLVME 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 227 LCGGGELlDRILArggKYSEDDAKAV--LIQILNVVAFCHLQG---VVHRDLKPENFLYTSKEE-----NSMLKVIDFGL 296
Cdd:cd14061  74 YARGGAL-NRVLA---GRKIPPHVLVdwAIQIARGMNYLHNEApvpIIHRDLKSSNILILEAIEnedleNKTLKITDFGL 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15230288 297 SDFVRPDERLnDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPF 348
Cdd:cd14061 150 AREWHKTTRM-SAAGTYAWMAPEVIKSStFSKASDVWSYGVLLWELLTGEVPY 201
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
193-401 9.08e-22

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 98.55  E-value: 9.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  193 RREVKILRALSgHQNLVQFYDAFEDNANVYIVMELCGGGELLDRILARGGK---YSEDDAKAVLIQILNVVAFCHLQGVV 269
Cdd:PTZ00267 113 RSELHCLAACD-HFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQIKQRLKEhlpFQEYEVGLLFYQIVLALDEVHSRKMM 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  270 HRDLKPEN-FLYTSkeenSMLKVIDFGLS----DFVRPDERlNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLC 343
Cdd:PTZ00267 192 HRDLKSANiFLMPT----GIIKLGDFGFSkqysDSVSLDVA-SSFCGTPYYLAPELWERKrYSKKADMWSLGVILYELLT 266
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15230288  344 GSRPFWARTESGIFRAVLKADpsFDEPPWPsLSFEAKDFVKRLLYKDPRKRMTASQAL 401
Cdd:PTZ00267 267 LHRPFKGPSQREIMQQVLYGK--YDPFPCP-VSSGMKALLDPLLSKNPALRPTTQQLL 321
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
144-337 1.03e-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: 94.72  E-value: 1.03e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 144 IELGEEIGRGHFGytcsaKFKKGELKDQEVAVKVIpKSKMTSAISIEDvrrEVKILRALSgHQNLVQFYDAFEDNANVYI 223
Cdd:cd05039   8 LKLGELIGKGEFG-----DVMLGDYRGQKVAVKCL-KDDSTAAQAFLA---EASVMTTLR-HPNLVQLLGVVLEGNGLYI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDRILARGGKYSE-DDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDfvrp 302
Cdd:cd05039  78 VTEYMAKGSLVDYLRSRGRAVITrKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVS---EDNVAKVSDFGLAK---- 150
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 15230288 303 DERLNDIVGS--AYYVAPEVL-HRSYTTEADVWSIGVI 337
Cdd:cd05039 151 EASSNQDGGKlpIKWTAPEALrEKKFSTKSDVWSFGIL 188
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
143-358 1.47e-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: 1.47e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKvipKSKMTSAISIEDVRREVKILRAL-SGHQNLVQFYDAFEDNANV 221
Cdd:cd13977   1 KYSLIREVGRGSYGVVYEAVVRR---TGARVAVK---KIRCNAPENVELALREFWALSSIqRQHPNVIQLEECVLQRDGL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 ------------------------------------YIVMELCGGGELLDRILARggKYSEDDAKAVLIQILNVVAFCHL 265
Cdd:cd13977  75 aqrmshgssksdlylllvetslkgercfdprsacylWFVMEFCDGGDMNEYLLSR--RPDRQTNTSFMLQLSSALAFLHR 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 266 QGVVHRDLKPENFLYTSKEENSMLKVIDFGLSDF-----VRPDE-------RLNDIVGSAYYVAPEVLHRSYTTEADVWS 333
Cdd:cd13977 153 NQIVHRDLKPDNILISHKRGEPILKVADFGLSKVcsgsgLNPEEpanvnkhFLSSACGSDFYMAPEVWEGHYTAKADIFA 232
                       250       260
                ....*....|....*....|....*
gi 15230288 334 IGVIayillcgsrpFWARTESGIFR 358
Cdd:cd13977 233 LGII----------IWAMVERITFR 247
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
138-383 1.49e-21

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: 96.99  E-value: 1.49e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 138 KELQSRIE---LGEEIGRGHFGYTCSAKFKKGElkdQEVAVKVIPKSKMTSAISIEDVRREVKILrALSGHQNLVQFYDA 214
Cdd:cd05621  45 RELQMKAEdydVVKVIGRGAFGEVQLVRHKASQ---KVYAMKLLSKFEMIKRSDSAFFWEERDIM-AFANSPWVVQLFCA 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 215 FEDNANVYIVMELCGGGELLDriLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDF 294
Cdd:cd05621 121 FQDDKYLYMVMEYMPGGDLVN--LMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLL---DKYGHLKLADF 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 295 GLSdfVRPDE----RLNDIVGSAYYVAPEVLHRS-----YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADP 365
Cdd:cd05621 196 GTC--MKMDEtgmvHCDTAVGTPDYISPEVLKSQggdgyYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDHKN 273
                       250
                ....*....|....*...
gi 15230288 366 SFDEPPWPSLSFEAKDFV 383
Cdd:cd05621 274 SLNFPDDVEISKHAKNLI 291
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
150-385 1.64e-21

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: 96.67  E-value: 1.64e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGytcSAKFKKGELKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSGHQNLVQFYdAFEDNANVYIVMELCG 229
Cdd:cd05627  10 IGRGAFG---EVRLVQKKDTGHIYAMKILRKADMLEKEQVAHIRAERDILVEADGAWVVKMFY-SFQDKRNLYLIMEFLP 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDrILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGLSDFVRPDERLN-- 307
Cdd:cd05627  86 GGDMMT-LLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAK---GHVKLSDFGLCTGLKKAHRTEfy 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 308 ----------------------------------DIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWART 352
Cdd:cd05627 162 rnlthnppsdfsfqnmnskrkaetwkknrrqlaySTVGTPDYIAPEVFMQTgYNKLCDWWSLGVIMYEMLIGYPPFCSET 241
                       250       260       270
                ....*....|....*....|....*....|...
gi 15230288 353 ESGIFRAVLKADPSFDEPPWPSLSFEAKDFVKR 385
Cdd:cd05627 242 PQETYRKVMNWKETLVFPPEVPISEKAKDLILR 274
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
140-406 1.78e-21

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


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 95.51  E-value: 1.78e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 140 LQSRIELGEEIGRGHFgytcSAKFKKGELKDQE-VAVKVIPKSKMTSAISIEDVR----REVKILRALSgHQNLVQFYDA 214
Cdd:cd14041   4 LNDRYLLLHLLGRGGF----SEVYKAFDLTEQRyVAVKIHQLNKNWRDEKKENYHkhacREYRIHKELD-HPRIVKLYDY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 215 FE-DNANVYIVMELCGGGELlDRILARGGKYSEDDAKAVLIQILNVVAFCH--LQGVVHRDLKPENFLYTSKEENSMLKV 291
Cdd:cd14041  79 FSlDTDSFCTVLEYCEGNDL-DFYLKQHKLMSEKEARSIIMQIVNALKYLNeiKPPIIHYDLKPGNILLVNGTACGEIKI 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 292 IDFGLSDFVRPD--------ERLNDIVGSAYYVAPEVL-----HRSYTTEADVWSIGVIAYILLCGSRPF-WARTESGIF 357
Cdd:cd14041 158 TDFGLSKIMDDDsynsvdgmELTSQGAGTYWYLPPECFvvgkePPKISNKVDVWSVGVIFYQCLYGRKPFgHNQSQQDIL 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 15230288 358 R--AVLKADpSFDEPPWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14041 238 QenTILKAT-EVQFPPKPVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYL 287
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
148-403 2.69e-21

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: 94.09  E-value: 2.69e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKFKkgeLKDQEVAVKvipKSKMTSaisiEDVRREVKILRALSgHQNLVQFYDAFEDNAN------- 220
Cdd:cd14047  12 ELIGSGGFGQVFKAKHR---IDGKTYAIK---RVKLNN----EKAEREVKALAKLD-HPNIVRYNGCWDGFDYdpetsss 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 ---------VYIVMELCGGGELLDRILARGGKYSED-DAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLK 290
Cdd:cd14047  81 nssrsktkcLFIQMEFCEKGTLESWIEKRNGEKLDKvLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLV---DTGKVK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 291 VIDFGLSDFVRPDERLNDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILL--CGS----RPFWARTESGIFravlka 363
Cdd:cd14047 158 IGDFGLVTSLKNDGKRTKSKGTLSYMSPEQIsSQDYGKEVDIYALGLILFELLhvCDSafekSKFWTDLRNGIL------ 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15230288 364 DPSFDEppwpslSFEA-KDFVKRLLYKDPRKRMTASQALMH 403
Cdd:cd14047 232 PDIFDK------RYKIeKTIIKKMLSKKPEDRPNASEILRT 266
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
150-406 2.96e-21

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: 94.48  E-value: 2.96e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKkgeLKDQEVAVKVIPKSKMTSAISIEDVRrEVKILRALSgHQNLVQFYDAF----------EDNA 219
Cdd:cd07864  15 IGEGTYGQVYKAKDK---DTGELVALKKVRLDNEKEGFPITAIR-EIKILRQLN-HRSVVNLKEIVtdkqdaldfkKDKG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 220 NVYIVME-----LCGggeLLDRILArggKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsmLKVIDF 294
Cdd:cd07864  90 AFYLVFEymdhdLMG---LLESGLV---HFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQ---IKLADF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 295 GLSDFVRPDER--LNDIVGSAYYVAPEVL--HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEP 370
Cdd:cd07864 161 GLARLYNSEESrpYTNKVITLWYRPPELLlgEERYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRLCGSPCPA 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15230288 371 PWPSL-----------------------SF---EAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd07864 241 VWPDViklpyfntmkpkkqyrrrlreefSFiptPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
140-405 5.38e-21

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: 93.91  E-value: 5.38e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 140 LQSRIELgEEIGRGHFGYTCSAKFKkgeLKDQEVAVKVI----PKSKMTSAIsiedvrREVKILRALSgHQNLVQFYDAF 215
Cdd:cd07873   1 LETYIKL-DKLGEGTYATVYKGRSK---LTDNLVALKEIrlehEEGAPCTAI------REVSLLKDLK-HANIVTLHDII 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 216 EDNANVYIVMELcgggelLDRILAR-----GGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsmLK 290
Cdd:cd07873  70 HTEKSLTLVFEY------LDKDLKQylddcGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGE---LK 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 291 VIDFGLSDFVR-PDERLNDIVGSAYYVAPEVLHRS--YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSF 367
Cdd:cd07873 141 LADFGLARAKSiPTKTYSNEVVTLWYRPPDILLGStdYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIFRILGTP 220
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15230288 368 DEPPWPS--------------------------LSFEAKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd07873 221 TEETWPGilsneefksynypkyradalhnhaprLDSDGADLLSKLLQFEGRKRISAEEAMKHPY 284
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
149-406 5.63e-21

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 93.49  E-value: 5.63e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 149 EIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIEDVRrEVKILRALSG--HQNLVQFYDA-----FEDNANV 221
Cdd:cd07863   7 EIGVGAYGTVYKARDPH---SGHFVALKSVRVQTNEDGLPLSTVR-EVALLKRLEAfdHPNIVRLMDVcatsrTDRETKV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 YIVMELCGGG--ELLDRILARGgkYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGLSDF 299
Cdd:cd07863  83 TLVFEHVDQDlrTYLDKVPPPG--LPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSG---GQVKLADFGLARI 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 300 VRPDERLNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVI-AYI-----LLCGSRPfwARTESGIFRAVlkADPSFDEPPW 372
Cdd:cd07863 158 YSCQMALTPVVVTLWYRAPEVLLQStYATPVDMWSVGCIfAEMfrrkpLFCGNSE--ADQLGKIFDLI--GLPPEDDWPR 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15230288 373 ---------------------PSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd07863 234 dvtlprgafsprgprpvqsvvPEIEESGAQLLLEMLTFNPHKRISAFRALQHPFF 288
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
143-413 5.81e-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: 94.46  E-value: 5.81e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFGYTCSAKfkkGELKDQEVAVKVIPK--SKMTSAISIedvRREVKILRALSgHQNLVQFYD------- 213
Cdd:cd07859   1 RYKIQEVIGKGSYGVVCSAI---DTHTGEKVAIKKINDvfEHVSDATRI---LREIKLLRLLR-HPDIVEIKHimlppsr 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 214 -AFEDnanVYIVMELCGGGelLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVI 292
Cdd:cd07859  74 rEFKD---IYVVFELMESD--LHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANA---DCKLKIC 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 293 DFGLSDFVRPDER----LNDIVGSAYYVAPEV---LHRSYTTEADVWSIGVIAYILLCGsRPFW---------------- 349
Cdd:cd07859 146 DFGLARVAFNDTPtaifWTDYVATRWYRAPELcgsFFSKYTPAIDIWSIGCIFAEVLTG-KPLFpgknvvhqldlitdll 224
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15230288 350 --------ARTESGIFRAVL----KADPSFDEPPWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWIAGYKKID 413
Cdd:cd07859 225 gtpspetiSRVRNEKARRYLssmrKKQPVPFSQKFPNADPLALRLLERLLAFDPKDRPTAEEALADPYFKGLAKVE 300
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
142-348 8.16e-21

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: 92.41  E-value: 8.16e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 142 SRIELGEEIGRGHFGytcsaKFKKGELKDQEVAVKVI---PKSKMTSaiSIEDVRREVKILrALSGHQNLVQFYDAFEDN 218
Cdd:cd14145   6 SELVLEEIIGIGGFG-----KVYRAIWIGDEVAVKAArhdPDEDISQ--TIENVRQEAKLF-AMLKHPNIIALRGVCLKE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 219 ANVYIVMELCGGGELlDRILArGGKYSEDDAKAVLIQILNVVAFCHLQGVV---HRDLKPENFLYTSKEEN-----SMLK 290
Cdd:cd14145  78 PNLCLVMEFARGGPL-NRVLS-GKRIPPDILVNWAVQIARGMNYLHCEAIVpviHRDLKSSNILILEKVENgdlsnKILK 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15230288 291 VIDFGLSdfvRPDERLNDI--VGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPF 348
Cdd:cd14145 156 ITDFGLA---REWHRTTKMsaAGTYAWMAPEVIRSSmFSKGSDVWSYGVLLWELLTGEVPF 213
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
150-415 9.37e-21

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


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 92.59  E-value: 9.37e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKK-GELkdqeVAVKVIPKSKMTSAISIEDVRREVKILRALSGhQNLVQFYDAFEDNANVYIVMELC 228
Cdd:cd05577   1 LGRGGFGEVCACQVKAtGKM----YACKKLDKKRIKKKKGETMALNEKIILEKVSS-PFIVSLAYAFETKDKLCLVLTLM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 229 GGGELLDRILARGGK-YSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLSDFVRPDERLN 307
Cdd:cd05577  76 NGGDLKYHIYNVGTRgFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILL---DDHGHVRISDLGLAVEFKGGKKIK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 308 DIVGSAYYVAPEVL--HRSYTTEADVWSIGVIAYILLCGSRPFWARTES----GIFRAVLKADPSFDEppwpSLSFEAKD 381
Cdd:cd05577 153 GRVGTHGYMAPEVLqkEVAYDFSVDWFALGCMLYEMIAGRSPFRQRKEKvdkeELKRRTLEMAVEYPD----SFSPEARS 228
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 15230288 382 FVKRLLYKDPRKRM-----TASQALMHPWiagYKKIDIP 415
Cdd:cd05577 229 LCEGLLQKDPERRLgcrggSADEVKEHPF---FRSLNWQ 264
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
141-405 1.05e-20

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: 93.15  E-value: 1.05e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 141 QSRIELGEEIGRGHFGYTcsakFKKGELKDQE-VAVKVIPKSKMTSAISIEDVRrEVKILRALSgHQNLVQFYDAFEDNA 219
Cdd:cd07866   7 LRDYEILGKLGEGTFGEV----YKARQIKTGRvVALKKILMHNEKDGFPITALR-EIKILKKLK-HPNVVPLIDMAVERP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 220 N--------VYIVM-----ELCGggeLLD--RIlarggKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKe 284
Cdd:cd07866  81 DkskrkrgsVYMVTpymdhDLSG---LLEnpSV-----KLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQ- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 285 enSMLKVIDFGLSdfvRP---------------DERLNDIVGSAYYVAPEVL--HRSYTTEADVWSIG-VIAY------I 340
Cdd:cd07866 152 --GILKIADFGLA---RPydgpppnpkggggggTRKYTNLVVTRWYRPPELLlgERRYTTAVDIWGIGcVFAEmftrrpI 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 341 L--------------LCGSrPfwarTESGI--FRAVLKADPSFDEPPWP--------SLSFEAKDFVKRLLYKDPRKRMT 396
Cdd:cd07866 227 LqgksdidqlhlifkLCGT-P----TEETWpgWRSLPGCEGVHSFTNYPrtleerfgKLGPEGLDLLSKLLSLDPYKRLT 301

                ....*....
gi 15230288 397 ASQALMHPW 405
Cdd:cd07866 302 ASDALEHPY 310
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
194-407 1.53e-20

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: 92.50  E-value: 1.53e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 194 REVKILRALSGhQNLVQFYDAFEDNANVYIVMELCGGGELlDRILARGGKYSEDdakavliqILNVVAFCHLQG------ 267
Cdd:cd06615  48 RELKVLHECNS-PYIVGFYGAFYSDGEISICMEHMDGGSL-DQVLKKAGRIPEN--------ILGKISIAVLRGltylre 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 268 ---VVHRDLKPENFLYTSKEEnsmLKVIDFGLSDFVRpDERLNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLC 343
Cdd:cd06615 118 khkIMHRDVKPSNILVNSRGE---IKLCDFGVSGQLI-DSMANSFVGTRSYMSPERLQGThYTVQSDIWSLGLSLVEMAI 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 344 GSRPFWARTESG---IFRAVLKADPSFD---------------------------EPPwPSL-----SFEAKDFVKRLLY 388
Cdd:cd06615 194 GRYPIPPPDAKEleaMFGRPVSEGEAKEshrpvsghppdsprpmaifelldyivnEPP-PKLpsgafSDEFQDFVDKCLK 272
                       250
                ....*....|....*....
gi 15230288 389 KDPRKRMTASQALMHPWIA 407
Cdd:cd06615 273 KNPKERADLKELTKHPFIK 291
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
145-383 1.53e-20

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: 94.30  E-value: 1.53e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKKGElkdQEVAVKVIPKSKMTSAISIEDVRREVKILrALSGHQNLVQFYDAFEDNANVYIV 224
Cdd:cd05622  76 EVVKVIGRGAFGEVQLVRHKSTR---KVYAMKLLSKFEMIKRSDSAFFWEERDIM-AFANSPWVVQLFYAFQDDRYLYMV 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGELLDriLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLSDFVRPDE 304
Cdd:cd05622 152 MEYMPGGDLVN--LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL---DKSGHLKLADFGTCMKMNKEG 226
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 305 --RLNDIVGSAYYVAPEVLHRS-----YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSF 377
Cdd:cd05622 227 mvRCDTAVGTPDYISPEVLKSQggdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISK 306

                ....*.
gi 15230288 378 EAKDFV 383
Cdd:cd05622 307 EAKNLI 312
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
150-386 1.62e-20

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: 93.57  E-value: 1.62e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGytcSAKFKKGELKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSGHQNLVQFYdAFEDNANVYIVMELCG 229
Cdd:cd05628   9 IGRGAFG---EVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRAERDILVEADSLWVVKMFY-SFQDKLNLYLIMEFLP 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDrILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGL------------- 296
Cdd:cd05628  85 GGDMMT-LLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSK---GHVKLSDFGLctglkkahrtefy 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 297 --------SDFV--------------RPDERLN-DIVGSAYYVAPEV-LHRSYTTEADVWSIGVIAYILLCGSRPFWART 352
Cdd:cd05628 161 rnlnhslpSDFTfqnmnskrkaetwkRNRRQLAfSTVGTPDYIAPEVfMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSET 240
                       250       260       270
                ....*....|....*....|....*....|....
gi 15230288 353 ESGIFRAVLKADPSFDEPPWPSLSFEAKDFVKRL 386
Cdd:cd05628 241 PQETYKKVMNWKETLIFPPEVPISEKAKDLILRF 274
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
163-405 1.63e-20

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


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 92.06  E-value: 1.63e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 163 FK-KGELKDQEVAVKVI----PKSKMTSAIsiedvrREVKILRALSgHQNLVQFYDAFEDNANVYIVMELcgggelLDRI 237
Cdd:cd07844  17 YKgRSKLTGQLVALKEIrlehEEGAPFTAI------REASLLKDLK-HANIVTLHDIIHTKKTLTLVFEY------LDTD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 238 LAR-----GGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsmLKVIDFGLSdfvR----PDERLND 308
Cdd:cd07844  84 LKQymddcGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGE---LKLADFGLA---RaksvPSKTYSN 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 309 IVGSAYYVAPEVLHRS--YTTEADVWSIGVIAYILLCGSRPFWARTESG-----IFRAV----------LKADPSF---- 367
Cdd:cd07844 158 EVVTLWYRPPDVLLGSteYSTSLDMWGVGCIFYEMATGRPLFPGSTDVEdqlhkIFRVLgtpteetwpgVSSNPEFkpys 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 15230288 368 --DEPP------WPSLSF--EAKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd07844 238 fpFYPPrplinhAPRLDRipHGEELALKFLQYEPKKRISAAEAMKHPY 285
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
137-412 1.73e-20

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 94.94  E-value: 1.73e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  137 SKELQSRIELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAiSIEDVRREVKIL------RALSGHQNLVQ 210
Cdd:PTZ00283  27 AKEQAKKYWISRVLGSGATGTVLCAKRVS---DGEPFAVKVVDMEGMSEA-DKNRAQAEVCCLlncdffSIVKCHEDFAK 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  211 FYDAFEDN-ANVYIVMELCGGGELLDRILAR---GGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeN 286
Cdd:PTZ00283 103 KDPRNPENvLMIALVLDYANAGDLRQEIKSRaktNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCS---N 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  287 SMLKVIDFGLSDFVR---PDERLNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLK 362
Cdd:PTZ00283 180 GLVKLGDFGFSKMYAatvSDDVGRTFCGTPYYVAPEIWRRKpYSKKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLA 259
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15230288  363 AdpSFDEPPwPSLSFEAKDFVKRLLYKDPRKRMTASQALMHP----WIAGYKKI 412
Cdd:PTZ00283 260 G--RYDPLP-PSISPEMQEIVTALLSSDPKRRPSSSKLLNMPicklFISGLLEI 310
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
149-406 1.90e-20

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: 92.42  E-value: 1.90e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 149 EIGRGHFGytcSAKFKKGELKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELC 228
Cdd:cd06635  32 EIGHGSFG---AVYFARDVRTSEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQRIK-HPNSIEYKGCYLREHTAWLVMEYC 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 229 GGGELlDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFVRPderLND 308
Cdd:cd06635 108 LGSAS-DLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLT---EPGQVKLADFGSASIASP---ANS 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 309 IVGSAYYVAPEVL----HRSYTTEADVWSIGvIAYILLCGSRP--FWARTESGIFRAVLKADPSFDEPPWpslSFEAKDF 382
Cdd:cd06635 181 FVGTPYWMAPEVIlamdEGQYDGKVDVWSLG-ITCIELAERKPplFNMNAMSALYHIAQNESPTLQSNEW---SDYFRNF 256
                       250       260
                ....*....|....*....|....
gi 15230288 383 VKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd06635 257 VDSCLQKIPQDRPTSEELLKHMFV 280
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
194-406 2.83e-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: 92.04  E-value: 2.83e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 194 REVKILRALSGhQNLVQFYDAFEDNANVYIVMELCGGGELlDRILARGGKYSEDDAKAVLIQILNVVAFCHLQ-GVVHRD 272
Cdd:cd06650  52 RELQVLHECNS-PYIVGFYGAFYSDGEISICMEHMDGGSL-DQVLKKAGRIPEQILGKVSIAVIKGLTYLREKhKIMHRD 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 273 LKPENFLYTSKEEnsmLKVIDFGLSDFVrPDERLNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFW-- 349
Cdd:cd06650 130 VKPSNILVNSRGE---IKLCDFGVSGQL-IDSMANSFVGTRSYMSPERLQGThYSVQSDIWSMGLSLVEMAVGRYPIPpp 205
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 350 -ARTESGIFRAVLKADPS---------------------------------FDEPP--WPSLSF--EAKDFVKRLLYKDP 391
Cdd:cd06650 206 dAKELELMFGCQVEGDAAetpprprtpgrplssygmdsrppmaifelldyiVNEPPpkLPSGVFslEFQDFVNKCLIKNP 285
                       250
                ....*....|....*
gi 15230288 392 RKRMTASQALMHPWI 406
Cdd:cd06650 286 AERADLKQLMVHAFI 300
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
150-404 3.34e-20

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: 91.21  E-value: 3.34e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISiEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd07848   9 VGEGAYGVVLKCRHKE---TKEIVAIKKFKDSEENEEVK-ETTLRELKMLRTLK-QENIVELKEAFRRRGKLYLVFEYVE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GG--ELLDRiLARGGkySEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSDFVRP--DER 305
Cdd:cd07848  84 KNmlELLEE-MPNGV--PPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISH---NDVLKLCDFGFARNLSEgsNAN 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 306 LNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLK--------------ADPSFDEP 370
Cdd:cd07848 158 YTEYVATRWYRSPELLLGApYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKvlgplpaeqmklfySNPRFHGL 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 15230288 371 PWPSLSFEAK--------------DFVKRLLYKDPRKRMTASQALMHP 404
Cdd:cd07848 238 RFPAVNHPQSlerrylgilsgvllDLMKNLLKLNPTDRYLTEQCLNHP 285
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
149-419 3.92e-20

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: 91.24  E-value: 3.92e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 149 EIGRGHFGytcSAKFKKGELKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELC 228
Cdd:cd06634  22 EIGHGSFG---AVYFARDVRNNEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQKLR-HPNTIEYRGCYLREHTAWLVMEYC 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 229 GGGELlDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFVRPderLND 308
Cdd:cd06634  98 LGSAS-DLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLT---EPGLVKLGDFGSASIMAP---ANS 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 309 IVGSAYYVAPEVL----HRSYTTEADVWSIGvIAYILLCGSRP--FWARTESGIFRAVLKADPSFDEPPWpSLSFeaKDF 382
Cdd:cd06634 171 FVGTPYWMAPEVIlamdEGQYDGKVDVWSLG-ITCIELAERKPplFNMNAMSALYHIAQNESPALQSGHW-SEYF--RNF 246
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 15230288 383 VKRLLYKDPRKRMTASQALMHPWIAGYKKIDIPFDIL 419
Cdd:cd06634 247 VDSCLQKIPQDRPTSDVLLKHRFLLRERPPTVIMDLI 283
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
171-401 4.26e-20

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


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 94.91  E-value: 4.26e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288    171 QEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFE-DNANVYIVMELCGGGELLDRiLARGGKYSEDDA 249
Cdd:TIGR03903    4 HEVAIKLLRTDAPEEEHQRARFRRETALCARLY-HPNIVALLDSGEaPPGLLFAVFEYVPGRTLREV-LAADGALPAGET 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288    250 KAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFG----LSDFVRPDE----RLNDIVGSAYYVAPEVL 321
Cdd:TIGR03903   82 GRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRPHAKVLDFGigtlLPGVRDADVatltRTTEVLGTPTYCAPEQL 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288    322 H-RSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPsFDEPPWPSlSFEAKDFVKRLLYKDPRKRMTASQA 400
Cdd:TIGR03903  162 RgEPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQLSPVD-VSLPPWIA-GHPLGQVLRKALNKDPRQRAASAPA 239

                   .
gi 15230288    401 L 401
Cdd:TIGR03903  240 L 240
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
151-406 7.05e-20

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


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 91.16  E-value: 7.05e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 151 GRGHFGYTcsakFKKGELKDQE-VAVKVIpKSK---MTSAisiedvRREVKILRAL------SGHQNLVQFYDAFEDNAN 220
Cdd:cd14212   8 GQGTFGQV----VKCQDLKTNKlVAVKVL-KNKpayFRQA------MLEIAILTLLntkydpEDKHHIVRLLDHFMHHGH 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 VYIVMELCGGG--ELLDRILARGgkYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkEENSMLKVIDFGLSD 298
Cdd:cd14212  77 LCIVFELLGVNlyELLKQNQFRG--LSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVN-LDSPEIKLIDFGSAC 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 299 FvrPDERLNDIVGSAYYVAPEV-LHRSYTTEADVWSIGVIA---------------YILLC------GSRPFW------- 349
Cdd:cd14212 154 F--ENYTLYTYIQSRFYRSPEVlLGLPYSTAIDMWSLGCIAaelflglplfpgnseYNQLSriiemlGMPPDWmlekgkn 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 350 -----ARTESGIFRAVLKADPSFD---------EP-----------------PWPSLSFEAK-----------DFVKRLL 387
Cdd:cd14212 232 tnkffKKVAKSGGRSTYRLKTPEEfeaenncklEPgkryfkyktlediimnyPMKKSKKEQIdkemetrlafiDFLKGLL 311
                       330
                ....*....|....*....
gi 15230288 388 YKDPRKRMTASQALMHPWI 406
Cdd:cd14212 312 EYDPKKRWTPDQALNHPFI 330
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
143-406 7.12e-20

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


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 91.30  E-value: 7.12e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIedvrREVKILRAL-----SGHQNLVQFYDAFED 217
Cdd:cd14225  44 RYEILEVIGKGSFGQVVKALDHK---TNEHVAIKIIRNKKRFHHQAL----VEVKILDALrrkdrDNSHNVIHMKEYFYF 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 218 NANVYIVMELCGGG--ELLDRILARGgkYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSmLKVIDFG 295
Cdd:cd14225 117 RNHLCITFELLGMNlyELIKKNNFQG--FSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQSS-IKVIDFG 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 296 LSDFVrpDERLNDIVGSAYYVAPEV-LHRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKAdpsFDEPP--- 371
Cdd:cd14225 194 SSCYE--HQRVYTYIQSRFYRSPEViLGLPYSMAIDMWSLGCILAELYTGYPLFPGENEVEQLACIMEV---LGLPPpel 268
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15230288 372 ----------------------------WPS---LSFEAK-------DFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14225 269 ienaqrrrlffdskgnprcitnskgkkrRPNskdLASALKtsdplflDFIRRCLEWDPSKRMTPDEALQHEWI 341
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
139-405 8.63e-20

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: 90.07  E-value: 8.63e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 139 ELQSRIELGEeIGRGhfgyTCSAKFK-KGELKDQEVAVKVI----PKSKMTSAIsiedvrREVKILRALSgHQNLVQFYD 213
Cdd:cd07871   3 KLETYVKLDK-LGEG----TYATVFKgRSKLTENLVALKEIrlehEEGAPCTAI------REVSLLKNLK-HANIVTLHD 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 214 AFEDNANVYIVMELcgggelLDRILAR-----GGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsm 288
Cdd:cd07871  71 IIHTERCLTLVFEY------LDSDLKQyldncGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGE--- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 289 LKVIDFGLSDFVR-PDERLNDIVGSAYYVAPEVLHRS--YTTEADVWSIGVIAYILLCGsRPFWARTESG-----IFRav 360
Cdd:cd07871 142 LKLADFGLARAKSvPTKTYSNEVVTLWYRPPDVLLGSteYSTPIDMWGVGCILYEMATG-RPMFPGSTVKeelhlIFR-- 218
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15230288 361 LKADPSFDEPPW------------------------PSLSFEAKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd07871 219 LLGTPTEETWPGvtsneefrsylfpqyraqplinhaPRLDTDGIDLLSSLLLYETKSRISAEAALRHSY 287
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
150-406 8.75e-20

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: 90.42  E-value: 8.75e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSGhQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd05632  10 LGKGGFGEVCACQVRA---TGKMYACKRLEKKRIKKRKGESMALNEKQILEKVNS-QFVVNLAYAYETKDALCLVLTIMN 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRILARGGK-YSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLSDFVRPDERLND 308
Cdd:cd05632  86 GGDLKFHIYNMGNPgFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILL---DDYGHIRISDLGLAVKIPEGESIRG 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 309 IVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTE----SGIFRAVLKADPSFDEppwpSLSFEAKDFV 383
Cdd:cd05632 163 RVGTVGYMAPEVLnNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEkvkrEEVDRRVLETEEVYSA----KFSEEAKSIC 238
                       250       260
                ....*....|....*....|....*...
gi 15230288 384 KRLLYKDPRKRM-----TASQALMHPWI 406
Cdd:cd05632 239 KMLLTKDPKQRLgcqeeGAGEVKRHPFF 266
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
150-406 1.00e-19

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: 91.24  E-value: 1.00e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKfkkGELKDQEVAVKVI--PKSKMTSAisiEDVRREVKILRALSgHQNLVQFYDAF------EDNANV 221
Cdd:cd07876  29 IGSGAQGIVCAAF---DTVLGINVAVKKLsrPFQNQTHA---KRAYRELVLLKCVN-HKNIISLLNVFtpqkslEEFQDV 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 YIVMELcgggelLDRILARGGKYSEDDAKA--VLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSDF 299
Cdd:cd07876 102 YLVMEL------MDANLCQVIHMELDHERMsyLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKS---DCTLKILDFGLART 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 300 VRPDERLNDIVGSAYYVAPEV-LHRSYTTEADVWSIGVIAYILLCGSRPF--------WAR------TESGIFRAVLKA- 363
Cdd:cd07876 173 ACTNFMMTPYVVTRYYRAPEViLGMGYKENVDIWSVGCIMGELVKGSVIFqgtdhidqWNKvieqlgTPSAEFMNRLQPt 252
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15230288 364 --DPSFDEPPWPSLSFE---------------------AKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd07876 253 vrNYVENRPQYPGISFEelfpdwifpseserdklktsqARDLLSKMLVIDPDKRISVDEALRHPYI 318
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
150-348 1.40e-19

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: 88.89  E-value: 1.40e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGytcsaKFKKGELKDQEVAVKVI---PKSKMtsAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVME 226
Cdd:cd14148   2 IGVGGFG-----KVYKGLWRGEEVAVKAArqdPDEDI--AVTAENVRQEARLFWMLQ-HPNIIALRGVCLNPPHLCLVME 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 227 LCGGGELlDRILArGGKYSEDDAKAVLIQILNVVAFCHLQGVV---HRDLKPENFLYTSKEEN-----SMLKVIDFGLSD 298
Cdd:cd14148  74 YARGGAL-NRALA-GKKVPPHVLVNWAVQIARGMNYLHNEAIVpiiHRDLKSSNILILEPIENddlsgKTLKITDFGLAR 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15230288 299 FVRPDERLNdIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPF 348
Cdd:cd14148 152 EWHKTTKMS-AAGTYAWMAPEVIRLSlFSKSSDVWSFGVLLWELLTGEVPY 201
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
150-348 1.43e-19

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: 89.36  E-value: 1.43e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFG--YTCSAKF---KKGElkdqEVAVKVIpkSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNA--NVY 222
Cdd:cd05038  12 LGEGHFGsvELCRYDPlgdNTGE----QVAVKSL--QPSGEEQHMSDFKREIEILRTLD-HEYIVKYKGVCESPGrrSLR 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 223 IVMELCGGGELldRILARGGKYSEDDAKAVL--IQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLSDFV 300
Cdd:cd05038  85 LIMEYLPSGSL--RDYLQRHRDQIDLKRLLLfaSQICKGMEYLGSQRYIHRDLAARNILV---ESEDLVKISDFGLAKVL 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15230288 301 RPDE---RLNDIVGS-AYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPF 348
Cdd:cd05038 160 PEDKeyyYVKEPGESpIFWYAPECLRESrFSSASDVWSFGVTLYELFTYGDPS 212
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
135-421 1.85e-19

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: 89.28  E-value: 1.85e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 135 GFSKeLQSRIELgEEIGRGhfgyTCSAKFK-KGELKDQEVAVKVIPKSKMTSAISIedVRREVKILRALSgHQNLVQFYD 213
Cdd:cd07872   1 GFGK-METYIKL-EKLGEG----TYATVFKgRSKLTENLVALKEIRLEHEEGAPCT--AIREVSLLKDLK-HANIVTLHD 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 214 AFEDNANVYIVMELcgggelLDRILAR-----GGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsm 288
Cdd:cd07872  72 IVHTDKSLTLVFEY------LDKDLKQymddcGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGE--- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 289 LKVIDFGLSDFVR-PDERLNDIVGSAYYVAPEVLHRS--YTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADP 365
Cdd:cd07872 143 LKLADFGLARAKSvPTKTYSNEVVTLWYRPPDVLLGSseYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFRLLG 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 366 SFDEPPWPSLS----FEAKDFVK----------------------RLLYKDPRKRMTASQALMHPWIA--GYKKIDIPFD 417
Cdd:cd07872 223 TPTEETWPGISsndeFKNYNFPKykpqplinhaprldtegielltKFLQYESKKRISAEEAMKHAYFRslGTRIHSLPES 302

                ....
gi 15230288 418 ILIF 421
Cdd:cd07872 303 ISIF 306
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
135-394 3.14e-19

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: 88.55  E-value: 3.14e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 135 GFSKELQSRIElgEEIGRGHFGYTCSAKFKkgeLKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDA 214
Cdd:cd08229  19 GYNTLANFRIE--KKIGRGQFSEVYRATCL---LDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLN-HPNVIKYYAS 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 215 FEDNANVYIVMELCGGGELlDRILARGGKYS----EDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLK 290
Cdd:cd08229  93 FIEDNELNIVLELADAGDL-SRMIKHFKKQKrlipEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITA---TGVVK 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 291 VIDFGLSDFVRPDER-LNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPFWARTESgiFRAVLKADPSFD 368
Cdd:cd08229 169 LGDLGLGRFFSSKTTaAHSLVGTPYYMSPERIHENgYNFKSDIWSLGCLLYEMAALQSPFYGDKMN--LYSLCKKIEQCD 246
                       250       260
                ....*....|....*....|....*...
gi 15230288 369 EPPWPS--LSFEAKDFVKRLLYKDPRKR 394
Cdd:cd08229 247 YPPLPSdhYSEELRQLVNMCINPDPEKR 274
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
150-348 3.54e-19

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: 87.79  E-value: 3.54e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGytcsaKFKKGELKDQEVAVKVI---PKSKMTSAisIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVME 226
Cdd:cd14146   2 IGVGGFG-----KVYRATWKGQEVAVKAArqdPDEDIKAT--AESVRQEAKLFSMLR-HPNIIKLEGVCLEEPNLCLVME 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 227 LCGGGELLDRILARGGKYSEDDAKAV--------LIQILNVVAFCHLQGVV---HRDLKPENFLYTSKEE-----NSMLK 290
Cdd:cd14146  74 FARGGTLNRALAAANAAPGPRRARRIpphilvnwAVQIARGMLYLHEEAVVpilHRDLKSSNILLLEKIEhddicNKTLK 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15230288 291 VIDFGLSDFVRPDERLNdIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPF 348
Cdd:cd14146 154 ITDFGLAREWHRTTKMS-AAGTYAWMAPEVIKSSlFSKGSDIWSYGVLLWELLTGEVPY 211
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
214-426 4.70e-19

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: 87.80  E-value: 4.70e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 214 AFEDNANVYIVMELCGGGELLDRILARGGK-YSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVI 292
Cdd:cd05605  68 AYETKDALCLVLTIMNGGDLKFHIYNMGNPgFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILL---DDHGHVRIS 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 293 DFGLSDFVRPDERLNDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTE----SGIFRAVLKADPSF 367
Cdd:cd05605 145 DLGLAVEIPEGETIRGRVGTVGYMAPEVVkNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEkvkrEEVDRRVKEDQEEY 224
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15230288 368 DEppwpSLSFEAKDFVKRLLYKDPRKRM-----TASQALMHPWiagYKKIDipfdiliFKQIKA 426
Cdd:cd05605 225 SE----KFSEEAKSICSQLLQKDPKTRLgcrgeGAEDVKSHPF---FKSIN-------FKRLEA 274
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
148-405 5.35e-19

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: 87.58  E-value: 5.35e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAK---------FKKGELKDQEVAVkviPKSKMtsaisiedvrREVKILRALSGHQNLVQFYDA--FE 216
Cdd:cd07837   7 EKIGEGTYGKVYKARdkntgklvaLKKTRLEMEEEGV---PSTAL----------REVSLLQMLSQSIYIVRLLDVehVE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 217 DN--ANVYIVMELCGGGelLDRILARGGKYSEDDAKAVLI-----QILNVVAFCHLQGVVHRDLKPENFLYtsKEENSML 289
Cdd:cd07837  74 ENgkPLLYLVFEYLDTD--LKKFIDSYGRGPHNPLPAKTIqsfmyQLCKGVAHCHSHGVMHRDLKPQNLLV--DKQKGLL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 290 KVIDFGLSD-FVRPDERLNDIVGSAYYVAPEVLHRS--YTTEADVWSIGVIAYILLCGSRPFWARTESG----IFR---- 358
Cdd:cd07837 150 KIADLGLGRaFTIPIKSYTHEIVTLWYRAPEVLLGSthYSTPVDMWSVGCIFAEMSRKQPLFPGDSELQqllhIFRllgt 229
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15230288 359 -------AVLKADPSFDEPPW---------PSLSFEAKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd07837 230 pneevwpGVSKLRDWHEYPQWkpqdlsravPDLEPEGVDLLTKMLAYDPAKRISAKAALQHPY 292
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
150-348 6.92e-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: 87.93  E-value: 6.92e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKgelKDQEVAVKVI-PKSKMTSAisieDVR-REVKILRALSgHQNLVQFYDAFED--NANVYIVM 225
Cdd:cd13988   1 LGQGATANVFRGRHKK---TGDLYAVKVFnNLSFMRPL----DVQmREFEVLKKLN-HKNIVKLFAIEEEltTRHKVLVM 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 226 ELCGGGELLDRILARGGKY--SEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEE-NSMLKVIDFGLSDFVRP 302
Cdd:cd13988  73 ELCPCGSLYTVLEEPSNAYglPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMRVIGEDgQSVYKLTDFGAARELED 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15230288 303 DERLNDIVGSAYYVAPEVLHR---------SYTTEADVWSIGVIAYILLCGSRPF 348
Cdd:cd13988 153 DEQFVSLYGTEEYLHPDMYERavlrkdhqkKYGATVDLWSIGVTFYHAATGSLPF 207
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
150-395 7.24e-19

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: 87.86  E-value: 7.24e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd05588   3 IGRGSYAKVLMVELKK---TKRIYAMKVIKKELVNDDEDIDWVQTEKHVFETASNHPFLVGLHSCFQTESRLFFVIEFVN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRiLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGL-SDFVRPDERLND 308
Cdd:cd05588  80 GGDLMFH-MQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSE---GHIKLTDYGMcKEGLRPGDTTST 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 309 IVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPF---------WARTESGIFRAVLKADPSFDEppwpSLSFE 378
Cdd:cd05588 156 FCGTPNYIAPEILRgEDYGFSVDWWALGVLMFEMLAGRSPFdivgssdnpDQNTEDYLFQVILEKPIRIPR----SLSVK 231
                       250
                ....*....|....*..
gi 15230288 379 AKDFVKRLLYKDPRKRM 395
Cdd:cd05588 232 AASVLKGFLNKNPAERL 248
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
150-426 7.56e-19

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: 87.00  E-value: 7.56e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFK-KGELkdqeVAVKVIPKSKMTSAISIEDVRREVKILRALSGhQNLVQFYDAFEDNANVYIVMELC 228
Cdd:cd05630   8 LGKGGFGEVCACQVRaTGKM----YACKKLEKKRIKKRKGEAMALNEKQILEKVNS-RFVVSLAYAYETKDALCLVLTLM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 229 GGGELLDRILARG-GKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLSDFVRPDERLN 307
Cdd:cd05630  83 NGGDLKFHIYHMGqAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILL---DDHGHIRISDLGLAVHVPEGQTIK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 308 DIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDFVKRL 386
Cdd:cd05630 160 GRVGTVGYMAPEVVkNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLVKEVPEEYSEKFSPQARSLCSML 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 15230288 387 LYKDPRKRM-----TASQALMHPWiagYKKIDipfdiliFKQIKA 426
Cdd:cd05630 240 LCKDPAERLgcrggGAREVKEHPL---FKKLN-------FKRLGA 274
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
193-416 8.11e-19

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


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 86.91  E-value: 8.11e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 193 RREVKILRALSGHQNLVQFYDAFEdNANVYIVMELCGGGELLDRILARGGKYSEDDAKAV-LIQ-----ILNVVAFCHLQ 266
Cdd:cd14020  51 AKERAALEQLQGHRNIVTLYGVFT-NHYSANVPSRCLLLELLDVSVSELLLRSSNQGCSMwMIQhcardVLEALAFLHHE 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 267 GVVHRDLKPENFLYTSKEEnsMLKVIDFGLSdFVRPDERLNDIVGSAYYvAPEV-LHRSY-----------TTEADVWSI 334
Cdd:cd14020 130 GYVHADLKPRNILWSAEDE--CFKLIDFGLS-FKEGNQDVKYIQTDGYR-APEAeLQNCLaqaglqsetecTSAVDLWSL 205
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 335 GVIAYILLCGSR-------PFWARTESGIFRAVLkADPSFDEPPWPslSFEAKDFVKRLLYKDPRKRMTASQALMHPWIA 407
Cdd:cd14020 206 GIVLLEMFSGMKlkhtvrsQEWKDNSSAIIDHIF-ASNAVVNPAIP--AYHLRDLIKSMLHNDPGKRATAEAALCSPFFS 282

                ....*....
gi 15230288 408 gykkidIPF 416
Cdd:cd14020 283 ------IPF 285
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
140-406 1.00e-18

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: 87.03  E-value: 1.00e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 140 LQSRIELGEEIGRGHFgytcSAKFKKGELKDQE-VAVKVIPKSKMTSAISIEDVR----REVKILRALSgHQNLVQFYDA 214
Cdd:cd14040   4 LNERYLLLHLLGRGGF----SEVYKAFDLYEQRyAAVKIHQLNKSWRDEKKENYHkhacREYRIHKELD-HPRIVKLYDY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 215 FEDNANVY-IVMELCGGGELlDRILARGGKYSEDDAKAVLIQILNVVAFCH--LQGVVHRDLKPENFLYTSKEENSMLKV 291
Cdd:cd14040  79 FSLDTDTFcTVLEYCEGNDL-DFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGTACGEIKI 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 292 IDFGLSDFVRPD-------ERLNDIVGSAYYVAPEVL-----HRSYTTEADVWSIGVIAYILLCGSRPF-WARTESGIFR 358
Cdd:cd14040 158 TDFGLSKIMDDDsygvdgmDLTSQGAGTYWYLPPECFvvgkePPKISNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDILQ 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 15230288 359 --AVLKADpSFDEPPWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd14040 238 enTILKAT-EVQFPVKPVVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYL 286
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
148-348 1.59e-18

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: 85.57  E-value: 1.59e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKFKKGELkdqEVAVKVIpKSKMTsaisiEDVRR----EVKILRALSgHQNLVQFYDAFEDNANVYI 223
Cdd:cd05041   1 EKIGRGNFGDVYRGVLKPDNT---EVAVKTC-RETLP-----PDLKRkflqEARILKQYD-HPNIVKLIGVCVQKQPIMI 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSdfvRPD 303
Cdd:cd05041  71 VMELVPGGSLLTFLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVG---ENNVLKISDFGMS---REE 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15230288 304 ERLNDIVGSAY------YVAPEVLHRS-YTTEADVWSIGVIAY-ILLCGSRPF 348
Cdd:cd05041 145 EDGEYTVSDGLkqipikWTAPEALNYGrYTSESDVWSFGILLWeIFSLGATPY 197
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
141-348 2.00e-18

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: 85.55  E-value: 2.00e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 141 QSRIELGEEIGRGHFGYTCSAKFKKGELKDQEVAVKVIpKSKMTSAISiEDVRREVKILRALSgHQNLVQFYDAFEDNAn 220
Cdd:cd05056   5 REDITLGRCIGEGQFGDVYQGVYMSPENEKIAVAVKTC-KNCTSPSVR-EKFLQEAYIMRQFD-HPHIVKLIGVITENP- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 VYIVMELCGGGELldRILARGGKYSEDDAKAVL--IQILNVVAFCHLQGVVHRDLKPENFLYTSKEensMLKVIDFGLSD 298
Cdd:cd05056  81 VWIVMELAPLGEL--RSYLQVNKYSLDLASLILyaYQLSTALAYLESKRFVHRDIAARNVLVSSPD---CVKLGDFGLSR 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15230288 299 FVRPDERLNDIVGS--AYYVAPEVLH-RSYTTEADVWSIGVIAY-ILLCGSRPF 348
Cdd:cd05056 156 YMEDESYYKASKGKlpIKWMAPESINfRRFTSASDVWMFGVCMWeILMLGVKPF 209
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
148-339 2.09e-18

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: 85.03  E-value: 2.09e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKFKKgelkDQEVAVKVIPKSKMtsaiSIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMEL 227
Cdd:cd05034   1 KKLGAGQFGEVWMGVWNG----TTKVAVKTLKPGTM----SPEAFLQEAQIMKKLR-HDKLVQLYAVCSDEEPIYIVTEL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 228 CGGGELLDRIlarggkySEDDAKAVLI--------QILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDF 299
Cdd:cd05034  72 MSKGSLLDYL-------RTGEGRALRLpqlidmaaQIASGMAYLESRNYIHRDLAARNILVG---ENNVCKVADFGLARL 141
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15230288 300 VRPDERLNDiVGSAY---YVAPE-VLHRSYTTEADVWSIGVIAY 339
Cdd:cd05034 142 IEDDEYTAR-EGAKFpikWTAPEaALYGRFTIKSDVWSFGILLY 184
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
150-403 2.16e-18

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: 85.06  E-value: 2.16e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKGElkdQEVAVKVIPKSKMTSAisieDVRrevkiLRALSGHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd13995  12 IPRGAFGKVYLAQDTKTK---KRMACKLIPVEQFKPS----DVE-----IQACFRHENIAELYGALLWEETVHLFMEAGE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRiLARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsmlKVIDFGLSDFVRPDERL-ND 308
Cdd:cd13995  80 GGSVLEK-LESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKA----VLVDFGLSVQMTEDVYVpKD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 309 IVGSAYYVAPEV-LHRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVL----KADPSFDEPPwPSLSFEAKDFV 383
Cdd:cd13995 155 LRGTEIYMSPEViLCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAYPSYLyiihKQAPPLEDIA-QDCSPAMRELL 233
                       250       260
                ....*....|....*....|
gi 15230288 384 KRLLYKDPRKRMTASQALMH 403
Cdd:cd13995 234 EAALERNPNHRSSAAELLKH 253
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
166-407 2.33e-18

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: 84.47  E-value: 2.33e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 166 GELKDQEVAVKVIPKSKMTsaisiedvrrEVKILRALSgHQNLVQFyDAFEDNANVY-IVMELCGGGELLDrILARGGKY 244
Cdd:cd14059  12 GKFRGEEVAVKKVRDEKET----------DIKHLRKLN-HPNIIKF-KGVCTQAPCYcILMEYCPYGQLYE-VLRAGREI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 245 SEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSDFVRPDERLNDIVGSAYYVAPEVLHRS 324
Cdd:cd14059  79 TPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTY---NDVLKISDFGTSKELSEKSTKMSFAGTVAWMAPEVIRNE 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 325 YTTE-ADVWSIGVIAYILLCGSRPFWARTESGIFRAVlkADPSFDEPPWPSLSFEAKDFVKRLLYKDPRKRMTASQALMH 403
Cdd:cd14059 156 PCSEkVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGV--GSNSLQLPVPSTCPDGFKLLMKQCWNSKPRNRPSFRQILMH 233

                ....
gi 15230288 404 PWIA 407
Cdd:cd14059 234 LDIA 237
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
150-401 2.81e-18

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: 85.25  E-value: 2.81e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKkgeLKDQEVAVKVIPKSKMTsaisIEDVR---REVKILRALSgHQNLVQFYDAFEDN--ANVYIV 224
Cdd:cd14049  14 LGKGGYGKVYKVRNK---LDGQYYAIKKILIKKVT----KRDCMkvlREVKVLAGLQ-HPNIVGYHTAWMEHvqLMLYIQ 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGgELLDRILARGGKYSEDDAKA-------------VLIQILNVVAFCHLQGVVHRDLKPEN-FLYTSKEEnsmLK 290
Cdd:cd14049  86 MQLCEL-SLWDWIVERNKRPCEEEFKSapytpvdvdvttkILQQLLEGVTYIHSMGIVHRDLKPRNiFLHGSDIH---VR 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 291 VIDFGLS--DFVRPD------ERLNDI-----VGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLcgsRPFWARTEsgi 356
Cdd:cd14049 162 IGDFGLAcpDILQDGndsttmSRLNGLthtsgVGTCLYAAPEQLEGShYDFKSDMYSIGVILLELF---QPFGTEME--- 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 15230288 357 fRAVLKAD------PSFDEPPWPSLSfeakDFVKRLLYKDPRKRMTASQAL 401
Cdd:cd14049 236 -RAEVLTQlrngqiPKSLCKRWPVQA----KYIKLLTSTEPSERPSASQLL 281
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
150-404 4.68e-18

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: 84.66  E-value: 4.68e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFK-KGELkdqeVAVKVIPKSKMTSAISIEDVRREVKILRALSGhQNLVQFYDAFEDNANVYIVMELC 228
Cdd:cd05631   8 LGKGGFGEVCACQVRaTGKM----YACKKLEKKRIKKRKGEAMALNEKRILEKVNS-RFVVSLAYAYETKDALCLVLTIM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 229 GGGELLDRILARGGK-YSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLSDFVRPDERLN 307
Cdd:cd05631  83 NGGDLKFHIYNMGNPgFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILL---DDRGHIRISDLGLAVQIPEGETVR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 308 DIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTE----SGIFRAVLKADPSFDEppwpSLSFEAKDF 382
Cdd:cd05631 160 GRVGTVGYMAPEVInNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKErvkrEEVDRRVKEDQEEYSE----KFSEDAKSI 235
                       250       260
                ....*....|....*....|....*..
gi 15230288 383 VKRLLYKDPRKRM-----TASQALMHP 404
Cdd:cd05631 236 CRMLLTKNPKERLgcrgnGAAGVKQHP 262
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
148-415 4.77e-18

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: 84.78  E-value: 4.77e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKFKKGElkdQEVAVKvipksKMTSAISIEDVRR---EVKILRALSGHQNLVQFYDAFEDNANVYIV 224
Cdd:cd06617   7 EELGRGAYGVVDKMRHVPTG---TIMAVK-----RIRATVNSQEQKRllmDLDISMRSVDCPYTVTFYGALFREGDVWIC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGelLDR----ILARGGKYSEDdakaVLIQI-LNVV-AFCHLQ---GVVHRDLKPENFLYtskEENSMLKVIDFG 295
Cdd:cd06617  79 MEVMDTS--LDKfykkVYDKGLTIPED----ILGKIaVSIVkALEYLHsklSVIHRDVKPSNVLI---NRNGQVKLCDFG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 296 LSDFVrpderLNDIV-----GSAYYVAPEVL-----HRSYTTEADVWSIGVIAYILLCGSRPF--WaRTESGIFRAVLKa 363
Cdd:cd06617 150 ISGYL-----VDSVAktidaGCKPYMAPERInpelnQKGYDVKSDVWSLGITMIELATGRFPYdsW-KTPFQQLKQVVE- 222
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15230288 364 DPSfdePPWPSLSF--EAKDFVKRLLYKDPRKRMTASQALMHPWI--AGYKKIDIP 415
Cdd:cd06617 223 EPS---PQLPAEKFspEFQDFVNKCLKKNYKERPNYPELLQHPFFelHLSKNTDVA 275
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
148-405 4.81e-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: 84.63  E-value: 4.81e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGhfgytCSAKFKKG--ELKDQEVAVKVIpKSKMTSAISIEDVRrEVKILRALSgHQNLVQFYDAFEDNANVYIVM 225
Cdd:cd07870   6 EKLGEG-----SYATVYKGisRINGQLVALKVI-SMKTEEGVPFTAIR-EASLLKGLK-HANIVLLHDIIHTKETLTFVF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 226 ELCGGgELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsmLKVIDFGLSDFVR-PDE 304
Cdd:cd07870  78 EYMHT-DLAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGE---LKLADFGLARAKSiPSQ 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 305 RLNDIVGSAYYVAPEVLHRS--YTTEADVWSIGVIaYILLCGSRPFWARTeSGIFRAVLK-----ADPSfdEPPWPSLS- 376
Cdd:cd07870 154 TYSSEVVTLWYRPPDVLLGAtdYSSALDIWGAGCI-FIEMLQGQPAFPGV-SDVFEQLEKiwtvlGVPT--EDTWPGVSk 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15230288 377 ---------------------------FEAKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd07870 230 lpnykpewflpckpqqlrvvwkrlsrpPKAEDLASQMLMMFPKDRISAQDALLHPY 285
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
150-405 5.95e-18

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: 84.25  E-value: 5.95e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFgytcSAKFKKGELKD-QEVAVKvipksKMTSAI-SIEDVR--REVKILRALSGHQNLVQFYDAFEDNAN--VYI 223
Cdd:cd07831   7 IGEGTF----SEVLKAQSRKTgKYYAIK-----CMKKHFkSLEQVNnlREIQALRRLSPHPNILRLIEVLFDRKTgrLAL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGgELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEensmLKVIDFGLSDFVRPD 303
Cdd:cd07831  78 VFELMDM-NLYELIKGRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDDI----LKLADFGSCRGIYSK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ERLNDIVGSAYYVAPEVLHRS--YTTEADVWSIGVIAYILLCGSRPFWARTE----SGIF-------RAVLK-----ADP 365
Cdd:cd07831 153 PPYTEYISTRWYRAPECLLTDgyYGPKMDIWAVGCVFFEILSLFPLFPGTNEldqiAKIHdvlgtpdAEVLKkfrksRHM 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 15230288 366 SFDEPP---------WPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd07831 233 NYNFPSkkgtglrklLPNASAEGLDLLKKLLAYDPDERITAKQALRHPY 281
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
142-360 8.97e-18

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: 83.58  E-value: 8.97e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 142 SRIELGEEIGRGHFGYTCSAKFKKGELKDQEVAVKVIPKSKMTSAISieDVRREVKILRALSgHQNLVQFYDAFEDNANV 221
Cdd:cd05033   4 SYVTIEKVIGGGEFGEVCSGSLKLPGKKEIDVAIKTLKSGYSDKQRL--DFLTEASIMGQFD-HPNVIRLEGVVTKSRPV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 YIVMELCGGGELlDRILarggkySEDDAKAVLIQILNVvafchLQGV------------VHRDLKPENFLYTSkeeNSML 289
Cdd:cd05033  81 MIVTEYMENGSL-DKFL------RENDGKFTVTQLVGM-----LRGIasgmkylsemnyVHRDLAARNILVNS---DLVC 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15230288 290 KVIDFGLSDFVRPDERLNDIVG---SAYYVAPEVL-HRSYTTEADVWSIGVIAY-ILLCGSRPFWARTESGIFRAV 360
Cdd:cd05033 146 KVSDFGLSRRLEDSEATYTTKGgkiPIRWTAPEAIaYRKFTSASDVWSFGIVMWeVMSYGERPYWDMSNQDVIKAV 221
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
148-360 9.28e-18

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: 83.16  E-value: 9.28e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKFKKGELKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNAnVYIVMEL 227
Cdd:cd05040   1 EKLGDGSFGVVRRGEWTTPSGKVIQVAVKCLKSDVLSQPNAMDDFLKEVNAMHSLD-HPNLIRLYGVVLSSP-LMMVTEL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 228 CGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEensMLKVIDFGLSdfvrpdeRLN 307
Cdd:cd05040  79 APLGSLLDRLRKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKD---KVKIGDFGLM-------RAL 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15230288 308 DiVGSAYYV------------APEVL-HRSYTTEADVWSIGVIAY-ILLCGSRPFWARTESGIFRAV 360
Cdd:cd05040 149 P-QNEDHYVmqehrkvpfawcAPESLkTRKFSHASDVWMFGVTLWeMFTYGEEPWLGLNGSQILEKI 214
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
142-364 1.10e-17

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: 82.99  E-value: 1.10e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 142 SRIELGEEIGRGHFGYTcsakfKKGELKDQ-EVAVKVIPKSKMtsaiSIEDVRREVKILRALSgHQNLVQFYDAFEDNAN 220
Cdd:cd05114   4 SELTFMKELGSGLFGVV-----RLGKWRAQyKVAIKAIREGAM----SEEDFIEEAKVMMKLT-HPKLVQLYGVCTQQKP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 VYIVMELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFV 300
Cdd:cd05114  74 IYIVTEFMENGCLLNYLRQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVN---DTGVVKVSDFGMTRYV 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15230288 301 RPDERLNDiVGSAYYV---APEVLHRS-YTTEADVWSIGVIAY-ILLCGSRPFWARTESGIFRAVLKAD 364
Cdd:cd05114 151 LDDQYTSS-SGAKFPVkwsPPEVFNYSkFSSKSDVWSFGVLMWeVFTEGKMPFESKSNYEVVEMVSRGH 218
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
148-348 1.13e-17

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


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 83.01  E-value: 1.13e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTcsakfKKGELKDQ-EVAVKVIPKSKMtsaiSIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVME 226
Cdd:cd05113  10 KELGTGQFGVV-----KYGKWRGQyDVAIKMIKEGSM----SEDEFIEEAKVMMNLS-HEKLVQLYGVCTKQRPIFIITE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 227 LCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSDFVRPDERL 306
Cdd:cd05113  80 YMANGCLLNYLREMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVND---QGVVKVSDFGLSRYVLDDEYT 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15230288 307 NDiVGSAYYV---APEVLHRS-YTTEADVWSIGVIAY-ILLCGSRPF 348
Cdd:cd05113 157 SS-VGSKFPVrwsPPEVLMYSkFSSKSDVWAFGVLMWeVYSLGKMPY 202
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
148-406 1.16e-17

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: 83.04  E-value: 1.16e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHF-----GYtcsakfkkgelkDQ----EVAVKVIPKSKMTSAiSIEDVRREVKILRALSgHQNLVQFYDAFEDN 218
Cdd:cd13983   7 EVLGRGSFktvyrAF------------DTeegiEVAWNEIKLRKLPKA-ERQRFKQEIEILKSLK-HPNIIKFYDSWESK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 219 ANVYIVM--ELCGGGELLDRIlARGGKYSEDDAKAVLIQILNVVAFCHLQG--VVHRDLKPEN-FLYTSKEEnsmLKVID 293
Cdd:cd13983  73 SKKEVIFitELMTSGTLKQYL-KRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNiFINGNTGE---VKIGD 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 294 FGLSDFVRPDERlNDIVGSAYYVAPEVLHRSYTTEADVWSIGVIAYILLCGSRPFWARTESG-IFRAVLKADP--SFDEP 370
Cdd:cd13983 149 LGLATLLRQSFA-KSVIGTPEFMAPEMYEEHYDEKVDIYAFGMCLLEMATGEYPYSECTNAAqIYKKVTSGIKpeSLSKV 227
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15230288 371 PWPslsfEAKDFVKRLLyKDPRKRMTASQALMHPWI 406
Cdd:cd13983 228 KDP----ELKDFIEKCL-KPPDERPSARELLEHPFF 258
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
145-360 1.29e-17

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: 82.87  E-value: 1.29e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKKgelkDQEVAVKVIpksKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIV 224
Cdd:cd05148   9 TLERKLGSGYFGEVWEGLWKN----RVRVAIKIL---KSDDLLKQQDFQKEVQALKRLR-HKHLISLFAVCSVGEPVYII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGELLDRILARGGKySEDDAKAVLI--QILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLSDFVRP 302
Cdd:cd05148  81 TELMEKGSLLAFLRSPEGQ-VLPVASLIDMacQVAEGMAYLEEQNSIHRDLAARNILV---GEDLVCKVADFGLARLIKE 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15230288 303 DERLNDIVGSAY-YVAPEVL-HRSYTTEADVWSIGVIAY-ILLCGSRPFWARTESGIFRAV 360
Cdd:cd05148 157 DVYLSSDKKIPYkWTAPEAAsHGTFSTKSDVWSFGILLYeMFTYGQVPYPGMNNHEVYDQI 217
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
131-399 1.46e-17

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


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 83.69  E-value: 1.46e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 131 DKRFGFSKElqsRIELGEEIGRGHFGYTCSAKfKKGELKDQ---EVAVKVIPKSKMTSaiSIEDVRREVKILRALSGHQN 207
Cdd:cd05055  27 DLKWEFPRN---NLSFGKTLGAGAFGKVVEAT-AYGLSKSDavmKVAVKMLKPTAHSS--EREALMSELKIMSHLGNHEN 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 208 LVQFYDAFEDNANVYIVMELCGGGELLDRILARGGKYSE-DDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeEN 286
Cdd:cd05055 101 IVNLLGACTIGGPILVITEYCCYGDLLNFLRRKRESFLTlEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLT---HG 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 287 SMLKVIDFGLSDFVRPDErlNDIV-GSAY----YVAPE-VLHRSYTTEADVWSIGVIAY-ILLCGSRPFWARTESGIFRA 359
Cdd:cd05055 178 KIVKICDFGLARDIMNDS--NYVVkGNARlpvkWMAPEsIFNCVYTFESDVWSYGILLWeIFSLGSNPYPGMPVDSKFYK 255
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 15230288 360 VLKADPSFDEPPWPSLsfEAKDFVKRLLYKDPRKRMTASQ 399
Cdd:cd05055 256 LIKEGYRMAQPEHAPA--EIYDIMKTCWDADPLKRPTFKQ 293
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
150-406 1.73e-17

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: 84.37  E-value: 1.73e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKfkkGELKDQEVAVKVI--PKSKMTSAisiEDVRREVKILRALSgHQNLVQFYDAF------EDNANV 221
Cdd:cd07874  25 IGSGAQGIVCAAY---DAVLDRNVAIKKLsrPFQNQTHA---KRAYRELVLMKCVN-HKNIISLLNVFtpqkslEEFQDV 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 YIVMELcgggelLDRILARGGKYSEDDAKA--VLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSDF 299
Cdd:cd07874  98 YLVMEL------MDANLCQVIQMELDHERMsyLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKS---DCTLKILDFGLART 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 300 VRPDERLNDIVGSAYYVAPEV-LHRSYTTEADVWSIGVIA------YILLCGSR----------------PFWARTESGI 356
Cdd:cd07874 169 AGTSFMMTPYVVTRYYRAPEViLGMGYKENVDIWSVGCIMgemvrhKILFPGRDyidqwnkvieqlgtpcPEFMKKLQPT 248
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15230288 357 FRAVLKADPSFDEPPWPSL----------------SFEAKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd07874 249 VRNYVENRPKYAGLTFPKLfpdslfpadsehnklkASQARDLLSKMLVIDPAKRISVDEALQHPYI 314
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
150-348 1.93e-17

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: 83.09  E-value: 1.93e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTcsAKFKKGELKDQeVAVKvipksKMTSAISIEDVRR---EVKILRALSgHQNLVQFYDAFEDNANV----- 221
Cdd:cd14038   2 LGTGGFGNV--LRWINQETGEQ-VAIK-----QCRQELSPKNRERwclEIQIMKRLN-HPNVVAARDVPEGLQKLapndl 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 -YIVMELCGGGEL---LDRILARGGkYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLS 297
Cdd:cd14038  73 pLLAMEYCQGGDLrkyLNQFENCCG-LREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRLIHKIIDLGYA 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15230288 298 DFVRPDERLNDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPF 348
Cdd:cd14038 152 KELDQGSLCTSFVGTLQYLAPELLeQQKYTVTVDYWSFGTLAFECITGFRPF 203
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
151-348 2.16e-17

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: 81.93  E-value: 2.16e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 151 GRGHFGYTCSAKFKKgelKDQEVAVKVIPKskmtsaisiedVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELCGG 230
Cdd:cd14060   2 GGGSFGSVYRAIWVS---QDKEVAVKKLLK-----------IEKEAEILSVLS-HRNIIQFYGAILEAPNYGIVTEYASY 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 231 GELLDRI-LARGGKYSEDDAKAVLIQILNVVAFCHLQG---VVHRDLKPENFLYTSkeeNSMLKVIDFGLSDFVRPDERL 306
Cdd:cd14060  67 GSLFDYLnSNESEEMDMDQIMTWATDIAKGMHYLHMEApvkVIHRDLKSRNVVIAA---DGVLKICDFGASRFHSHTTHM 143
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15230288 307 NdIVGSAYYVAPEVLHRSYTTE-ADVWSIGVIAYILLCGSRPF 348
Cdd:cd14060 144 S-LVGTFPWMAPEVIQSLPVSEtCDTYSYGVVLWEMLTREVPF 185
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
243-403 2.32e-17

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: 82.84  E-value: 2.32e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 243 KYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENsmLKVIDFGLSD-FVRPDERLNDIVGSAYYVAPEVL 321
Cdd:cd13974 128 RLSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKRTRK--ITITNFCLGKhLVSEDDLLKDQRGSPAYISPDVL 205
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 322 H-RSYTTEA-DVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADpsFDEPPWPSLSFEAKDFVKRLLYKDPRKRMTASQ 399
Cdd:cd13974 206 SgKPYLGKPsDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAAE--YTIPEDGRVSENTVCLIRKLLVLNPQKRLTASE 283

                ....
gi 15230288 400 ALMH 403
Cdd:cd13974 284 VLDS 287
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
144-396 3.47e-17

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: 82.01  E-value: 3.47e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 144 IELGEEIGRGHFGYTCSAKFKKgelkDQEVAVKVIPKSKMtsaiSIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYI 223
Cdd:cd05072   9 IKLVKKLGAGQFGEVWMGYYNN----STKVAVKTLKPGTM----SVQAFLEEANLMKTLQ-HDKLVRLYAVVTKEEPIYI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDRILA-RGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFVRP 302
Cdd:cd05072  80 ITEYMAKGSLLDFLKSdEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVS---ESLMCKIADFGLARVIED 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 303 DErLNDIVGSAY---YVAPEVLHR-SYTTEADVWSIGVIAY-ILLCGSRPFWARTESGIFRAVLKAdpsFDEPPWPSLSF 377
Cdd:cd05072 157 NE-YTAREGAKFpikWTAPEAINFgSFTIKSDVWSFGILLYeIVTYGKIPYPGMSNSDVMSALQRG---YRMPRMENCPD 232
                       250
                ....*....|....*....
gi 15230288 378 EAKDFVKRLLYKDPRKRMT 396
Cdd:cd05072 233 ELYDIMKTCWKEKAEERPT 251
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
131-370 3.87e-17

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: 82.76  E-value: 3.87e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 131 DKRFGFSKElqsRIELGEEIGRGHFGYTCSAK---FKKGELKDQ-EVAVKVIPKSKMTSAISieDVRREVKILRALSGHQ 206
Cdd:cd05101  16 DPKWEFPRD---KLTLGKPLGEGCFGQVVMAEavgIDKDKPKEAvTVAVKMLKDDATEKDLS--DLVSEMEMMKMIGKHK 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 207 NLVQFYDAFEDNANVYIVMELCGGGELLDRILAR---GGKYSED------------DAKAVLIQILNVVAFCHLQGVVHR 271
Cdd:cd05101  91 NIINLLGACTQDGPLYVIVEYASKGNLREYLRARrppGMEYSYDinrvpeeqmtfkDLVSCTYQLARGMEYLASQKCIHR 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 272 DLKPENFLYTskeENSMLKVIDFGLSdfvrpderlNDIVGSAYY------------VAPEVL-HRSYTTEADVWSIGVIA 338
Cdd:cd05101 171 DLAARNVLVT---ENNVMKIADFGLA---------RDINNIDYYkkttngrlpvkwMAPEALfDRVYTHQSDVWSFGVLM 238
                       250       260       270
                ....*....|....*....|....*....|...
gi 15230288 339 Y-ILLCGSRPFWARTESGIFRaVLKADPSFDEP 370
Cdd:cd05101 239 WeIFTLGGSPYPGIPVEELFK-LLKEGHRMDKP 270
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
150-406 4.45e-17

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 83.17  E-value: 4.45e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKfkkGELKDQEVAVKVI--PKSKMTSAisiEDVRREVKILRALSgHQNLVQFYDAF------EDNANV 221
Cdd:cd07875  32 IGSGAQGIVCAAY---DAILERNVAIKKLsrPFQNQTHA---KRAYRELVLMKCVN-HKNIIGLLNVFtpqkslEEFQDV 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 YIVMELcgggelLDRILARGGKYSEDDAKA--VLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSDF 299
Cdd:cd07875 105 YIVMEL------MDANLCQVIQMELDHERMsyLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKS---DCTLKILDFGLART 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 300 VRPDERLNDIVGSAYYVAPEV-LHRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVL------------KADPS 366
Cdd:cd07875 176 AGTSFMMTPYVVTRYYRAPEViLGMGYKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVIeqlgtpcpefmkKLQPT 255
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15230288 367 F-----DEPPWPSLSFE---------------------AKDFVKRLLYKDPRKRMTASQALMHPWI 406
Cdd:cd07875 256 VrtyveNRPKYAGYSFEklfpdvlfpadsehnklkasqARDLLSKMLVIDASKRISVDEALQHPYI 321
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
141-348 4.63e-17

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


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 81.30  E-value: 4.63e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 141 QSRIELGEEIGRGHFGYTCSAKFKKgelkDQEVAVKVIPKSKMtsaiSIEDVRREVKILRALSgHQNLVQFYDAFEDNAN 220
Cdd:cd05068   7 RKSLKLLRKLGSGQFGEVWEGLWNN----TTPVAVKTLKPGTM----DPEDFLREAQIMKKLR-HPKLIQLYAVCTLEEP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 VYIVMELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFV 300
Cdd:cd05068  78 IYIITELMKHGSLLEYLQGKGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVG---ENNICKVADFGLARVI 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15230288 301 RPDERLNDIVGSAY---YVAPE-VLHRSYTTEADVWSIGVIAY-ILLCGSRPF 348
Cdd:cd05068 155 KVEDEYEAREGAKFpikWTAPEaANYNRFSIKSDVWSFGILLTeIVTYGRIPY 207
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
150-408 8.27e-17

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: 80.94  E-value: 8.27e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFG--YTCSaKFKKGELkdqeVAVKVIPKS--KMTSAISIedVRREVKILRALSGHQN---LVQFYDAFEDNANVY 222
Cdd:cd05606   2 IGRGGFGevYGCR-KADTGKM----YAMKCLDKKriKMKQGETL--ALNERIMLSLVSTGGDcpfIVCMTYAFQTPDKLC 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 223 IVMELCGGGELlDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLS-DFvr 301
Cdd:cd05606  75 FILDLMNGGDL-HYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILL---DEHGHVRISDLGLAcDF-- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 302 PDERLNDIVGSAYYVAPEVLHR--SYTTEADVWSIGVIAYILLCGSRPFW---ARTESGIFRAVLKADPSFDEppwpSLS 376
Cdd:cd05606 149 SKKKPHASVGTHGYMAPEVLQKgvAYDSSADWFSLGCMLYKLLKGHSPFRqhkTKDKHEIDRMTLTMNVELPD----SFS 224
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 15230288 377 FEAKDFVKRLLYKDPRKRM-----TASQALMHPWIAG 408
Cdd:cd05606 225 PELKSLLEGLLQRDVSKRLgclgrGATEVKEHPFFKG 261
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
150-348 1.16e-16

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: 80.73  E-value: 1.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSakfkkgeLKDQEVAVKVIPKSKMTSAISIEDVR--REVKILRALSgHQNLVQFYDAFED-----NANVY 222
Cdd:cd14039   1 LGTGGFGNVCL-------YQNQETGEKIAIKSCRLELSVKNKDRwcHEIQIMKKLN-HPNVVKACDVPEEmnflvNDVPL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 223 IVMELCGGGELlDRILAR-----GGKYSEddAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLS 297
Cdd:cd14039  73 LAMEYCSGGDL-RKLLNKpenccGLKESQ--VLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKIVHKIIDLGYA 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15230288 298 DFVRPDERLNDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPF 348
Cdd:cd14039 150 KDLDQGSLCTSFVGTLQYLAPELFeNKSYTVTVDYWSFGTMVFECIAGFRPF 201
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
147-348 1.38e-16

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: 80.62  E-value: 1.38e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 147 GEEIGRGHFGYTCsakfkKGELKDQEVAVKvipKSKMTSAISIEDVRR----EVKILRALSgHQNLVQFYDAFEDNANVY 222
Cdd:cd14158  20 GNKLGEGGFGVVF-----KGYINDKNVAVK---KLAAMVDISTEDLTKqfeqEIQVMAKCQ-HENLVELLGYSCDGPQLC 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 223 IVMELCGGGELLDRILARggkyseDDAKAVLIQI--------LNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDF 294
Cdd:cd14158  91 LVYTYMPNGSLLDRLACL------NDTPPLSWHMrckiaqgtANGINYLHENNHIHRDIKSANILLD---ETFVPKISDF 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 295 GLSDFVRPD------ERlndIVGSAYYVAPEVLHRSYTTEADVWSIGVIAYILLCGSRPF 348
Cdd:cd14158 162 GLARASEKFsqtimtER---IVGTTAYMAPEALRGEITPKSDIFSFGVVLLEIITGLPPV 218
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
144-349 1.81e-16

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: 79.82  E-value: 1.81e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 144 IELGEEIGRGHFGYTCSAKFKKGELKDQE--VAVKVIpkSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANV 221
Cdd:cd05049   7 IVLKRELGEGAFGKVFLGECYNLEPEQDKmlVAVKTL--KDASSPDARKDFEREAELLTNLQ-HENIVKFYGVCTEGDPL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 YIVMELCGGGELLDRILARG-------------GKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSM 288
Cdd:cd05049  84 LMVFEYMEHGDLNKFLRSHGpdaaflasedsapGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVG---TNLV 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15230288 289 LKVIDFGLSdfvrpderlNDIVGSAYY------------VAPE-VLHRSYTTEADVWSIGVIAY-ILLCGSRPFW 349
Cdd:cd05049 161 VKIGDFGMS---------RDIYSTDYYrvgghtmlpirwMPPEsILYRKFTTESDVWSFGVVLWeIFTYGKQPWF 226
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
170-406 2.28e-16

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 79.52  E-value: 2.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  170 DQEVAVKVIPKSKMTSAIsiedvrrEVKILRALSGHQNLVQFYDAFEDNANVYIVMELCGGGELLDrILARGGKYSEDDA 249
Cdd:PHA03390  40 TQKLFVQKIIKAKNFNAI-------EPMVHQLMKDNPNFIKLYYSVTTLKGHVLIMDYIKDGDLFD-LLKKEGKLSEAEV 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  250 KAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENsmLKVIDFGLSdfvrpderlnDIVG--SAY-----YVAPE-VL 321
Cdd:PHA03390 112 KKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAKDR--IYLCDYGLC----------KIIGtpSCYdgtldYFSPEkIK 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  322 HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDFVKRLLYKDPRKRMTASQAL 401
Cdd:PHA03390 180 GHNYDVSFDWWAVGVLTYELLTGKHPFKEDEDEELDLESLLKRQQKKLPFIKNVSKNANDFVQSMLKYNINYRLTNYNEI 259

                 ....*.
gi 15230288  402 M-HPWI 406
Cdd:PHA03390 260 IkHPFL 265
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
139-348 3.32e-16

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: 79.38  E-value: 3.32e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 139 ELQ-SRIELGEEIGRGHFGYTCSAKFK---KGELKDQEVAVKVIPKSKMTSAISieDVRREVKILRALSGHQNLVQFYDA 214
Cdd:cd05053   8 ELPrDRLTLGKPLGEGAFGQVVKAEAVgldNKPNEVVTVAVKMLKDDATEKDLS--DLVSEMEMMKMIGKHKNIINLLGA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 215 FEDNANVYIVMELCGGGELLDRILAR---GGKYSEDDAKAVLIQILNV--VAFCHL----------QGVVHRDLKPENFL 279
Cdd:cd05053  86 CTQDGPLYVVVEYASKGNLREFLRARrppGEEASPDDPRVPEEQLTQKdlVSFAYQvargmeylasKKCIHRDLAARNVL 165
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15230288 280 YTskeENSMLKVIDFGLS------DFVRP--DERLndivgSAYYVAPEVL-HRSYTTEADVWSIGVIAY-ILLCGSRPF 348
Cdd:cd05053 166 VT---EDNVMKIADFGLArdihhiDYYRKttNGRL-----PVKWMAPEALfDRVYTHQSDVWSFGVLLWeIFTLGGSPY 236
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
147-339 3.38e-16

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: 78.51  E-value: 3.38e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 147 GEEIGRGHFGytcsaKFKKGELKDQ-EVAVKVIpKSKMTSAISIEDVRrEVKILRALSgHQNLVQFYDAFEDNANVYIVM 225
Cdd:cd05085   1 GELLGKGNFG-----EVYKGTLKDKtPVAVKTC-KEDLPQELKIKFLS-EARILKQYD-HPNIVKLIGVCTQRQPIYIVM 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 226 ELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLS----DFVR 301
Cdd:cd05085  73 ELVPGGDFLSFLRKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVG---ENNALKISDFGMSrqedDGVY 149
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15230288 302 PDERLNDIvgSAYYVAPEVL-HRSYTTEADVWSIGVIAY 339
Cdd:cd05085 150 SSSGLKQI--PIKWTAPEALnYGRYSSESDVWSFGILLW 186
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
147-405 4.79e-16

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: 79.34  E-value: 4.79e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 147 GEEIGRGHFGYTCSAKFKKGElKDQEVAVKVIPKSKMTSAISiedvrREVKILRALSgHQNLVQFYDAFEDNANVYIVME 226
Cdd:cd07867   7 GCKVGRGTYGHVYKAKRKDGK-DEKEYALKQIEGTGISMSAC-----REIALLRELK-HPNVIALQKVFLSHSDRKVWLL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 227 LCGGGELLDRILA--RGGKYSEDD-------AKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSK-EENSMLKVIDFGL 296
Cdd:cd07867  80 FDYAEHDLWHIIKfhRASKANKKPmqlprsmVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEgPERGRVKIADMGF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 297 SDF----VRPDERLNDIVGSAYYVAPEVL--HRSYTTEADVWSIGVIAYILLCGSRPFWARTE-------------SGIF 357
Cdd:cd07867 160 ARLfnspLKPLADLDPVVVTFWYRAPELLlgARHYTKAIDIWAIGCIFAELLTSEPIFHCRQEdiktsnpfhhdqlDRIF 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 358 RAV-LKADPSFDE----PPWPSLSfeaKDF----------------------------VKRLLYKDPRKRMTASQALMHP 404
Cdd:cd07867 240 SVMgFPADKDWEDirkmPEYPTLQ---KDFrrttyansslikymekhkvkpdskvfllLQKLLTMDPTKRITSEQALQDP 316

                .
gi 15230288 405 W 405
Cdd:cd07867 317 Y 317
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
149-405 5.87e-16

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: 78.54  E-value: 5.87e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 149 EIGRGHFGYTcsakFKKGELKD--QEVAVKVIPKSKMTSAISIEDVRrEVKILRALSG--HQNLVQFYDA-----FEDNA 219
Cdd:cd07862   8 EIGEGAYGKV----FKARDLKNggRFVALKRVRVQTGEEGMPLSTIR-EVAVLRHLETfeHPNVVRLFDVctvsrTDRET 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 220 NVYIVMELCGGG--ELLDRILARGgkYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLS 297
Cdd:cd07862  83 KLTLVFEHVDQDltTYLDKVPEPG--VPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTS---SGQIKLADFGLA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 298 DFVRPDERLNDIVGSAYYVAPEV-LHRSYTTEADVWSIGVIaYILLCGSRPFWaRTESG------IFRAVLKADPSfDEP 370
Cdd:cd07862 158 RIYSFQMALTSVVVTLWYRAPEVlLQSSYATPVDLWSVGCI-FAEMFRRKPLF-RGSSDvdqlgkILDVIGLPGEE-DWP 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15230288 371 -----------PWPSLSFE---------AKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd07862 235 rdvalprqafhSKSAQPIEkfvtdidelGKDLLLKCLTFNPAKRISAYSALSHPY 289
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
150-348 7.19e-16

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: 78.08  E-value: 7.19e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFG--YtcsakfkKGELKD-QEVAVKVIpkSKMTSAISIEDVRREVKILRALSgHQNLVQ---FYDAFEDNANVYI 223
Cdd:cd14066   1 IGSGGFGtvY-------KGVLENgTVVAVKRL--NEMNCAASKKEFLTELEMLGRLR-HPNLVRllgYCLESDEKLLVYE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMElcgGGELLDRILARGGK--YSEDDAKAVLIQILNVVAFCHLQG---VVHRDLKPENFLYtskEENSMLKVIDFGLSD 298
Cdd:cd14066  71 YMP---NGSLEDRLHCHKGSppLPWPQRLKIAKGIARGLEYLHEECpppIIHGDIKSSNILL---DEDFEPKLTDFGLAR 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15230288 299 FVRPDE---RLNDIVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPF 348
Cdd:cd14066 145 LIPPSEsvsKTSAVKGTIGYLAPEYIRtGRVSTKSDVYSFGVVLLELLTGKPAV 198
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
194-343 7.33e-16

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: 77.53  E-value: 7.33e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 194 REVKILRALSgHQNLVQFYDAFEDNANVYIVMELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDL 273
Cdd:cd14065  37 KEVKLMRRLS-HPNILRFIGVCVKDNKLNFITEYVNGGTLEELLKSMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDL 115
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15230288 274 KPENFLYTSKEENSMLKVIDFGLSDFVrPDERLND--------IVGSAYYVAPEVLH-RSYTTEADVWSIGviayILLC 343
Cdd:cd14065 116 NSKNCLVREANRGRNAVVADFGLAREM-PDEKTKKpdrkkrltVVGSPYWMAPEMLRgESYDEKVDVFSFG----IVLC 189
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
148-404 7.57e-16

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: 78.14  E-value: 7.57e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFG--YTCsakfkkgeLKDQEVAVKVIPKSKMTSAISI--EDVRREVKILRALSGHQNLVQFYDAFEDNANVYI 223
Cdd:cd14138  11 EKIGSGEFGsvFKC--------VKRLDGCIYAIKRSKKPLAGSVdeQNALREVYAHAVLGQHSHVVRYYSAWAEDDHMLI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDRILA--RGGKY-SEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLY-------TSKEE-------- 285
Cdd:cd14138  83 QNEYCNGGSLADAISEnyRIMSYfTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFIsrtsipnAASEEgdedewas 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 286 -NSMLKVIDFG-LSDFVRPDERlndiVGSAYYVAPEVLHRSYT--TEADVWSIGvIAYILLCGSRPF------WARTESG 355
Cdd:cd14138 163 nKVIFKIGDLGhVTRVSSPQVE----EGDSRFLANEVLQENYThlPKADIFALA-LTVVCAAGAEPLptngdqWHEIRQG 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 15230288 356 IFravlkadpsfdePPWPS-LSFEAKDFVKRLLYKDPRKRMTASQALMHP 404
Cdd:cd14138 238 KL------------PRIPQvLSQEFLDLLKVMIHPDPERRPSAVALVKHS 275
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
131-399 1.34e-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: 78.14  E-value: 1.34e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 131 DKRFGFSKelqSRIELGEEIGRGHFGYTCSAKF----KKGELKDQEVAVKVIPKSKMTSAISieDVRREVKILRALSGHQ 206
Cdd:cd05100   4 DPKWELSR---TRLTLGKPLGEGCFGQVVMAEAigidKDKPNKPVTVAVKMLKDDATDKDLS--DLVSEMEMMKMIGKHK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 207 NLVQFYDAFEDNANVYIVMELCGGGELLDRILAR---GGKYSEDDAK------------AVLIQILNVVAFCHLQGVVHR 271
Cdd:cd05100  79 NIINLLGACTQDGPLYVLVEYASKGNLREYLRARrppGMDYSFDTCKlpeeqltfkdlvSCAYQVARGMEYLASQKCIHR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 272 DLKPENFLYTskeENSMLKVIDFGLSDFVRPDERLNDIVGS---AYYVAPEVL-HRSYTTEADVWSIGVIAY-ILLCGSR 346
Cdd:cd05100 159 DLAARNVLVT---EDNVMKIADFGLARDVHNIDYYKKTTNGrlpVKWMAPEALfDRVYTHQSDVWSFGVLLWeIFTLGGS 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 15230288 347 PFWARTESGIFRaVLKADPSFDEPpwPSLSFEAKDFVKRLLYKDPRKRMTASQ 399
Cdd:cd05100 236 PYPGIPVEELFK-LLKEGHRMDKP--ANCTHELYMIMRECWHAVPSQRPTFKQ 285
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
164-399 1.34e-15

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: 77.05  E-value: 1.34e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 164 KKGELKDQEVAVKVIpkskMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELCGGGELLDrILARGGK 243
Cdd:cd13992  19 KVGVYGGRTVAIKHI----TFSRTEKRTILQELNQLKELV-HDNLNKFIGICINPPNIAVVTEYCTRGSLQD-VLLNREI 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 244 YSEDDAKAVLIQ-ILNVVAFCHLQ-GVVHRDLKPENFLYTSkeeNSMLKVIDFGLSDFVRPDE-RLNDIVGSAY---YVA 317
Cdd:cd13992  93 KMDWMFKSSFIKdIVKGMNYLHSSsIGYHGRLKSSNCLVDS---RWVVKLTDFGLRNLLEEQTnHQLDEDAQHKkllWTA 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 318 PEVLhRSYTTE------ADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADpsfDEPPWPSLSFEAKDF-------VK 384
Cdd:cd13992 170 PELL-RGSLLEvrgtqkGDVYSFAIILYEILFRSDPFALEREVAIVEKVISGG---NKPFRPELAVLLDEFpprlvllVK 245
                       250
                ....*....|....*
gi 15230288 385 RLLYKDPRKRMTASQ 399
Cdd:cd13992 246 QCWAENPEKRPSFKQ 260
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
142-373 1.36e-15

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: 77.22  E-value: 1.36e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 142 SRIELGEEIGRGHFGYTCSAKFKKGELKDQEVAVKVIpKSKMTsaisiEDVRREVKILRALSG---HQNLVQFYDAFEDN 218
Cdd:cd05065   4 SCVKIEEVIGAGEFGEVCRGRLKLPGKREIFVAIKTL-KSGYT-----EKQRRDFLSEASIMGqfdHPNIIHLEGVVTKS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 219 ANVYIVMELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSD 298
Cdd:cd05065  78 RPVMIITEFMENGALDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNS---NLVCKVSDFGLSR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 299 FVRpDERLNDIVGSAY-------YVAPE-VLHRSYTTEADVWSIGVIAY-ILLCGSRPFWARTESGIFRAVlkaDPSFDE 369
Cdd:cd05065 155 FLE-DDTSDPTYTSSLggkipirWTAPEaIAYRKFTSASDVWSYGIVMWeVMSYGERPYWDMSNQDVINAI---EQDYRL 230

                ....
gi 15230288 370 PPWP 373
Cdd:cd05065 231 PPPM 234
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
147-405 1.42e-15

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: 78.18  E-value: 1.42e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 147 GEEIGRGHFGYTCSAKFKKGElKDQEVAVKVIPKSKMTSAISiedvrREVKILRALSgHQNLVQFYDAFEDNANVYIVME 226
Cdd:cd07868  22 GCKVGRGTYGHVYKAKRKDGK-DDKDYALKQIEGTGISMSAC-----REIALLRELK-HPNVISLQKVFLSHADRKVWLL 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 227 LCGGGELLDRILA--RGGKYSEDDA-------KAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSK-EENSMLKVIDFGL 296
Cdd:cd07868  95 FDYAEHDLWHIIKfhRASKANKKPVqlprgmvKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEgPERGRVKIADMGF 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 297 SDF----VRPDERLNDIVGSAYYVAPEVL--HRSYTTEADVWSIGVIAYILLCGSRPFWARTE-------------SGIF 357
Cdd:cd07868 175 ARLfnspLKPLADLDPVVVTFWYRAPELLlgARHYTKAIDIWAIGCIFAELLTSEPIFHCRQEdiktsnpyhhdqlDRIF 254
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15230288 358 RAV-LKADPSFDE-PPWPSLSFEAKDF----------------------------VKRLLYKDPRKRMTASQALMHPW 405
Cdd:cd07868 255 NVMgFPADKDWEDiKKMPEHSTLMKDFrrntytncslikymekhkvkpdskafhlLQKLLTMDPIKRITSEQAMQDPY 332
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
142-360 1.45e-15

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: 77.21  E-value: 1.45e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 142 SRIELGEEIGRGHFGYTCSAKFKKGELKDQEVAVKVIpKSKMTSAiSIEDVRREVKILRALSgHQNLVQFYDAFEDNANV 221
Cdd:cd05066   4 SCIKIEKVIGAGEFGEVCSGRLKLPGKREIPVAIKTL-KAGYTEK-QRRDFLSEASIMGQFD-HPNIIHLEGVVTRSKPV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 YIVMELCGGGElLDRILARggkyseDDAKAVLIQILNVV-------AFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDF 294
Cdd:cd05066  81 MIVTEYMENGS-LDAFLRK------HDGQFTVIQLVGMLrgiasgmKYLSDMGYVHRDLAARNILVNS---NLVCKVSDF 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15230288 295 GLSDFVRPDERlndivgSAY----------YVAPEVL-HRSYTTEADVWSIGVIAY-ILLCGSRPFWARTESGIFRAV 360
Cdd:cd05066 151 GLSRVLEDDPE------AAYttrggkipirWTAPEAIaYRKFTSASDVWSYGIVMWeVMSYGERPYWEMSNQDVIKAI 222
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
143-406 1.50e-15

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


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 78.13  E-value: 1.50e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFGYTCSAKfkkgELKDQE-VAVKVIPKSKMTsaisIEDVRREVKILRALSGHQ-----NLVQFYDAFE 216
Cdd:cd14226  14 RYEIDSLIGKGSFGQVVKAY----DHVEQEwVAIKIIKNKKAF----LNQAQIEVRLLELMNKHDtenkyYIVRLKRHFM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 217 DNANVYIVMELCGGG--ELLDRILARGgkYSEDDAKAVLIQILNvvAFCHLQ----GVVHRDLKPENFLYTSKEEnSMLK 290
Cdd:cd14226  86 FRNHLCLVFELLSYNlyDLLRNTNFRG--VSLNLTRKFAQQLCT--ALLFLStpelSIIHCDLKPENILLCNPKR-SAIK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 291 VIDFGLSdfVRPDERLNDIVGSAYYVAPEV-LHRSYTTEADVWSIGVIAYILLCGSRPFWARTESG-IFR--AVL----- 361
Cdd:cd14226 161 IIDFGSS--CQLGQRIYQYIQSRFYRSPEVlLGLPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDqMNKivEVLgmppv 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 362 -------KADPSFD-------------------EPPWPSLS---------------FEA----------KDFVKRLLYKD 390
Cdd:cd14226 239 hmldqapKARKFFEklpdgtyylkktkdgkkykPPGSRKLHeilgvetggpggrraGEPghtvedylkfKDLILRMLDYD 318
                       330
                ....*....|....*.
gi 15230288 391 PRKRMTASQALMHPWI 406
Cdd:cd14226 319 PKTRITPAEALQHSFF 334
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
150-395 1.77e-15

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: 77.25  E-value: 1.77e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSGhQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd05607  10 LGKGGFGEVCAVQVKN---TGQMYACKKLDKKRLKKKSGEKMALLEKEILEKVNS-PFIVSLAYAFETKTHLCLVMSLMN 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRILARGGKYSEddAKAVLI---QILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLSDFVRPDERL 306
Cdd:cd05607  86 GGDLKYHIYNVGERGIE--MERVIFysaQITCGILHLHSLKIVYRDMKPENVLL---DDNGNCRLSDLGLAVEVKEGKPI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 307 NDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILLCGSRPFWARTE----SGIFRAVLKADPSFDEppwPSLSFEAKD 381
Cdd:cd05607 161 TQRAGTNGYMAPEILkEESYSYPVDWFAMGCSIYEMVAGRTPFRDHKEkvskEELKRRTLEDEVKFEH---QNFTEEAKD 237
                       250
                ....*....|....
gi 15230288 382 FVKRLLYKDPRKRM 395
Cdd:cd05607 238 ICRLFLAKKPENRL 251
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
136-342 1.86e-15

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: 76.89  E-value: 1.86e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 136 FSKELQSRIElgeEIGRGHFGYTCSAKFK-KGELKDQEVAVKVI-PKSKMTSaisIEDVRREVKILRALSgHQNLVQFYD 213
Cdd:cd05079   1 FEKRFLKRIR---DLGEGHFGKVELCRYDpEGDNTGEQVAVKSLkPESGGNH---IADLKKEIEILRNLY-HENIVKYKG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 214 AFEDNAN--VYIVMELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKV 291
Cdd:cd05079  74 ICTEDGGngIKLIMEFLPSGSLKEYLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLV---ESEHQVKI 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15230288 292 IDFGLSDFVRPDERL----NDIVGSAYYVAPEVL-HRSYTTEADVWSIGVIAYILL 342
Cdd:cd05079 151 GDFGLTKAIETDKEYytvkDDLDSPVFWYAPECLiQSKFYIASDVWSFGVTLYELL 206
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
143-348 2.50e-15

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: 76.55  E-value: 2.50e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFGYTCSAKFKKgelkdqEVAVKVIpKSKMTSAISIEDVRREVKILRAlSGHQNLVQFYDAFEDNANVY 222
Cdd:cd14152   1 QIELGELIGQGRWGKVHRGRWHG------EVAIRLL-EIDGNNQDHLKLFKKEVMNYRQ-TRHENVVLFMGACMHPPHLA 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 223 IVMELCGGGELLDriLARGGKYSEDDAKAVLI--QILNVVAFCHLQGVVHRDLKPENFLYtskeENSMLKVIDFGL---S 297
Cdd:cd14152  73 IITSFCKGRTLYS--FVRDPKTSLDINKTRQIaqEIIKGMGYLHAKGIVHKDLKSKNVFY----DNGKVVITDFGLfgiS 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15230288 298 DFVRPDERLNDIV---GSAYYVAPEVLHR----------SYTTEADVWSIGVIAYILLCGSRPF 348
Cdd:cd14152 147 GVVQEGRRENELKlphDWLCYLAPEIVREmtpgkdedclPFSKAADVYAFGTIWYELQARDWPL 210
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
150-399 3.01e-15

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 76.01  E-value: 3.01e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKGELKdqeVAVKVIPKSKMTSaisiedvrREVKILRALSGHQnLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd13991  14 IGRGSFGEVHRMEDKQTGFQ---CAVKKVRLEVFRA--------EELMACAGLTSPR-VVPLYGAVREGPWVNIFMDLKE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELlDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLkvIDFGLSDFVRPDE----- 304
Cdd:cd13991  82 GGSL-GQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGSDAFL--CDFGHAECLDPDGlgksl 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 305 -RLNDIVGSAYYVAPEV-LHRSYTTEADVWSIGVIAYILLCGSRPfWARTESG-IFRAVLKADPSFDEPPwPS---LSFE 378
Cdd:cd13991 159 fTGDYIPGTETHMAPEVvLGKPCDAKVDVWSSCCMMLHMLNGCHP-WTQYYSGpLCLKIANEPPPLREIP-PScapLTAQ 236
                       250       260
                ....*....|....*....|.
gi 15230288 379 AkdfVKRLLYKDPRKRMTASQ 399
Cdd:cd13991 237 A---IQAGLRKEPVHRASAAE 254
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
150-406 3.21e-15

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


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 76.88  E-value: 3.21e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKGElkDQEVAVKVIPKSKMTSAISiedvRREVKILRALSGHQ-----NLVQFYDAFEDNANVYIV 224
Cdd:cd14135   8 LGKGVFSNVVRARDLARG--NQEVAIKIIRNNELMHKAG----LKELEILKKLNDADpddkkHCIRLLRHFEHKNHLCLV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGelLDRILARGGKYSEDDAKAVLI---QILnvVAFCHLQ--GVVHRDLKPENFLYTskEENSMLKVIDFGLSDF 299
Cdd:cd14135  82 FESLSMN--LREVLKKYGKNVGLNIKAVRSyaqQLF--LALKHLKkcNILHADIKPDNILVN--EKKNTLKLCDFGSASD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 300 VRPDERLNDIVgSAYYVAPEV-LHRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRA-----------VLKA---- 363
Cdd:cd14135 156 IGENEITPYLV-SRFYRAPEIiLGLPYDYPIDMWSVGCTLYELYTGKILFPGKTNNHMLKLmmdlkgkfpkkMLRKgqfk 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 364 DPSFDE-------------------------PPWPSLSF----------------EAKDFVKRLLYKDPRKRMTASQALM 402
Cdd:cd14135 235 DQHFDEnlnfiyrevdkvtkkevrrvmsdikPTKDLKTLligkqrlpdedrkkllQLKDLLDKCLMLDPEKRITPNEALQ 314

                ....
gi 15230288 403 HPWI 406
Cdd:cd14135 315 HPFI 318
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
150-396 3.31e-15

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: 75.95  E-value: 3.31e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKGELkdqEVAVKVIPKSKmTSAISIEDVRREVKILRALsGHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd13978   1 LGSGGFGTVSKARHVSWFG---MVAIKCLHSSP-NCIEERKALLKEAEKMERA-RHSYVLPLLGVCVERRSLGLVMEYME 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELlDRILARggkYSEDDAKAVLIQILNVVA----FCH--LQGVVHRDLKPENFLYtskEENSMLKVIDFGLSDFVRPD 303
Cdd:cd13978  76 NGSL-KSLLER---EIQDVPWSLRFRIIHEIAlgmnFLHnmDPPLLHHDLKPENILL---DNHFHVKISDFGLSKLGMKS 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ERLNDIVGSA------YYVAPEVL---HRSYTTEADVWSIGVIAYILLCGSRPFWARTESG-IFRAVLKAD-PSFDE--- 369
Cdd:cd13978 149 ISANRRRGTEnlggtpIYMAPEAFddfNKKPTSKSDVYSFAIVIWAVLTRKEPFENAINPLlIMQIVSKGDrPSLDDigr 228
                       250       260
                ....*....|....*....|....*...
gi 15230288 370 -PPWPSLSfEAKDFVKRLLYKDPRKRMT 396
Cdd:cd13978 229 lKQIENVQ-ELISLMIRCWDGNPDARPT 255
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
150-395 3.42e-15

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 76.46  E-value: 3.42e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFK-KGELkdqeVAVKVIPKSKMTSAISIEDVRREVKILrALSGHQNLVQFYDAFEDNANVYIVMELC 228
Cdd:cd05608   9 LGKGGFGEVSACQMRaTGKL----YACKKLNKKRLKKRKGYEGAMVEKRIL-AKVHSRFIVSLAYAFQTKTDLCLVMTIM 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 229 GGGELLDRIL---ARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLS-DFVRPDE 304
Cdd:cd05608  84 NGGDLRYHIYnvdEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLL---DDDGNVRISDLGLAvELKDGQT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 305 RLNDIVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPFWARTE----SGIFRAVLKADPSFDEppwpSLSFEA 379
Cdd:cd05608 161 KTKGYAGTPGFMAPELLLgEEYDYSVDYFTLGVTLYEMIAARGPFRARGEkvenKELKQRILNDSVTYSE----KFSPAS 236
                       250
                ....*....|....*.
gi 15230288 380 KDFVKRLLYKDPRKRM 395
Cdd:cd05608 237 KSICEALLAKDPEKRL 252
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
147-394 3.96e-15

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: 75.35  E-value: 3.96e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 147 GEEIGRGHFGYTCSAKFKKgelKDQEVAVK----VIP---KSKMTsaisiedvrREVKILRALSgHQNLVQFYDAFEDNA 219
Cdd:cd05084   1 GERIGRGNFGEVFSGRLRA---DNTPVAVKscreTLPpdlKAKFL---------QEARILKQYS-HPNIVRLIGVCTQKQ 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 220 NVYIVMELCGGGELLDRILARGGKYSEDDakavLIQILNVVA----FCHLQGVVHRDLKPENFLYTskeENSMLKVIDFG 295
Cdd:cd05084  68 PIYIVMELVQGGDFLTFLRTEGPRLKVKE----LIRMVENAAagmeYLESKHCIHRDLAARNCLVT---EKNVLKISDFG 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 296 LSdfvRPDErlnDIVGSAY---------YVAPEVL-HRSYTTEADVWSIGVIAY-ILLCGSRPFWARTESGIFRAVLKAd 364
Cdd:cd05084 141 MS---REEE---DGVYAATggmkqipvkWTAPEALnYGRYSSESDVWSFGILLWeTFSLGAVPYANLSNQQTREAVEQG- 213
                       250       260       270
                ....*....|....*....|....*....|....
gi 15230288 365 psfDEPPWPSLsfeAKDFVKRLLYK----DPRKR 394
Cdd:cd05084 214 ---VRLPCPEN---CPDEVYRLMEQcweyDPRKR 241
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
144-348 4.45e-15

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: 75.84  E-value: 4.45e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 144 IELGEEIGRGHFGytcsaKFKKGELKDQEVAVKVI---PKSKMTsaISIEDVRREVKILRALSgHQNLVQFYDAFEDNAN 220
Cdd:cd14147   5 LRLEEVIGIGGFG-----KVYRGSWRGELVAVKAArqdPDEDIS--VTAESVRQEARLFAMLA-HPNIIALKAVCLEEPN 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 VYIVMELCGGGELlDRILArGGKYSEDDAKAVLIQILNVVAFCHLQG---VVHRDLKPENFLYTSKEENS-----MLKVI 292
Cdd:cd14147  77 LCLVMEYAAGGPL-SRALA-GRRVPPHVLVNWAVQIARGMHYLHCEAlvpVIHRDLKSNNILLLQPIENDdmehkTLKIT 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15230288 293 DFGLSDFVRPDERLNdIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPF 348
Cdd:cd14147 155 DFGLAREWHKTTQMS-AAGTYAWMAPEVIKAStFSKGSDVWSFGVLLWELLTGEVPY 210
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
144-415 6.02e-15

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: 75.48  E-value: 6.02e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 144 IELGEeIGRGHFGYTCSAKFKKgelKDQEVAVKVIpkskmtSAISIE----DVRREVKILRALSGHQNLVQFYDAFEDNA 219
Cdd:cd06616   9 KDLGE-IGRGAFGTVNKMLHKP---SGTIMAVKRI------RSTVDEkeqkRLLMDLDVVMRSSDCPYIVKFYGALFREG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 220 NVYIVMELcgggelLDRILARGGKYSEDDAKAVLI-QILNVVAFC------HLQ---GVVHRDLKPENFLYtskEENSML 289
Cdd:cd06616  79 DCWICMEL------MDISLDKFYKYVYEVLDSVIPeEILGKIAVAtvkalnYLKeelKIIHRDVKPSNILL---DRNGNI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 290 KVIDFGLSDFVrpderLNDI-----VGSAYYVAPEVLHRS-----YTTEADVWSIGVIAYILLCGSRPFwaRTESGIF-- 357
Cdd:cd06616 150 KLCDFGISGQL-----VDSIaktrdAGCRPYMAPERIDPSasrdgYDVRSDVWSLGITLYEVATGKFPY--PKWNSVFdq 222
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 358 -RAVLKAD-PSFDEPPWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWIAGYKKIDIP 415
Cdd:cd06616 223 lTQVVKGDpPILSNSEEREFSPSFVNFVNLCLIKDESKRPKYKELLKHPFIKMYEERNVD 282
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
142-337 7.40e-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: 74.91  E-value: 7.40e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 142 SRIELGEEIGRGHFGYTCsakfkKGELKDQEVAVKVIpKSKMTSAISIEDVRREVKIlralsGHQNLVQFYDAFEDNAnV 221
Cdd:cd05083   6 QKLTLGEIIGEGEFGAVL-----QGEYMGQKVAVKNI-KCDVTAQAFLEETAVMTKL-----QHKNLVRLLGVILHNG-L 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 YIVMELCGGGELLDRILARGgkysedDAKAVLIQILNV-------VAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDF 294
Cdd:cd05083  74 YIVMELMSKGNLVNFLRSRG------RALVPVIQLLQFsldvaegMEYLESKKLVHRDLAARNILVS---EDGVAKISDF 144
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15230288 295 GLSdfvRPDERLNDIVG-SAYYVAPEVL-HRSYTTEADVWSIGVI 337
Cdd:cd05083 145 GLA---KVGSMGVDNSRlPVKWTAPEALkNKKFSSKSDVWSYGVL 186
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
141-370 8.21e-15

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: 75.43  E-value: 8.21e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 141 QSRIELGEEIGRGHFGYTCSAKF----KKGELKDQEVAVKVIpKSKMTSAiSIEDVRREVKILRALSGHQNLVQFYDAFE 216
Cdd:cd05098  12 RDRLVLGKPLGEGCFGQVVLAEAigldKDKPNRVTKVAVKML-KSDATEK-DLSDLISEMEMMKMIGKHKNIINLLGACT 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 217 DNANVYIVMELCGGGELLDRILAR---GGKY------------SEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYT 281
Cdd:cd05098  90 QDGPLYVIVEYASKGNLREYLQARrppGMEYcynpshnpeeqlSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVT 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 282 skeENSMLKVIDFGLS-DFVRPDERLNDIVGS--AYYVAPEVL-HRSYTTEADVWSIGVIAY-ILLCGSRPFWARTESGI 356
Cdd:cd05098 170 ---EDNVMKIADFGLArDIHHIDYYKKTTNGRlpVKWMAPEALfDRIYTHQSDVWSFGVLLWeIFTLGGSPYPGVPVEEL 246
                       250
                ....*....|....
gi 15230288 357 FRaVLKADPSFDEP 370
Cdd:cd05098 247 FK-LLKEGHRMDKP 259
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
195-396 8.44e-15

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: 74.84  E-value: 8.44e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 195 EVKILRALSgHQNLVQFYDAFEDNANVYIVMELCGGGELLDRILARGGKYSeddAKAVLI-QILNVVAFCHLQGVVHRDL 273
Cdd:cd14027  41 EGKMMNRLR-HSRVVKLLGVILEEGKYSLVMEYMEKGNLMHVLKKVSVPLS---VKGRIIlEIIEGMAYLHGKGVIHKDL 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 274 KPENFLYtskEENSMLKVIDFGLSDFVR-------PDERLNDIVGSA-------YYVAPEVL---HRSYTTEADVWSIGV 336
Cdd:cd14027 117 KPENILV---DNDFHIKIADLGLASFKMwskltkeEHNEQREVDGTAkknagtlYYMAPEHLndvNAKPTEKSDVYSFAI 193
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15230288 337 IAYILLCGSRPFW-ARTESGIFRAVLKAD-PSFDEPPwPSLSFEAKDFVKRLLYKDPRKRMT 396
Cdd:cd14027 194 VLWAIFANKEPYEnAINEDQIIMCIKSGNrPDVDDIT-EYCPREIIDLMKLCWEANPEARPT 254
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
163-295 1.52e-14

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


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 70.93  E-value: 1.52e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 163 FKKGELKDQEVAVKVIpksKMTSAISIEDVRREVKILRALSGHQ-NLVQFYDAFEDNANVYIVMELCGGGELLDRILarG 241
Cdd:cd13968  11 WAEGECTTIGVAVKIG---DDVNNEEGEDLESEMDILRRLKGLElNIPKVLVTEDVDGPNILLMELVKGGTLIAYTQ--E 85
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 15230288 242 GKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFG 295
Cdd:cd13968  86 EELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLS---EDGNVKLIDFG 136
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
140-405 1.54e-14

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


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 75.05  E-value: 1.54e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 140 LQSRIELGEEIGRGHFGYTCSAK-FKKGelkDQEVAVKVIPKSKMTSaisiEDVRREVKILRALS----GHQNL-VQFYD 213
Cdd:cd14215  10 LQERYEIVSTLGEGTFGRVVQCIdHRRG---GARVALKIIKNVEKYK----EAARLEINVLEKINekdpENKNLcVQMFD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 214 AFEDNANVYIVMELCGGGELldRILARGG--KYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKE------- 284
Cdd:cd14215  83 WFDYHGHMCISFELLGLSTF--DFLKENNylPYPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVNSDyeltynl 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 285 ---------ENSMLKVIDFGLSDFvrPDERLNDIVGSAYYVAPEV-LHRSYTTEADVWSIGVIAYILLCGSRPFWA---R 351
Cdd:cd14215 161 ekkrdersvKSTAIRVVDFGSATF--DHEHHSTIVSTRHYRAPEViLELGWSQPCDVWSIGCIIFEYYVGFTLFQThdnR 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 352 TESGIFRAVLKADPS------------------FDE-------------PPWPSLSFEAK------DFVKRLLYKDPRKR 394
Cdd:cd14215 239 EHLAMMERILGPIPSrmirktrkqkyfyhgrldWDEntsagryvrenckPLRRYLTSEAEehhqlfDLIESMLEYEPSKR 318
                       330
                ....*....|.
gi 15230288 395 MTASQALMHPW 405
Cdd:cd14215 319 LTLAAALKHPF 329
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
150-399 1.95e-14

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: 73.45  E-value: 1.95e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKgelkdQEVAVKVIPKSKmtsaiSIEDVRREVKILRALSgHQNLVQFYDAfeDNANVYIVMELCG 229
Cdd:cd14068   2 LGDGGFGSVYRAVYRG-----EDVAVKIFNKHT-----SFRLLRQELVVLSHLH-HPSLVALLAA--GTAPRMLVMELAP 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELlDRILAR-GGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPEN-FLYTSKEENSML-KVIDFGLSDF-----VR 301
Cdd:cd14068  69 KGSL-DALLQQdNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNvLLFTLYPNCAIIaKIADYGIAQYccrmgIK 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 302 PDErlndivGSAYYVAPEVLHRS--YTTEADVWSIGVIAY-ILLCGsrpfwARTESGifravLKADPSFDE--------- 369
Cdd:cd14068 148 TSE------GTPGFRAPEVARGNviYNQQADVYSFGLLLYdILTCG-----ERIVEG-----LKFPNEFDElaiqgklpd 211
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 15230288 370 -------PPWPSLsfeaKDFVKRLLYKDPRKRMTASQ 399
Cdd:cd14068 212 pvkeygcAPWPGV----EALIKDCLKENPQCRPTSAQ 244
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
144-339 1.95e-14

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: 73.48  E-value: 1.95e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 144 IELGEEIGRGHFGytcsaKFKKGELKDQEVAVKVIpKSKMTSAISIEdvrrEVKILRALSgHQNLVQFYDAF-EDNANVY 222
Cdd:cd05082   8 LKLLQTIGKGEFG-----DVMLGDYRGNKVAVKCI-KNDATAQAFLA----EASVMTQLR-HSNLVQLLGVIvEEKGGLY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 223 IVMELCGGGELLDRILARGgkYSEDDAKAVLIQILNVV-AFCHLQG--VVHRDLKPENFLYTskeENSMLKVIDFGLSDF 299
Cdd:cd05082  77 IVTEYMAKGSLVDYLRSRG--RSVLGGDCLLKFSLDVCeAMEYLEGnnFVHRDLAARNVLVS---EDNVAKVSDFGLTKE 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 15230288 300 VRPDERLNDIvgSAYYVAPEVL-HRSYTTEADVWSIGVIAY 339
Cdd:cd05082 152 ASSTQDTGKL--PVKWTAPEALrEKKFSTKSDVWSFGILLW 190
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
148-407 3.32e-14

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: 73.57  E-value: 3.32e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKFK-KGELkdqeVAVKVI--PKSKMTSAISIedvrREVKILRALSgHQNLVQFYDAFEDNANVYIV 224
Cdd:cd07869  11 EKLGEGSYATVYKGKSKvNGKL----VALKVIrlQEEEGTPFTAI----REASLLKGLK-HANIVLLHDIIHTKETLTLV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGgELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsmLKVIDFGLSDFVR-PD 303
Cdd:cd07869  82 FEYVHT-DLCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGE---LKLADFGLARAKSvPS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 304 ERLNDIVGSAYYVAPEVLHRS--YTTEADVWSIGVIAYILLCGSRPFWARTE-----SGIFraVLKADPSFDEPP----- 371
Cdd:cd07869 158 HTYSNEVVTLWYRPPDVLLGSteYSTCLDMWGVGCIFVEMIQGVAAFPGMKDiqdqlERIF--LVLGTPNEDTWPgvhsl 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15230288 372 -------------------WPSLSF--EAKDFVKRLLYKDPRKRMTASQALMHPWIA 407
Cdd:cd07869 236 phfkperftlyspknlrqaWNKLSYvnHAEDLASKLLQCFPKNRLSAQAALSHEYFS 292
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
142-406 3.51e-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: 73.76  E-value: 3.51e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 142 SRIELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMTSaisiEDVRREVKILRALS-------GHQNLVQFYDA 214
Cdd:cd14136  10 GRYHVVRKLGWGHFSTVWLCWDLQ---NKRFVALKVVKSAQHYT----EAALDEIKLLKCVReadpkdpGREHVVQLLDD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 215 FE----DNANVYIVMELcGGGELLDRIlarggKYSE------DDAKAVLIQILNVVAFCHLQ-GVVHRDLKPENFLYTSK 283
Cdd:cd14136  83 FKhtgpNGTHVCMVFEV-LGPNLLKLI-----KRYNyrgiplPLVKKIARQVLQGLDYLHTKcGIIHTDIKPENVLLCIS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 284 eeNSMLKVIDFGLSDFVrpDERLNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRPF-------WARTES- 354
Cdd:cd14136 157 --KIEVKIADLGNACWT--DKHFTEDIQTRQYRSPEVILGAgYGTPADIWSTACMAFELATGDYLFdphsgedYSRDEDh 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 355 ---------GIFRAVLKADP----SFDEP----------PWPSLS----------FEAKDFVKRLLYK---DPRKRMTAS 398
Cdd:cd14136 233 laliiellgRIPRSIILSGKysreFFNRKgelrhisklkPWPLEDvlvekykwskEEAKEFASFLLPMleyDPEKRATAA 312

                ....*...
gi 15230288 399 QALMHPWI 406
Cdd:cd14136 313 QCLQHPWL 320
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
148-404 3.89e-14

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: 73.04  E-value: 3.89e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFG--YTCsakfkkgeLKDQEVAVKVIPKSKMTSAISIED--VRREVKILRALSGHQNLVQFYDAFEDNANVYI 223
Cdd:cd14139   6 EKIGVGEFGsvYKC--------IKRLDGCVYAIKRSMRPFAGSSNEqlALHEVYAHAVLGHHPHVVRYYSAWAEDDHMII 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDRILAR---GGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSK--------EENS----- 287
Cdd:cd14139  78 QNEYCNGGSLQDAISENtksGNHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFICHKmqsssgvgEEVSneede 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 288 ------MLKVIDFG-LSDFVRPDERlndiVGSAYYVAPEVLHRSYT--TEADVWSIGvIAYILLCGSRPF------WART 352
Cdd:cd14139 158 flsanvVYKIGDLGhVTSINKPQVE----EGDSRFLANEILQEDYRhlPKADIFALG-LTVALAAGAEPLptngaaWHHI 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 15230288 353 ESGIFravlkadpsfdePPWP-SLSFEAKDFVKRLLYKDPRKRMTASQALMHP 404
Cdd:cd14139 233 RKGNF------------PDVPqELPESFSSLLKNMIQPDPEQRPSATALARHT 273
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
144-349 4.67e-14

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: 72.69  E-value: 4.67e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 144 IELGEEIGRGHFGYTCSAKFKKgELKDQE---VAVKVIpksKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNAN 220
Cdd:cd05092   7 IVLKWELGEGAFGKVFLAECHN-LLPEQDkmlVAVKAL---KEATESARQDFQREAELLTVLQ-HQHIVRFYGVCTEGEP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 VYIVMELCGGGELlDRILARGGKysedDAKAV------------LIQILNVVA-----FCHLQGV--VHRDLKPENFLYT 281
Cdd:cd05092  82 LIMVFEYMRHGDL-NRFLRSHGP----DAKILdggegqapgqltLGQMLQIASqiasgMVYLASLhfVHRDLATRNCLVG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 282 skeENSMLKVIDFGLSdfvrpderlNDIVGSAYY------------VAPE-VLHRSYTTEADVWSIGVIAY-ILLCGSRP 347
Cdd:cd05092 157 ---QGLVVKIGDFGMS---------RDIYSTDYYrvggrtmlpirwMPPEsILYRKFTTESDIWSFGVVLWeIFTYGKQP 224

                ..
gi 15230288 348 FW 349
Cdd:cd05092 225 WY 226
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
140-405 5.61e-14

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


Pssm-ID: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 73.35  E-value: 5.61e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 140 LQSRIELGEEIGRGHFGYT--CSAKFKKGelkdQEVAVKVIPKSKMTSaisiEDVRREVKILRALSGHQ-----NLVQFY 212
Cdd:cd14213  10 LRARYEIVDTLGEGAFGKVveCIDHKMGG----MHVAVKIVKNVDRYR----EAARSEIQVLEHLNTTDpnstfRCVQML 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 213 DAFEDNANVYIVMELCGGGELlDRILARG-GKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKE------- 284
Cdd:cd14213  82 EWFDHHGHVCIVFELLGLSTY-DFIKENSfLPFPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFVQSDyvvkynp 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 285 ---------ENSMLKVIDFGLSDFvrPDERLNDIVGSAYYVAPEV-LHRSYTTEADVWSIGVIAYILLCGSRPFW---AR 351
Cdd:cd14213 161 kmkrdertlKNPDIKVVDFGSATY--DDEHHSTLVSTRHYRAPEViLALGWSQPCDVWSIGCILIEYYLGFTVFQthdSK 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 352 TESGIFRAVLKADPSF-------------DEPPWPSLSFEAK------------------------DFVKRLLYKDPRKR 394
Cdd:cd14213 239 EHLAMMERILGPLPKHmiqktrkrkyfhhDQLDWDEHSSAGRyvrrrckplkefmlsqdvdheqlfDLIQKMLEYDPAKR 318
                       330
                ....*....|.
gi 15230288 395 MTASQALMHPW 405
Cdd:cd14213 319 ITLDEALKHPF 329
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
148-336 5.82e-14

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: 72.00  E-value: 5.82e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKFKKGELKDQEVAVKVIPKSKMTSaiSIEDVRREVKILRALSgHQNLVQFYDAFEDNAnVYIVMEL 227
Cdd:cd05060   1 KELGHGNFGSVRKGVYLMKSGKEVEVAVKTLKQEHEKA--GKKEFLREASVMAQLD-HPCIVRLIGVCKGEP-LMLVMEL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 228 CGGGELLDRILARgGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsmLKVIDFGLSDFVRPderln 307
Cdd:cd05060  77 APLGPLLKYLKKR-REIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQ---AKISDFGMSRALGA----- 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 15230288 308 divGSAYY------------VAPEVLH-RSYTTEADVWSIGV 336
Cdd:cd05060 148 ---GSDYYrattagrwplkwYAPECINyGKFSSKSDVWSYGV 186
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
194-347 6.61e-14

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 73.16  E-value: 6.61e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 194 REVKILRALSGhQNLVQFYDAFEDNANVYIVMELCGGGELlDRILARGGKYSEDDAKAVLIQILNVVAFCHLQ-GVVHRD 272
Cdd:cd06649  52 RELQVLHECNS-PYIVGFYGAFYSDGEISICMEHMDGGSL-DQVLKEAKRIPEEILGKVSIAVLRGLAYLREKhQIMHRD 129
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15230288 273 LKPENFLYTSKEEnsmLKVIDFGLSDFVrPDERLNDIVGSAYYVAPEVLHRS-YTTEADVWSIGVIAYILLCGSRP 347
Cdd:cd06649 130 VKPSNILVNSRGE---IKLCDFGVSGQL-IDSMANSFVGTRSYMSPERLQGThYSVQSDIWSMGLSLVELAIGRYP 201
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
141-399 8.98e-14

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: 71.99  E-value: 8.98e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 141 QSRIELGEEIGRGHFGYT---CSAKFKKGElKDQEVAVK-VIPKSKMTSAISIedvRREVKILRALSGHqNLVQFYDAFE 216
Cdd:cd05032   5 REKITLIRELGQGSFGMVyegLAKGVVKGE-PETRVAIKtVNENASMRERIEF---LNEASVMKEFNCH-HVVRLLGVVS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 217 DNANVYIVMELCGGGELLDRILAR---------GGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENS 287
Cdd:cd05032  80 TGQPTLVVMELMAKGDLKSYLRSRrpeaennpgLGPPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVA---EDL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 288 MLKVIDFGLSdfvrpderlNDIVGSAYY------------VAPEVLHRS-YTTEADVWSIGVIAY-ILLCGSRPFWARTE 353
Cdd:cd05032 157 TVKIGDFGMT---------RDIYETDYYrkggkgllpvrwMAPESLKDGvFTTKSDVWSFGVVLWeMATLAEQPYQGLSN 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 15230288 354 SGIFRAVLKAD--PSFDEPPWPSLsfeakDFVKRLLYKDPRKRMTASQ 399
Cdd:cd05032 228 EEVLKFVIDGGhlDLPENCPDKLL-----ELMRMCWQYNPKMRPTFLE 270
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
150-371 9.45e-14

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: 71.68  E-value: 9.45e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFG--YTCSAKFKKGE-LKDQEVAVKVIPKSKMTSaiSIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVME 226
Cdd:cd05044   3 LGSGAFGevFEGTAKDILGDgSGETKVAVKTLRKGATDQ--EKAEFLKEAHLMSNFK-HPNILKLLGVCLDNDPQYIILE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 227 LCGGGELL-----DRILARGG-KYSEDDakavLIQI-LNVVAFC-HLQGV--VHRDLKPENFLYTSKEENSM-LKVIDFG 295
Cdd:cd05044  80 LMEGGDLLsylraARPTAFTPpLLTLKD----LLSIcVDVAKGCvYLEDMhfVHRDLAARNCLVSSKDYRERvVKIGDFG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 296 LSdfvrpderlNDIVGSAYY------------VAPEVLHRSY-TTEADVWSIGVIAY-ILLCGSRPFWARTESGIFRAVl 361
Cdd:cd05044 156 LA---------RDIYKNDYYrkegegllpvrwMAPESLVDGVfTTQSDVWAFGVLMWeILTLGQQPYPARNNLEVLHFV- 225
                       250
                ....*....|
gi 15230288 362 KADPSFDEPP 371
Cdd:cd05044 226 RAGGRLDQPD 235
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
148-342 1.06e-13

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: 71.97  E-value: 1.06e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKFKKgeLKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQF----YDAfeDNANVYI 223
Cdd:cd14205  10 QQLGKGNFGSVEMCRYDP--LQDNTGEVVAVKKLQHSTEEHLRDFEREIEILKSLQ-HDNIVKYkgvcYSA--GRRNLRL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLSDFVRPD 303
Cdd:cd14205  85 IMEYLPYGSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILV---ENENRVKIGDFGLTKVLPQD 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15230288 304 ERLNDIV----GSAYYVAPEVLHRS-YTTEADVWSIGVIAYILL 342
Cdd:cd14205 162 KEYYKVKepgeSPIFWYAPESLTESkFSVASDVWSFGVVLYELF 205
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
130-371 1.16e-13

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: 72.30  E-value: 1.16e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 130 LDKRFGFSKElqsRIELGEEIGRGHFGYTCSAKFKKGELKDQE----VAVKVIpKSKMTSAiSIEDVRREVKILRALSGH 205
Cdd:cd05099   3 LDPKWEFPRD---RLVLGKPLGEGCFGQVVRAEAYGIDKSRPDqtvtVAVKML-KDNATDK-DLADLISEMELMKLIGKH 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 206 QNLVQFYDAFEDNANVYIVMELCGGGELLDRILAR---GGKYSED------------DAKAVLIQILNVVAFCHLQGVVH 270
Cdd:cd05099  78 KNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARrppGPDYTFDitkvpeeqlsfkDLVSCAYQVARGMEYLESRRCIH 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 271 RDLKPENFLYTskEENSMlKVIDFGLS------DFVR--PDERLndivgSAYYVAPEVL-HRSYTTEADVWSIGVIAY-I 340
Cdd:cd05099 158 RDLAARNVLVT--EDNVM-KIADFGLArgvhdiDYYKktSNGRL-----PVKWMAPEALfDRVYTHQSDVWSFGILMWeI 229
                       250       260       270
                ....*....|....*....|....*....|.
gi 15230288 341 LLCGSRPFWARTESGIFRaVLKADPSFDEPP 371
Cdd:cd05099 230 FTLGGSPYPGIPVEELFK-LLREGHRMDKPS 259
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
141-348 1.16e-13

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: 71.68  E-value: 1.16e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 141 QSRIELGEEIGRGHFGYTCSAKFK-KGELKDQEVAVKVIPKSkmTSAISIEDVRREVKILrALSGHQNLVQFYdAFEDNA 219
Cdd:cd05057   6 ETELEKGKVLGSGAFGTVYKGVWIpEGEKVKIPVAIKVLREE--TGPKANEEILDEAYVM-ASVDHPHLVRLL-GICLSS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 220 NVYIVMELCGGGELLDRILARGGKYsedDAKAVL---IQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGL 296
Cdd:cd05057  82 QVQLITQLMPLGCLLDYVRNHRDNI---GSQLLLnwcVQIAKGMSYLEEKRLVHRDLAARNVLVKTP---NHVKITDFGL 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15230288 297 SDFVRPDERLNDIVGSAY---YVAPE-VLHRSYTTEADVWSIGVIAYILLC-GSRPF 348
Cdd:cd05057 156 AKLLDVDEKEYHAEGGKVpikWMALEsIQYRIYTHKSDVWSYGVTVWELMTfGAKPY 212
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
150-348 1.30e-13

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 71.34  E-value: 1.30e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKGELKDQE--VAVKVIPKSKMTSAISieDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMEL 227
Cdd:cd05046  13 LGRGEFGEVFLAKAKGIEEEGGEtlVLVKALQKTKDENLQS--EFRRELDMFRKLS-HKNVVRLLGLCREAEPHYMILEY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 228 CGGGELLDRILARGGKysEDDAKAVLIQILNVVAFCH--LQGV--------VHRDLKPENFLYTSKEEnsmLKVIDFGLS 297
Cdd:cd05046  90 TDLGDLKQFLRATKSK--DEKLKPPPLSTKQKVALCTqiALGMdhlsnarfVHRDLAARNCLVSSQRE---VKVSLLSLS 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15230288 298 DFVRPDE--RLNDIVGSAYYVAPE-VLHRSYTTEADVWSIGVIAY-ILLCGSRPF 348
Cdd:cd05046 165 KDVYNSEyyKLRNALIPLRWLAPEaVQEDDFSTKSDVWSFGVLMWeVFTQGELPF 219
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
150-348 1.50e-13

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 71.02  E-value: 1.50e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGytcsaKFKKGELKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDA-FEDNANVYIVMELC 228
Cdd:cd14064   1 IGSGSFG-----KVYKGRCRNKIVAIKRYRANTYCSKSDVDMFCREVSILCRLN-HPCVIQFVGAcLDDPSQFAIVTQYV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 229 GGGELLDRIlarGGKYSEDDAKAVLIQILNV---VAFCH--LQGVVHRDLKPENFLYtskEENSMLKVIDFGLSDFV--R 301
Cdd:cd14064  75 SGGSLFSLL---HEQKRVIDLQSKLIIAVDVakgMEYLHnlTQPIIHRDLNSHNILL---YEDGHAVVADFGESRFLqsL 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15230288 302 PDERLNDIVGSAYYVAPEVLHRS--YTTEADVWSIGVIAYILLCGSRPF 348
Cdd:cd14064 149 DEDNMTKQPGNLRWMAPEVFTQCtrYSIKADVFSYALCLWELLTGEIPF 197
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
145-405 1.86e-13

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 72.76  E-value: 1.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  145 ELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVI---PKSKmtsaisiedvRREVKILRALSgHQNLVQFYDAF------ 215
Cdd:PTZ00036  69 KLGNIIGNGSFGVVYEAICID---TSEKVAIKKVlqdPQYK----------NRELLIMKNLN-HINIIFLKDYYytecfk 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  216 --EDNANVYIVMELcgggelLDRILARGGKYSEDDAKAVLI--------QILNVVAFCHLQGVVHRDLKPENFLYTSKEE 285
Cdd:PTZ00036 135 knEKNIFLNVVMEF------IPQTVHKYMKHYARNNHALPLflvklysyQLCRALAYIHSKFICHRDLKPQNLLIDPNTH 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  286 NsmLKVIDFGLSDFVRPDERLNDIVGSAYYVAPEVL--HRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLK- 362
Cdd:PTZ00036 209 T--LKLCDFGSAKNLLAGQRSVSYICSRFYRAPELMlgATNYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLVRIIQv 286
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15230288  363 -ADPSFDE-----PPWPSLSF------------------EAKDFVKRLLYKDPRKRMTASQALMHPW 405
Cdd:PTZ00036 287 lGTPTEDQlkemnPNYADIKFpdvkpkdlkkvfpkgtpdDAINFISQFLKYEPLKRLNPIEALADPF 353
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
144-348 1.88e-13

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: 70.82  E-value: 1.88e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 144 IELGEEIGRGHFGYTCSAKFKKgelkdqEVAVKVIPKSKMTSAiSIEDVRREVKILRAlSGHQNLVQFYdAFEDNANVYI 223
Cdd:cd14150   2 VSMLKRIGTGSFGTVFRGKWHG------DVAVKILKVTEPTPE-QLQAFKNEMQVLRK-TRHVNILLFM-GFMTRPNFAI 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPEN-FLYtskeENSMLKVIDFGLSDfVRP 302
Cdd:cd14150  73 ITQWCEGSSLYRHLHVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNiFLH----EGLTVKIGDFGLAT-VKT 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15230288 303 ----DERLNDIVGSAYYVAPEVLH----RSYTTEADVWSIGVIAYILLCGSRPF 348
Cdd:cd14150 148 rwsgSQQVEQPSGSILWMAPEVIRmqdtNPYSFQSDVYAYGVVLYELMSGTLPY 201
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
141-348 1.98e-13

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: 70.86  E-value: 1.98e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 141 QSRIELGEEIGRGHFGYTCSAKFKKgelkdqEVAVKVIPKSKMTSAiSIEDVRREVKILRAlSGHQNLVQFYdAFEDNAN 220
Cdd:cd14151   7 DGQITVGQRIGSGSFGTVYKGKWHG------DVAVKMLNVTAPTPQ-QLQAFKNEVGVLRK-TRHVNILLFM-GYSTKPQ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 VYIVMELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPEN-FLYtskeENSMLKVIDFGLSDF 299
Cdd:cd14151  78 LAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNiFLH----EDLTVKIGDFGLATV 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15230288 300 V---RPDERLNDIVGSAYYVAPEVLH----RSYTTEADVWSIGVIAYILLCGSRPF 348
Cdd:cd14151 154 KsrwSGSHQFEQLSGSILWMAPEVIRmqdkNPYSFQSDVYAFGIVLYELMTGQLPY 209
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
143-406 2.21e-13

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: 72.09  E-value: 2.21e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFGYTCSAKFKKGElkdQEVAVKVIPKSKMTSAISIEdvrrEVKILRAL-----SGHQNLVQFYDAFED 217
Cdd:cd14224  66 RYEVLKVIGKGSFGQVVKAYDHKTH---QHVALKMVRNEKRFHRQAAE----EIRILEHLkkqdkDNTMNVIHMLESFTF 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 218 NANVYIVMELCGGG--ELLDRILARGgkYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtSKEENSMLKVIDFG 295
Cdd:cd14224 139 RNHICMTFELLSMNlyELIKKNKFQG--FSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILL-KQQGRSGIKVIDFG 215
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 296 LSDFvrPDERLNDIVGSAYYVAPEV-LHRSYTTEADVWSIGVIAYILLCG------------------------------ 344
Cdd:cd14224 216 SSCY--EHQRIYTYIQSRFYRAPEViLGARYGMPIDMWSFGCILAELLTGyplfpgedegdqlacmiellgmppqkllet 293
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 345 ---SRPFW-----------------------ARTESGIFR---------AVLKA--DPSFdeppwpslsfeaKDFVKRLL 387
Cdd:cd14224 294 skrAKNFIsskgypryctvttlpdgsvvlngGRSRRGKMRgppgskdwvTALKGcdDPLF------------LDFLKRCL 361
                       330
                ....*....|....*....
gi 15230288 388 YKDPRKRMTASQALMHPWI 406
Cdd:cd14224 362 EWDPAARMTPSQALRHPWL 380
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
184-403 2.28e-13

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: 70.79  E-value: 2.28e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 184 TSAISIEDVRREVKILRALsGHQNLVQFYD---AFEDNAN--VYIVMELCGGGELLDRI---LARGGKYSEDDAKAVLIQ 255
Cdd:cd13986  36 HSKEDVKEAMREIENYRLF-NHPNILRLLDsqiVKEAGGKkeVYLLLPYYKRGSLQDEIerrLVKGTFFPEDRILHIFLG 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 256 ILNVVAFCH---LQGVVHRDLKPENFLYTSkeenSMLKVI-DFGLSDFVRPD-------ERLNDIV---GSAYYVAPEVL 321
Cdd:cd13986 115 ICRGLKAMHepeLVPYAHRDIKPGNVLLSE----DDEPILmDLGSMNPARIEiegrreaLALQDWAaehCTMPYRAPELF 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 322 H-RSYTT---EADVWSIGVIAYILLCGSRPFWARTESG--IFRAVLKADPSFdePPWPSLSFEAKDFVKRLLYKDPRKRM 395
Cdd:cd13986 191 DvKSHCTideKTDIWSLGCTLYALMYGESPFERIFQKGdsLALAVLSGNYSF--PDNSRYSEELHQLVKSMLVVNPAERP 268

                ....*...
gi 15230288 396 TASQALMH 403
Cdd:cd13986 269 SIDDLLSR 276
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
143-348 2.42e-13

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: 70.42  E-value: 2.42e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFGYTCSAKFKKgelkdqEVAVKVIPKSKMTSAiSIEDVRREVKILRAlSGHQNLVQFYDAFEDNANVY 222
Cdd:cd14153   1 QLEIGELIGKGRFGQVYHGRWHG------EVAIRLIDIERDNEE-QLKAFKREVMAYRQ-TRHENVVLFMGACMSPPHLA 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 223 IVMELCGGGELLdrILARGGKYSEDDAKAVLI--QILNVVAFCHLQGVVHRDLKPENFLYtskeENSMLKVIDFGLSDFV 300
Cdd:cd14153  73 IITSLCKGRTLY--SVVRDAKVVLDVNKTRQIaqEIVKGMGYLHAKGILHKDLKSKNVFY----DNGKVVITDFGLFTIS 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15230288 301 ------RPDERLNDIVGSAYYVAPEVLHR----------SYTTEADVWSIGVIAYILLCGSRPF 348
Cdd:cd14153 147 gvlqagRREDKLRIQSGWLCHLAPEIIRQlspeteedklPFSKHSDVFAFGTIWYELHAREWPF 210
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
194-401 2.72e-13

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: 70.62  E-value: 2.72e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 194 REVKILRALSGHQNLVQFYDA--------FEDNANVYIVMELCGGGeLLDRI--LARGGKYSEDDAKAVLIQILNVVAFC 263
Cdd:cd14036  46 QEINFMKKLSGHPNIVQFCSAasigkeesDQGQAEYLLLTELCKGQ-LVDFVkkVEAPGPFSPDTVLKIFYQTCRAVQHM 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 264 HLQG--VVHRDLKPENFLYTSKeenSMLKVIDFGLSDFV--RPD------------ERLNDiVGSAYYVAPEV--LHRSY 325
Cdd:cd14036 125 HKQSppIIHRDLKIENLLIGNQ---GQIKLCDFGSATTEahYPDyswsaqkrslveDEITR-NTTPMYRTPEMidLYSNY 200
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15230288 326 --TTEADVWSIGVIAYILLCGSRPFwartESGIFRAVLKADpsFDEPPWPSLSFEAKDFVKRLLYKDPRKRMTASQAL 401
Cdd:cd14036 201 piGEKQDIWALGCILYLLCFRKHPF----EDGAKLRIINAK--YTIPPNDTQYTVFHDLIRSTLKVNPEERLSITEIV 272
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
141-337 5.90e-13

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: 69.37  E-value: 5.90e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 141 QSRIELGEEIGRGHFGYTCSAKFKKgelKDQEVAVKVIPKSKMtsaiSIEDVRREVKILRALSgHQNLVQFYDAFEDNAN 220
Cdd:cd05052   5 RTDITMKHKLGGGQYGEVYEGVWKK---YNLTVAVKTLKEDTM----EVEEFLKEAAVMKEIK-HPNLVQLLGVCTREPP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 VYIVMELCGGGELLDRIlaRGGKYSEDDAKAVL---IQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLS 297
Cdd:cd05052  77 FYIITEFMPYGNLLDYL--RECNREELNAVVLLymaTQIASAMEYLEKKNFIHRDLAARNCLV---GENHLVKVADFGLS 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15230288 298 DFVRpDERLNDIVGSAY---YVAPEVL-HRSYTTEADVWSIGVI 337
Cdd:cd05052 152 RLMT-GDTYTAHAGAKFpikWTAPESLaYNKFSIKSDVWAFGVL 194
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
150-399 7.13e-13

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: 69.18  E-value: 7.13e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKgelkdQEVAVKVIPKSK------------------MTSAISIEDVRREVKILRALSgHQNLVQF 211
Cdd:cd14000   2 LGDGGFGSVYRASYKG-----EPVAVKIFNKHTssnfanvpadtmlrhlraTDAMKNFRLLRQELTVLSHLH-HPSIVYL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 212 YdafedNANVY---IVMELCGGGELlDRILArggKYSEDDA-------KAVLIQILNVVAFCHLQGVVHRDLKPENFLYT 281
Cdd:cd14000  76 L-----GIGIHplmLVLELAPLGSL-DHLLQ---QDSRSFAslgrtlqQRIALQVADGLRYLHSAMIIYRDLKSHNVLVW 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 282 SKEENSML--KVIDFGLSDFVRPdERLNDIVGSAYYVAPEVLHRS--YTTEADVWSIGVIAYILLCGSRPFWARTESGIF 357
Cdd:cd14000 147 TLYPNSAIiiKIADYGISRQCCR-MGAKGSEGTPGFRAPEIARGNviYNEKVDVFSFGMLLYEILSGGAPMVGHLKFPNE 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 15230288 358 RAVLKADP----SFDEPPWPslsfEAKDFVKRLLYKDPRKRMTASQ 399
Cdd:cd14000 226 FDIHGGLRpplkQYECAPWP----EVEVLMKKCWKENPQQRPTAVT 267
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
194-343 7.85e-13

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: 68.83  E-value: 7.85e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 194 REVKILRALSgHQNLVQFYDAFEDNANVYIVMELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDL 273
Cdd:cd14221  39 KEVKVMRCLE-HPNVLKFIGVLYKDKRLNFITEYIKGGTLRGIIKSMDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDL 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 274 KPENFLYtskEENSMLKVIDFGLSDFV--------------RPDERLN-DIVGSAYYVAPEVLH-RSYTTEADVWSIGvi 337
Cdd:cd14221 118 NSHNCLV---RENKSVVVADFGLARLMvdektqpeglrslkKPDRKKRyTVVGNPYWMAPEMINgRSYDEKVDVFSFG-- 192

                ....*.
gi 15230288 338 ayILLC 343
Cdd:cd14221 193 --IVLC 196
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
150-352 7.99e-13

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: 68.91  E-value: 7.99e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKGELKdQEVAVKVIpkSKMTSAISIEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd05047   3 IGEGNFGQVLKARIKKDGLR-MDAAIKRM--KEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLD-----RILARGGKYSEDDAKAVLI---QILNVVA-------FCHLQGVVHRDLKPENFLYTskeENSMLKVIDF 294
Cdd:cd05047  80 HGNLLDflrksRVLETDPAFAIANSTASTLssqQLLHFAAdvargmdYLSQKQFIHRDLAARNILVG---ENYVAKIADF 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15230288 295 GLSdfvRPDE-RLNDIVGS--AYYVAPEVLHRS-YTTEADVWSIGVIAY-ILLCGSRPFWART 352
Cdd:cd05047 157 GLS---RGQEvYVKKTMGRlpVRWMAIESLNYSvYTTNSDVWSYGVLLWeIVSLGGTPYCGMT 216
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
143-297 8.26e-13

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


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 68.82  E-value: 8.26e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFGYTCSAKfkkGELKDQEVAVKVIPKSKMTSAISIEdvrreVKILRALSGHQNLVQFYDAFEDNANVY 222
Cdd:cd14017   1 RWKVVKKIGGGGFGEIYKVR---DVVDGEEVAMKVESKSQPKQVLKME-----VAVLKKLQGKPHFCRLIGCGRTERYNY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 223 IVMELCGG--GELldRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENF---LYTSKEENsmLKVIDFGLS 297
Cdd:cd14017  73 IVMTLLGPnlAEL--RRSQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFaigRGPSDERT--VYILDFGLA 148
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
145-372 1.15e-12

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


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 68.29  E-value: 1.15e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFG--YTCSAKFKKGELKDQEVavkVIPKSKmtsaiSIEDVRREVKILRALSGHQNLVQFYDAFEDNA--- 219
Cdd:cd13975   3 KLGRELGRGQYGvvYACDSWGGHFPCALKSV---VPPDDK-----HWNDLALEFHYTRSLPKHERIVSLHGSVIDYSygg 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 220 ----NVYIVMELcgggelLDRILARGGK--YSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENsmlKVID 293
Cdd:cd13975  75 gssiAVLLIMER------LHRDLYTGIKagLSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRA---KITD 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 294 FGlsdFVRPDERLN-DIVGSAYYVAPEVLHRSYTTEADVWSIGVIAYILLCGS-------------RPFWARTESGIFRA 359
Cdd:cd13975 146 LG---FCKPEAMMSgSIVGTPIHMAPELFSGKYDNSVDVYAFGILFWYLCAGHvklpeafeqcaskDHLWNNVRKGVRPE 222
                       250
                ....*....|...
gi 15230288 360 VLkadPSFDEPPW 372
Cdd:cd13975 223 RL---PVFDEECW 232
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
150-401 1.33e-12

Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein 15; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Vps15 is a large protein consisting of an N-terminal kinase domain, a C-terminal WD-repeat containing domain, and an intermediate bridge domain that contain HEAT repeats. The kinase domain is necessary for the signaling functions of Vps15. Human Vps15 was previously called p150. It associates and regulates Vps34, also called Class III phosphoinositide 3-kinase (PI3K), which catalyzes the phosphorylation of D-myo-phosphatidylinositol (PtdIns). Vps34 is the only PI3K present in yeast. It plays an important role in the regulation of protein and vesicular trafficking and sorting, autophagy, trimeric G-protein signaling, and phagocytosis. The Vps15 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 68.43  E-value: 1.33e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKGElkdqeVAVKVIPKSKmtSAISIEDVRREVKILR-ALSGHQNLVQFYDAFEDNANVYIVMELC 228
Cdd:cd13980   8 LGSTRFLKVARARHDEGL-----VVVKVFVKPD--PALPLRSYKQRLEEIRdRLLELPNVLPFQKVIETDKAAYLIRQYV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 229 GGgELLDRILARggKYSEDDAKAVLI-QILNVVAFCHLQGVVHRDLKPENFLYTSkeENSMLkvidfgLSDF-------- 299
Cdd:cd13980  81 KY-NLYDRISTR--PFLNLIEKKWIAfQLLHALNQCHKRGVCHGDIKTENVLVTS--WNWVY------LTDFasfkptyl 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 300 ---------------------VRPdERLNDivgSAYYVAPEVLHRSYTTEA-DVWSIG-VIAYILLCGSRPFwarTESGI 356
Cdd:cd13980 150 pednpadfsyffdtsrrrtcyIAP-ERFVD---ALTLDAESERRDGELTPAmDIFSLGcVIAELFTEGRPLF---DLSQL 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 15230288 357 FRavLKADPSFDEppwPSLSFEAKDFVKRL----LYKDPRKRMTASQAL 401
Cdd:cd13980 223 LA--YRKGEFSPE---QVLEKIEDPNIRELilhmIQRDPSKRLSAEDYL 266
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
172-396 1.60e-12

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: 67.63  E-value: 1.60e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 172 EVAVKVIPKSKMtsaiSIEDVRREVKILRALSgHQNLVQFYdAFEDNANVYIVMELCGGGELLDRILARGGKYSE----D 247
Cdd:cd14203  21 KVAIKTLKPGTM----SPEAFLEEAQIMKKLR-HDKLVQLY-AVVSEEPIYIVTEFMSKGSLLDFLKDGEGKYLKlpqlV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 248 DAKAvliQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFVRPDErLNDIVGSAY---YVAPEV-LHR 323
Cdd:cd14203  95 DMAA---QIASGMAYIERMNYIHRDLRAANILVG---DNLVCKIADFGLARLIEDNE-YTARQGAKFpikWTAPEAaLYG 167
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15230288 324 SYTTEADVWSIGVIAYILLCGSR-PFWARTEsgifRAVL-KADPSFDEPPWPSLSFEAKDFVKRLLYKDPRKRMT 396
Cdd:cd14203 168 RFTIKSDVWSFGILLTELVTKGRvPYPGMNN----REVLeQVERGYRMPCPPGCPESLHELMCQCWRKDPEERPT 238
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
148-405 2.14e-12

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


Pssm-ID: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 68.23  E-value: 2.14e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFG--YTCSAKFKKGELKDQEVAVKvipKSKMTSAISI---EDVRREV-----KILRALSGHQN---------L 208
Cdd:cd14013   1 KKLGEGGFGtvYKGSLLQKDPGGEKRRVVLK---KAKEYGEVEIwmnERVRRACpsscaEFVGAFLDTTSkkftkpslwL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 209 V-QF------YDAFEDNANVYIVMELCGGGELldrILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYT 281
Cdd:cd14013  78 VwKYegdatlADLMQGKEFPYNLEPIIFGRVL---IPPRGPKRENVIIKSIMRQILVALRKLHSTGIVHRDVKPQNIIVS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 282 skEENSMLKVIDFGLSDFVR------PDERLNDivgsAYYVAPEVLHRSYTTEA-----------------------DVW 332
Cdd:cd14013 155 --EGDGQFKIIDLGAAADLRiginyiPKEFLLD----PRYAPPEQYIMSTQTPSappapvaaalspvlwqmnlpdrfDMY 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 333 SIGViayILLCGSRPFwARTESGI--FRAVLKAdPSFDEPPWPSL-----------SFEAKD--------FVKRLLYKDP 391
Cdd:cd14013 229 SAGV---ILLQMAFPN-LRSDSNLiaFNRQLKQ-CDYDLNAWRMLveprasadlreGFEILDlddgagwdLVTKLIRYKP 303
                       330
                ....*....|....
gi 15230288 392 RKRMTASQALMHPW 405
Cdd:cd14013 304 RGRLSASAALAHPY 317
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
141-360 2.49e-12

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: 67.36  E-value: 2.49e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 141 QSRIELGEEIGRGHFGYTCSAKFKKgelkDQEVAVKVIPKSKMtsaiSIEDVRREVKILRALSgHQNLVQFYdAFEDNAN 220
Cdd:cd05073  10 RESLKLEKKLGAGQFGEVWMATYNK----HTKVAVKTMKPGSM----SVEAFLAEANVMKTLQ-HDKLVKLH-AVVTKEP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 VYIVMELCGGGELLDRILA-RGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKeenSMLKVIDFGLSDF 299
Cdd:cd05073  80 IYIITEFMAKGSLLDFLKSdEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSAS---LVCKIADFGLARV 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15230288 300 VRPDERLNDiVGSAY---YVAPEVL-HRSYTTEADVWSIGV-IAYILLCGSRPFWARTESGIFRAV 360
Cdd:cd05073 157 IEDNEYTAR-EGAKFpikWTAPEAInFGSFTIKSDVWSFGIlLMEIVTYGRIPYPGMSNPEVIRAL 221
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
142-348 3.28e-12

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


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 67.36  E-value: 3.28e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 142 SRIELGEEIGRGHFGYTCSAKFKKgelkdqEVAVKVIPKSKMTSAiSIEDVRREVKILRAlSGHQNLVQFYdAFEDNANV 221
Cdd:cd14149  12 SEVMLSTRIGSGSFGTVYKGKWHG------DVAVKILKVVDPTPE-QFQAFRNEVAVLRK-TRHVNILLFM-GYMTKDNL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 YIVMELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPEN-FLYtskeENSMLKVIDFGLSDFV 300
Cdd:cd14149  83 AIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNiFLH----EGLTVKIGDFGLATVK 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15230288 301 ---RPDERLNDIVGSAYYVAPEVL----HRSYTTEADVWSIGVIAYILLCGSRPF 348
Cdd:cd14149 159 srwSGSQQVEQPTGSILWMAPEVIrmqdNNPFSFQSDVYSYGIVLYELMTGELPY 213
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
150-360 3.74e-12

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: 66.92  E-value: 3.74e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKGELKDQEVAVKVIpKSKMTSAiSIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELCG 229
Cdd:cd05063  13 IGAGEFGEVFRGILKMPGRKEVAVAIKTL-KPGYTEK-QRQDFLSEASIMGQFS-HHNIIRLEGVVTKFKPAMIITEYME 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSDFVRPD-ERLND 308
Cdd:cd05063  90 NGALDKYLRDHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNS---NLECKVSDFGLSRVLEDDpEGTYT 166
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15230288 309 IVGSAY---YVAPEVL-HRSYTTEADVWSIGVIAY-ILLCGSRPFWARTESGIFRAV 360
Cdd:cd05063 167 TSGGKIpirWTAPEAIaYRKFTSASDVWSFGIVMWeVMSFGERPYWDMSNHEVMKAI 223
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
150-395 4.00e-12

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: 67.78  E-value: 4.00e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFG--YTCSaKFKKGELkdqeVAVKVIPKS--KMTSAISIEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIVM 225
Cdd:cd05633  13 IGRGGFGevYGCR-KADTGKM----YAMKCLDKKriKMKQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCFIL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 226 ELCGGGELlDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLS-DFVRpdE 304
Cdd:cd05633  88 DLMNGGDL-HYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL---DEHGHVRISDLGLAcDFSK--K 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 305 RLNDIVGSAYYVAPEVLHR--SYTTEADVWSIGVIAYILLCGSRPFW---ARTESGIFRAVLKADPSFDEppwpSLSFEA 379
Cdd:cd05633 162 KPHASVGTHGYMAPEVLQKgtAYDSSADWFSLGCMLFKLLRGHSPFRqhkTKDKHEIDRMTLTVNVELPD----SFSPEL 237
                       250
                ....*....|....*.
gi 15230288 380 KDFVKRLLYKDPRKRM 395
Cdd:cd05633 238 KSLLEGLLQRDVSKRL 253
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
144-352 4.12e-12

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: 67.33  E-value: 4.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 144 IELGEEIGRGHFGYTCSAKFKKGELKdQEVAVKVIpkSKMTSAISIEDVRREVKILRALSGHQNLVQFYDAFEDNANVYI 223
Cdd:cd05089   4 IKFEDVIGEGNFGQVIKAMIKKDGLK-MNAAIKML--KEFASENDHRDFAGELEVLCKLGHHPNIINLLGACENRGYLYI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLD-----RILARGGKYSEDDAKAV------LIQILNVVA----FCHLQGVVHRDLKPENFLYTskeENSM 288
Cdd:cd05089  81 AIEYAPYGNLLDflrksRVLETDPAFAKEHGTAStltsqqLLQFASDVAkgmqYLSEKQFIHRDLAARNVLVG---ENLV 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15230288 289 LKVIDFGLSdfvRPDE-RLNDIVGS--AYYVAPEVLHRS-YTTEADVWSIGVIAY-ILLCGSRPFWART 352
Cdd:cd05089 158 SKIADFGLS---RGEEvYVKKTMGRlpVRWMAIESLNYSvYTTKSDVWSFGVLLWeIVSLGGTPYCGMT 223
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
159-343 6.44e-12

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: 66.00  E-value: 6.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 159 CSAKFKKGELKDQEVAVKVIPKSKmtsaISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELCGGGeLLDRIL 238
Cdd:cd14156   6 FSKVYKVTHGATGKVMVVKIYKND----VDQHKIVREISLLQKLS-HPNIVRYLGICVKDEKLHPILEYVSGG-CLEELL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 239 ARGG-KYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLSDFV------RPDERLNdIVG 311
Cdd:cd14156  80 AREElPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGREAVVTDFGLAREVgempanDPERKLS-LVG 158
                       170       180       190
                ....*....|....*....|....*....|...
gi 15230288 312 SAYYVAPEVLH-RSYTTEADVWSIGviayILLC 343
Cdd:cd14156 159 SAFWMAPEMLRgEPYDRKVDVFSFG----IVLC 187
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
173-349 9.29e-12

Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-A binds and is activated by the atrial and B-type natriuretic peptides, ANP and BNP, which are important in blood pressure regulation and cardiac pathophysiology. GC-B binds the C-type natriuretic peptide, CNP, which is a potent vasorelaxant and functions in vascular remodeling and bone growth regulation. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-A/B subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270944 [Multi-domain]  Cd Length: 279  Bit Score: 66.08  E-value: 9.29e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 173 VAVKVIPKSkmtsaiSIED---VRREVKILRALSgHQNLVQFYDAFEDNANVYIVMELCGGGELLDrILarggkysEDDA 249
Cdd:cd14042  33 VAIKKVNKK------RIDLtreVLKELKHMRDLQ-HDNLTRFIGACVDPPNICILTEYCPKGSLQD-IL-------ENED 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 250 -------KAVLIQ-ILNVVAFCHLQGVV-HRDLKPENFLYTSKeenSMLKVIDFGLSDFVRPDERLNDivGSAYY----- 315
Cdd:cd14042  98 ikldwmfRYSLIHdIVKGMHYLHDSEIKsHGNLKSSNCVVDSR---FVLKITDFGLHSFRSGQEPPDD--SHAYYakllw 172
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15230288 316 VAPEVLHRSY-----TTEADVWSIGVIAYILLCGSRPFW 349
Cdd:cd14042 173 TAPELLRDPNppppgTQKGDVYSFGIILQEIATRQGPFY 211
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
194-337 9.61e-12

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: 65.57  E-value: 9.61e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 194 REVKILRALSgHQNLVQFYDAFEDNANVYIVMELCGGGELlDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDL 273
Cdd:cd14155  37 REVQLMNRLS-HPNILRFMGVCVHQGQLHALTEYINGGNL-EQLLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDL 114
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 274 KPENFLYTSKEENSMLKVIDFGLSDFVrPD-----ERLnDIVGSAYYVAPEVLH-RSYTTEADVWSIGVI 337
Cdd:cd14155 115 TSKNCLIKRDENGYTAVVGDFGLAEKI-PDysdgkEKL-AVVGSPYWMAPEVLRgEPYNEKADVFSYGII 182
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
144-396 1.01e-11

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: 65.86  E-value: 1.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 144 IELGEEIGRGHFGYTCSAKFKkGELKdqeVAVKVIPKSKMTSAISIEdvrrEVKILRALSgHQNLVQFYDAFEDNAnVYI 223
Cdd:cd05069  14 LRLDVKLGQGCFGEVWMGTWN-GTTK---VAIKTLKPGTMMPEAFLQ----EAQIMKKLR-HDKLVPLYAVVSEEP-IYI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDRILARGGKYSE-DDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFVRp 302
Cdd:cd05069  84 VTEFMGKGSLLDFLKEGDGKYLKlPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVG---DNLVCKIADFGLARLIE- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 303 DERLNDIVGSAY---YVAPE-VLHRSYTTEADVWSIGVIAYILLCGSR-PFwartESGIFRAVLKADPSFDEPPWPSLSF 377
Cdd:cd05069 160 DNEYTARQGAKFpikWTAPEaALYGRFTIKSDVWSFGILLTELVTKGRvPY----PGMVNREVLEQVERGYRMPCPQGCP 235
                       250       260
                ....*....|....*....|
gi 15230288 378 EAKDFVKRLLY-KDPRKRMT 396
Cdd:cd05069 236 ESLHELMKLCWkKDPDERPT 255
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
150-395 1.20e-11

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: 66.22  E-value: 1.20e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFG--YTCSaKFKKGELkdqeVAVKVIPKS--KMTSAISIEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIVM 225
Cdd:cd14223   8 IGRGGFGevYGCR-KADTGKM----YAMKCLDKKriKMKQGETLALNERIMLSLVSTGDCPFIVCMSYAFHTPDKLSFIL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 226 ELCGGGELlDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLS-DFVRpdE 304
Cdd:cd14223  83 DLMNGGDL-HYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILL---DEFGHVRISDLGLAcDFSK--K 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 305 RLNDIVGSAYYVAPEVLHR--SYTTEADVWSIGVIAYILLCGSRPFW---ARTESGIFRAVLKADPSFDEppwpSLSFEA 379
Cdd:cd14223 157 KPHASVGTHGYMAPEVLQKgvAYDSSADWFSLGCMLFKLLRGHSPFRqhkTKDKHEIDRMTLTMAVELPD----SFSPEL 232
                       250
                ....*....|....*.
gi 15230288 380 KDFVKRLLYKDPRKRM 395
Cdd:cd14223 233 RSLLEGLLQRDVNRRL 248
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
173-409 1.22e-11

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: 65.67  E-value: 1.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 173 VAVKVIPKSkmtsaISIEDVRR---EVKILRALSGhQNLVQFYDAFEDNANVYIVMELCGGGELldrilarggkyseDDA 249
Cdd:cd06619  29 LAVKVIPLD-----ITVELQKQimsELEILYKCDS-PYIIGFYGAFFVENRISICTEFMDGGSL-------------DVY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 250 KAVLIQILNVVAFCHLQG--------VVHRDLKPENFLYTSKEEnsmLKVIDFGLSDfvrpdERLNDI----VGSAYYVA 317
Cdd:cd06619  90 RKIPEHVLGRIAVAVVKGltylwslkILHRDVKPSNMLVNTRGQ---VKLCDFGVST-----QLVNSIaktyVGTNAYMA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 318 PE-VLHRSYTTEADVWSIGVIAYILLCGSRP---FWARTESGIFRAVLKADPSFDEPPWPSLSFEAK--DFVKRLLYKDP 391
Cdd:cd06619 162 PErISGEQYGIHSDVWSLGISFMELALGRFPypqIQKNQGSLMPLQLLQCIVDEDPPVLPVGQFSEKfvHFITQCMRKQP 241
                       250
                ....*....|....*...
gi 15230288 392 RKRMTASQALMHPWIAGY 409
Cdd:cd06619 242 KERPAPENLMDHPFIVQY 259
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
143-352 1.29e-11

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 65.49  E-value: 1.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFG--YTCSAKFKKGELKDQEVAVKVIPKSkmTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNAN 220
Cdd:cd05036   7 NLTLIRALGQGAFGevYEGTVSGMPGDPSPLQVAVKTLPEL--CSEQDEMDFLMEALIMSKFN-HPNIVRCIGVCFQRLP 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 VYIVMELCGGGEL---LDRILARGGKYSEDDAKAVLIQILNVVAFCHL---QGVVHRDLKPENFLYTSKEENSMLKVIDF 294
Cdd:cd05036  84 RFILLELMAGGDLksfLRENRPRPEQPSSLTMLDLLQLAQDVAKGCRYleeNHFIHRDIAARNCLLTCKGPGRVAKIGDF 163
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15230288 295 GLSdfvrpderlNDIVGSAYY------------VAPEV-LHRSYTTEADVWSIGVIAY-ILLCGSRPFWART 352
Cdd:cd05036 164 GMA---------RDIYRADYYrkggkamlpvkwMPPEAfLDGIFTSKTDVWSFGVLLWeIFSLGYMPYPGKS 226
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
143-396 1.33e-11

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: 65.75  E-value: 1.33e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFGYTCSA-KFK-KGELKDQEVAVKVIPKSkmTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNAN 220
Cdd:cd05045   1 NLVLGKTLGEGEFGKVVKAtAFRlKGRAGYTTVAVKMLKEN--ASSSELRDLLSEFNLLKQVN-HPHVIKLYGACSQDGP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 VYIVMELCGGGEL-----LDRILARGGKYSE----------DDAKAVLIQILNVVAFCHLQG--------VVHRDLKPEN 277
Cdd:cd05045  78 LLLIVEYAKYGSLrsflrESRKVGPSYLGSDgnrnssyldnPDERALTMGDLISFAWQISRGmqylaemkLVHRDLAARN 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 278 FLYTskeENSMLKVIDFGLSDFVRPDE----RLNDIVgSAYYVAPEVL-HRSYTTEADVWSIGVIAY-ILLCGSRPFWAR 351
Cdd:cd05045 158 VLVA---EGRKMKISDFGLSRDVYEEDsyvkRSKGRI-PVKWMAIESLfDHIYTTQSDVWSFGVLLWeIVTLGGNPYPGI 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 15230288 352 TESGIFrAVLKADPSFDEPpwPSLSFEAKDFVKRLLYKDPRKRMT 396
Cdd:cd05045 234 APERLF-NLLKTGYRMERP--ENCSEEMYNLMLTCWKQEPDKRPT 275
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
144-363 1.71e-11

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: 65.42  E-value: 1.71e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 144 IELGEEIGRGHFGYTCSAK-FKKGELKDQE-VAVKVIPKSKMTSAisiEDVRREVKILRALSgHQNLVQFYDAFEDNANV 221
Cdd:cd05094   7 IVLKRELGEGAFGKVFLAEcYNLSPTKDKMlVAVKTLKDPTLAAR---KDFQREAELLTNLQ-HDHIVKFYGVCGDGDPL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 YIVMELCGGGELLDRILARG--------GKYSEDDAKAVLIQILNV-------VAFCHLQGVVHRDLKPENFLYTSkeeN 286
Cdd:cd05094  83 IMVFEYMKHGDLNKFLRAHGpdamilvdGQPRQAKGELGLSQMLHIatqiasgMVYLASQHFVHRDLATRNCLVGA---N 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 287 SMLKVIDFGLSdfvrpderlNDIVGSAYY------------VAPE-VLHRSYTTEADVWSIGVIAY-ILLCGSRPFWART 352
Cdd:cd05094 160 LLVKIGDFGMS---------RDVYSTDYYrvgghtmlpirwMPPEsIMYRKFTTESDVWSFGVILWeIFTYGKQPWFQLS 230
                       250
                ....*....|.
gi 15230288 353 ESGIFRAVLKA 363
Cdd:cd05094 231 NTEVIECITQG 241
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
140-405 2.67e-11

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


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 65.03  E-value: 2.67e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 140 LQSRIELGEEIGRGHFGYTCSA-KFKKGElkdQEVAVKVIPKSKMTSaisiEDVRREVKILRAL----SGHQNL-VQFYD 213
Cdd:cd14214  11 LQERYEIVGDLGEGTFGKVVEClDHARGK---SQVALKIIRNVGKYR----EAARLEINVLKKIkekdKENKFLcVLMSD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 214 AFEDNANVYIVMELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKE--------- 284
Cdd:cd14214  84 WFNFHGHMCIAFELLGKNTFEFLKENNFQPYPLPHIRHMAYQLCHALKFLHENQLTHTDLKPENILFVNSEfdtlynesk 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 285 -------ENSMLKVIDFGLSDFvrPDERLNDIVGSAYYVAPEV-LHRSYTTEADVWSIGVIAYILLCGSRPFWA---RTE 353
Cdd:cd14214 164 sceeksvKNTSIRVADFGSATF--DHEHHTTIVATRHYRPPEViLELGWAQPCDVWSLGCILFEYYRGFTLFQThenREH 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 354 SGIFRAVLKADPS------------------FDEPP----------WPSLSFEAK---------DFVKRLLYKDPRKRMT 396
Cdd:cd14214 242 LVMMEKILGPIPShmihrtrkqkyfykgslvWDENSsdgryvsencKPLMSYMLGdslehtqlfDLLRRMLEFDPALRIT 321

                ....*....
gi 15230288 397 ASQALMHPW 405
Cdd:cd14214 322 LKEALLHPF 330
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
149-407 4.10e-11

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: 63.97  E-value: 4.10e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 149 EIGRGHFgytcsAKFKKGelKDQEVAVKV----IPKSKMTSAiSIEDVRREVKILRALSgHQNLVQFYDAFED----NAN 220
Cdd:cd14031  17 ELGRGAF-----KTVYKG--LDTETWVEVawceLQDRKLTKA-EQQRFKEEAEMLKGLQ-HPNIVRFYDSWESvlkgKKC 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 VYIVMELCGGGELlDRILARGGKYSEDDAKAVLIQILNVVAFCHLQG--VVHRDLKPENFLYTSKeeNSMLKVIDFGLSD 298
Cdd:cd14031  88 IVLVTELMTSGTL-KTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGP--TGSVKIGDLGLAT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 299 FVRPdERLNDIVGSAYYVAPEVLHRSYTTEADVWSIGVIAYILLCGSRPFW-ARTESGIFRAVLKA--DPSFDEPPWPsl 375
Cdd:cd14031 165 LMRT-SFAKSVIGTPEFMAPEMYEEHYDESVDVYAFGMCMLEMATSEYPYSeCQNAAQIYRKVTSGikPASFNKVTDP-- 241
                       250       260       270
                ....*....|....*....|....*....|..
gi 15230288 376 sfEAKDFVKRLLYKDPRKRMTASQALMHPWIA 407
Cdd:cd14031 242 --EVKEIIEGCIRQNKSERLSIKDLLNHAFFA 271
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
249-400 4.13e-11

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


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 64.44  E-value: 4.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 249 AKAVLIQILNVVAFCHLQGVVHRDLKPENFLYT-SKEENSMLKVIDFG--------------LSDFVrpderlnDIVGSA 313
Cdd:cd14018 140 ARVMILQLLEGVDHLVRHGIAHRDLKSDNILLElDFDGCPWLVIADFGccladdsiglqlpfSSWYV-------DRGGNA 212
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 314 YYVAPEVLHRS--------YtTEADVWSIGVIAYILLCGSRPFWARTESGIFRAvlkadpSFDEPPWPSLS----FEAKD 381
Cdd:cd14018 213 CLMAPEVSTAVpgpgvvinY-SKADAWAVGAIAYEIFGLSNPFYGLGDTMLESR------SYQESQLPALPsavpPDVRQ 285
                       170
                ....*....|....*....
gi 15230288 382 FVKRLLYKDPRKRMTASQA 400
Cdd:cd14018 286 VVKDLLQRDPNKRVSARVA 304
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
190-341 5.17e-11

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 61.13  E-value: 5.17e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 190 EDVRREVKILRALSGHQNLV-QFYDAFEDNAnvYIVMELCGGGELLDRILARggkyseDDAKAVLIQILNVVAFCHLQGV 268
Cdd:COG3642   1 ERTRREARLLRELREAGVPVpKVLDVDPDDA--DLVMEYIEGETLADLLEEG------ELPPELLRELGRLLARLHRAGI 72
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15230288 269 VHRDLKPENFLYTSKEensmLKVIDFGLSDFVRPDE-RLNDIvgsayyvapEVLHRSYTTEADVWSIGVIAYIL 341
Cdd:COG3642  73 VHGDLTTSNILVDDGG----VYLIDFGLARYSDPLEdKAVDL---------AVLKRSLESTHPDPAEELWEAFL 133
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
144-363 5.43e-11

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: 63.91  E-value: 5.43e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 144 IELGEEIGRGHFGYTCSAKFKKgELKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNANVYI 223
Cdd:cd05093   7 IVLKRELGEGAFGKVFLAECYN-LCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQ-HEHIVKFYGVCVEGDPLIM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGEL--------LDRILARGGKYSEDDAKAVLIQILNVVA----FCHLQGVVHRDLKPENFLYTskeENSMLKV 291
Cdd:cd05093  85 VFEYMKHGDLnkflrahgPDAVLMAEGNRPAELTQSQMLHIAQQIAagmvYLASQHFVHRDLATRNCLVG---ENLLVKI 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 292 IDFGLSdfvrpderlNDIVGSAYY------------VAPE-VLHRSYTTEADVWSIGVIAY-ILLCGSRPFWARTESGIF 357
Cdd:cd05093 162 GDFGMS---------RDVYSTDYYrvgghtmlpirwMPPEsIMYRKFTTESDVWSLGVVLWeIFTYGKQPWYQLSNNEVI 232

                ....*.
gi 15230288 358 RAVLKA 363
Cdd:cd05093 233 ECITQG 238
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
143-337 6.31e-11

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: 63.55  E-value: 6.31e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELgeEIGRGHFGYTCSAKFKKgelkDQEVAVKVIPKSKMtsaiSIEDVRREVKILRALSgHQNLVQFYDAFEDNAnVY 222
Cdd:cd05071  12 RLEV--KLGQGCFGEVWMGTWNG----TTRVAIKTLKPGTM----SPEAFLQEAQVMKKLR-HEKLVQLYAVVSEEP-IY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 223 IVMELCGGGELLDRILARGGKYSE-DDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFVR 301
Cdd:cd05071  80 IVTEYMSKGSLLDFLKGEMGKYLRlPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVG---ENLVCKVADFGLARLIE 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 15230288 302 pDERLNDIVGSAY---YVAPEV-LHRSYTTEADVWSIGVI 337
Cdd:cd05071 157 -DNEYTARQGAKFpikWTAPEAaLYGRFTIKSDVWSFGIL 195
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
144-358 6.51e-11

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: 63.37  E-value: 6.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 144 IELGEEIGRGHFGYTCSAKFKKgelkDQEVAVKVIPKSKMtsaiSIEDVRREVKILRALSgHQNLVQFYdAFEDNANVYI 223
Cdd:cd05067   9 LKLVERLGAGQFGEVWMGYYNG----HTKVAIKSLKQGSM----SPDAFLAEANLMKQLQ-HQRLVRLY-AVVTQEPIYI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDRI-LARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFVRP 302
Cdd:cd05067  79 ITEYMENGSLVDFLkTPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVS---DTLSCKIADFGLARLIED 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15230288 303 DERLNDiVGSAY---YVAPEVL-HRSYTTEADVWSIGV-IAYILLCGSRPFWARTESGIFR 358
Cdd:cd05067 156 NEYTAR-EGAKFpikWTAPEAInYGTFTIKSDVWSFGIlLTEIVTHGRIPYPGMTNPEVIQ 215
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
150-348 6.72e-11

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: 62.80  E-value: 6.72e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKKgelkdqEVAVKVIPKSKMTSAiSIEDVRREVKILRALSgHQNLVQFYDAFEDNaNVYIVMELCG 229
Cdd:cd14062   1 IGSGSFGTVYKGRWHG------DVAVKKLNVTDPTPS-QLQAFKNEVAVLRKTR-HVNILLFMGYMTKP-QLAIVTQWCE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 230 GGELLDRILArggkyseDDAKAVLIQILNV-------VAFCHLQGVVHRDLKPEN-FLYtskeENSMLKVIDFGLSDfVR 301
Cdd:cd14062  72 GSSLYKHLHV-------LETKFEMLQLIDIarqtaqgMDYLHAKNIIHRDLKSNNiFLH----EDLTVKIGDFGLAT-VK 139
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15230288 302 P----DERLNDIVGSAYYVAPEVLH----RSYTTEADVWSIGVIAYILLCGSRPF 348
Cdd:cd14062 140 TrwsgSQQFEQPTGSILWMAPEVIRmqdeNPYSFQSDVYAFGIVLYELLTGQLPY 194
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
141-348 8.12e-11

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


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 63.85  E-value: 8.12e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 141 QSRIELGEEIGRGHFGYTCSAKF----KKGELKdqEVAVKVIPKSKMTSAISIedVRREVKILRALSGHQNLVQFYDA-F 215
Cdd:cd05103   6 RDRLKLGKPLGRGAFGQVIEADAfgidKTATCR--TVAVKMLKEGATHSEHRA--LMSELKILIHIGHHLNVVNLLGAcT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 216 EDNANVYIVMELCGGGEL--------------------------------------LDRILARGGKYS------------ 245
Cdd:cd05103  82 KPGGPLMVIVEFCKFGNLsaylrskrsefvpyktkgarfrqgkdyvgdisvdlkrrLDSITSSQSSASsgfveekslsdv 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 246 -------EDDAKAVL---------IQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLS-------DFVRP 302
Cdd:cd05103 162 eeeeagqEDLYKDFLtledlicysFQVAKGMEFLASRKCIHRDLAARNILLS---ENNVVKICDFGLArdiykdpDYVRK 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 15230288 303 -DERLndivgSAYYVAPE-VLHRSYTTEADVWSIGVIAY-ILLCGSRPF 348
Cdd:cd05103 239 gDARL-----PLKWMAPEtIFDRVYTIQSDVWSFGVLLWeIFSLGASPY 282
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
143-348 1.13e-10

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. 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: 62.89  E-value: 1.13e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFGYTCSAK-FKKGELKD-QEVAVKVIPKSkmTSAISIEDVRREVKILRALSGHQNLVQFYDA-FEDNA 219
Cdd:cd05054   8 RLKLGKPLGRGAFGKVIQASaFGIDKSATcRTVAVKMLKEG--ATASEHKALMTELKILIHIGHHLNVVNLLGAcTKPGG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 220 NVYIVMELCGGGEL----------------LDRILARGGKYSEDDAKAVL---------IQILNVVAFCHLQGVVHRDLK 274
Cdd:cd05054  86 PLMVIVEFCKFGNLsnylrskreefvpyrdKGARDVEEEEDDDELYKEPLtledlicysFQVARGMEFLASRKCIHRDLA 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 275 PENFLYTskeENSMLKVIDFGLS-------DFVRP-DERLndivgSAYYVAPE-VLHRSYTTEADVWSIGVIAY-ILLCG 344
Cdd:cd05054 166 ARNILLS---ENNVVKICDFGLArdiykdpDYVRKgDARL-----PLKWMAPEsIFDKVYTTQSDVWSFGVLLWeIFSLG 237

                ....
gi 15230288 345 SRPF 348
Cdd:cd05054 238 ASPY 241
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
148-398 1.20e-10

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: 62.84  E-value: 1.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGytcsaKFKKGELKDQEVAVKVIPKSKMTSAISIEDVRREVkILRalsgHQNLVQFYDAFEDNAN----VYI 223
Cdd:cd13998   1 EVIGKGRFG-----EVWKASLKNEPVAVKIFSSRDKQSWFREKEIYRTP-MLK----HENILQFIAADERDTAlrteLWL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDrILARggkyseddakavliQILNVVAFCHLQG----------------------VVHRDLKPENFLYT 281
Cdd:cd13998  71 VTAFHPNGSL*D-YLSL--------------HTIDWVSLCRLALsvarglahlhseipgctqgkpaIAHRDLKSKNILVK 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 282 SkeeNSMLKVIDFGLSdfVRPDERLNDI-------VGSAYYVAPEVL-------HRSYTTEADVWSIGVIayillcgsrp 347
Cdd:cd13998 136 N---DGTCCIADFGLA--VRLSPSTGEEdnanngqVGTKRYMAPEVLegainlrDFESFKRVDIYAMGLV---------- 200
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 348 FW---ARTESGI---------FRAVLKADPSFDE-----------PPWPS--LSFEAKDFVKRLL----YKDPRKRMTAS 398
Cdd:cd13998 201 LWemaSRCTDLFgiveeykppFYSEVPNHPSFEDmqevvvrdkqrPNIPNrwLSHPGLQSLAETIeecwDHDAEARLTAQ 280
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
148-342 1.31e-10

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: 62.61  E-value: 1.31e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGYTCSAKFK-----KGELkdqeVAVKVIPKSkmTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNAN-- 220
Cdd:cd05080  10 RDLGEGHFGKVSLYCYDptndgTGEM----VAVKALKAD--CGPQHRSGWKQEIDILKTLY-HENIVKYKGCCSEQGGks 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 VYIVMELCGGGELLDRIlargGKYSEDDAKAVLI--QILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLSD 298
Cdd:cd05080  83 LQLIMEYVPLGSLRDYL----PKHSIGLAQLLLFaqQICEGMAYLHSQHYIHRDLAARNVLL---DNDRLVKIGDFGLAK 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15230288 299 FVRPDERL----NDIVGSAYYVAPEVLHR-SYTTEADVWSIGVIAYILL 342
Cdd:cd05080 156 AVPEGHEYyrvrEDGDSPVFWYAPECLKEyKFYYASDVWSFGVTLYELL 204
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
149-403 1.42e-10

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: 61.94  E-value: 1.42e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 149 EIGRGHFgytcsAKFKKGelKDQEVAVKVIPKSKMTSAISIEDVRR---EVKILRALSgHQNLVQFYDAFEDNAN----V 221
Cdd:cd14033   8 EIGRGSF-----KTVYRG--LDTETTVEVAWCELQTRKLSKGERQRfseEVEMLKGLQ-HPNIVRFYDSWKSTVRghkcI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 YIVMELCGGG----------ELLDRILARGGKyseddakavliQILNVVAFCHLQG--VVHRDLKPENFLYTSKeeNSML 289
Cdd:cd14033  80 ILVTELMTSGtlktylkrfrEMKLKLLQRWSR-----------QILKGLHFLHSRCppILHRDLKCDNIFITGP--TGSV 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 290 KVIDFGLSDFVRPdERLNDIVGSAYYVAPEVLHRSYTTEADVWSIGVIAYILLCGSRPFW-ARTESGIFRAV---LKADp 365
Cdd:cd14033 147 KIGDLGLATLKRA-SFAKSVIGTPEFMAPEMYEEKYDEAVDVYAFGMCILEMATSEYPYSeCQNAAQIYRKVtsgIKPD- 224
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 15230288 366 SFDEPPWPslsfEAKDFVKRLLYKDPRKRMTASQALMH 403
Cdd:cd14033 225 SFYKVKVP----ELKEIIEGCIRTDKDERFTIQDLLEH 258
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
148-369 1.87e-10

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: 61.90  E-value: 1.87e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 148 EEIGRGHFGytcsaKFKKGELKDQEVAVKVIPKSKMTSAisiedvRREVKI-----LRalsgHQNLVQFYDAfeDNAN-- 220
Cdd:cd14056   1 KTIGKGRYG-----EVWLGKYRGEKVAVKIFSSRDEDSW------FRETEIyqtvmLR----HENILGFIAA--DIKStg 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 ----VYIVMELCGGGELLDRILARggKYSEDDAKAVLIQILNVVAFCHLQ--------GVVHRDLKPENFLYtskeENSM 288
Cdd:cd14056  64 swtqLWLITEYHEHGSLYDYLQRN--TLDTEEALRLAYSAASGLAHLHTEivgtqgkpAIAHRDLKSKNILV----KRDG 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 289 LKVI-DFGLSdfVRPDERLNDI-------VGSAYYVAPEVLHRSYTTE-------ADVWSIGVIAYILLCgsrpfwaRTE 353
Cdd:cd14056 138 TCCIaDLGLA--VRYDSDTNTIdippnprVGTKRYMAPEVLDDSINPKsfesfkmADIYSFGLVLWEIAR-------RCE 208
                       250       260
                ....*....|....*....|....
gi 15230288 354 SGI--------FRAVLKADPSFDE 369
Cdd:cd14056 209 IGGiaeeyqlpYFGMVPSDPSFEE 232
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
150-348 3.71e-10

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: 60.97  E-value: 3.71e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGytcsaKFKKGELKD-QEVAVK-VIPKSKMTSAISIEdvrREVKILRALSgHQNLVQ---FYDAFEDNANVYIV 224
Cdd:cd14664   1 IGRGGAG-----TVYKGVMPNgTLVAVKrLKGEGTQGGDHGFQ---AEIQTLGMIR-HRNIVRlrgYCSNPTTNLLVYEY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 225 MELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCH---LQGVVHRDLKPENFLYTSKEEnsmLKVIDFGLSDFVR 301
Cdd:cd14664  72 MPNGSLGELLHSRPESQPPLDWETRQRIALGSARGLAYLHhdcSPLIIHRDVKSNNILLDEEFE---AHVADFGLAKLMD 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15230288 302 PD--ERLNDIVGSAYYVAPEVLHRSYTTE-ADVWSIGVIAYILLCGSRPF 348
Cdd:cd14664 149 DKdsHVMSSVAGSYGYIAPEYAYTGKVSEkSDVYSYGVVLLELITGKRPF 198
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
144-349 4.07e-10

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: 60.85  E-value: 4.07e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 144 IELGEEIGRGHFGytcsaKFKKGEL---KDQEVAVKVIPKSKMTSAISI--EDVRREVKILRALSgHQNLVQFYDAFEDN 218
Cdd:cd05048   7 VRFLEELGEGAFG-----KVYKGELlgpSSEESAISVAIKTLKENASPKtqQDFRREAELMSDLQ-HPNIVCLLGVCTKE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 219 ANVYIVMELCGGGELLDRILAR------GGKYSEDDAKAVL---------IQILNVVAFCHLQGVVHRDLKPENFLYTsk 283
Cdd:cd05048  81 QPQCMLFEYMAHGDLHEFLVRHsphsdvGVSSDDDGTASSLdqsdflhiaIQIAAGMEYLSSHHYVHRDLAARNCLVG-- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 284 eENSMLKVIDFGLSdfvrpderlNDIVGSAYY------------VAPE-VLHRSYTTEADVWSIGVIAY-ILLCGSRPFW 349
Cdd:cd05048 159 -DGLTVKISDFGLS---------RDIYSSDYYrvqsksllpvrwMPPEaILYGKFTTESDVWSFGVVLWeIFSYGLQPYY 228
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
219-348 5.08e-10

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: 60.74  E-value: 5.08e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 219 ANVYIVMELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSD 298
Cdd:cd05111  81 ASLQLVTQLLPLGSLLDHVRQHRGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKS---PSQVQVADFGVAD 157
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15230288 299 FVRPDER---LNDIVGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLC-GSRPF 348
Cdd:cd05111 158 LLYPDDKkyfYSEAKTPIKWMALESIHfGKYTHQSDVWSYGVTVWEMMTfGAEPY 212
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
142-352 7.24e-10

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: 60.40  E-value: 7.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 142 SRIELGEEIGRGHFGYTCSAKFKKGELKdQEVAVKvipksKMTSAISIEDVRR---EVKILRALSGHQNLVQFYDAFEDN 218
Cdd:cd05088   7 NDIKFQDVIGEGNFGQVLKARIKKDGLR-MDAAIK-----RMKEYASKDDHRDfagELEVLCKLGHHPNIINLLGACEHR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 219 ANVYIVMELCGGGELLD-----RILARGGKYSEDDAKAVLIQILNVVAFC----------HLQGVVHRDLKPENFLYTsk 283
Cdd:cd05088  81 GYLYLAIEYAPHGNLLDflrksRVLETDPAFAIANSTASTLSSQQLLHFAadvargmdylSQKQFIHRDLAARNILVG-- 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15230288 284 eENSMLKVIDFGLSdfvRPDE-RLNDIVGS--AYYVAPEVLHRS-YTTEADVWSIGVIAY-ILLCGSRPFWART 352
Cdd:cd05088 159 -ENYVAKIADFGLS---RGQEvYVKKTMGRlpVRWMAIESLNYSvYTTNSDVWSYGVLLWeIVSLGGTPYCGMT 228
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
150-342 7.59e-10

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: 60.29  E-value: 7.59e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 150 IGRGHFGYTCSAKFKK-GELKDQEVAVKvipKSKMTSAISIEDVRREVKILRALsgHQNLVQFYDAFEDNA---NVYIVM 225
Cdd:cd05081  12 LGKGNFGSVELCRYDPlGDNTGALVAVK---QLQHSGPDQQRDFQREIQILKAL--HSDFIVKYRGVSYGPgrrSLRLVM 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 226 ELCGGGELLDRILARGGKYsedDAKAVLI---QILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsmLKVIDFGLSDFVrP 302
Cdd:cd05081  87 EYLPSGCLRDFLQRHRARL---DASRLLLyssQICKGMEYLGSRRCVHRDLAARNILVESEAH---VKIADFGLAKLL-P 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15230288 303 DERLNDIV-----GSAYYVAPEVLHRS-YTTEADVWSIGVIAYILL 342
Cdd:cd05081 160 LDKDYYVVrepgqSPIFWYAPESLSDNiFSRQSDVWSFGVVLYELF 205
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
133-348 8.11e-10

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


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 60.79  E-value: 8.11e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 133 RFGFSKElqsRIELGEEIGRGHFGYTCSAK---FKKGELKdQEVAVKVIPKSkmTSAISIEDVRREVKILRALSGHQNLV 209
Cdd:cd14207   1 KWEFARE---RLKLGKSLGRGAFGKVVQASafgIKKSPTC-RVVAVKMLKEG--ATASEYKALMTELKILIHIGHHLNVV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 210 QFYDAFEDNAN-VYIVMELCGGGELLDRILAR--------------------------GGK-----------------YS 245
Cdd:cd14207  75 NLLGACTKSGGpLMVIVEYCKYGNLSNYLKSKrdffvtnkdtslqeelikekkeaeptGGKkkrlesvtssesfassgFQ 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 246 ED------------------------DAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLS---- 297
Cdd:cd14207 155 EDkslsdveeeeedsgdfykrpltmeDLISYSFQVARGMEFLSSRKCIHRDLAARNILLS---ENNVVKICDFGLArdiy 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15230288 298 ---DFVRP-DERLndivgSAYYVAPE-VLHRSYTTEADVWSIGVIAY-ILLCGSRPF 348
Cdd:cd14207 232 knpDYVRKgDARL-----PLKWMAPEsIFDKIYSTKSDVWSYGVLLWeIFSLGASPY 283
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
157-363 9.11e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 61.01  E-value: 9.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  157 YTCSakfKKGELKDQEVAVKVIPKSKmtsaisieDVRREVKILRALSgHQNLVQFYDAFEDNANVYIVMEL--CGGGELL 234
Cdd:PHA03207 109 FVCT---KHGDEQRKKVIVKAVTGGK--------TPGREIDILKTIS-HRAIINLIHAYRWKSTVCMVMPKykCDLFTYV 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  235 DRIlargGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENfLYTSKEENSMLKviDFGLSdfVRPDERLND-----I 309
Cdd:PHA03207 177 DRS----GPLPLEQAITIQRRLLEALAYLHGRGIIHRDVKTEN-IFLDEPENAVLG--DFGAA--CKLDAHPDTpqcygW 247
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15230288  310 VGSAYYVAPEVLH-RSYTTEADVWSIGVIAYILLCGSRPFWAR---TESGIFRAVLKA 363
Cdd:PHA03207 248 SGTLETNSPELLAlDPYCAKTDIWSAGLVLFEMSVKNVTLFGKqvkSSSSQLRSIIRC 305
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
149-407 9.55e-10

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 59.71  E-value: 9.55e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 149 EIGRGHFgytcsAKFKKGelKDQEVAVKV----IPKSKMTSaISIEDVRREVKILRALSgHQNLVQFYDAFEDNAN---- 220
Cdd:cd14032   8 ELGRGSF-----KTVYKG--LDTETWVEVawceLQDRKLTK-VERQRFKEEAEMLKGLQ-HPNIVRFYDFWESCAKgkrc 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 VYIVMELCGGGELlDRILARGGKYSEDDAKAVLIQILNVVAFCHLQG--VVHRDLKPENFLYTSKeeNSMLKVIDFGLSD 298
Cdd:cd14032  79 IVLVTELMTSGTL-KTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITGP--TGSVKIGDLGLAT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 299 FVRPdERLNDIVGSAYYVAPEVLHRSYTTEADVWSIGVIAYILLCGSRPFW-ARTESGIFRAVLKA--DPSFDEPPWPsl 375
Cdd:cd14032 156 LKRA-SFAKSVIGTPEFMAPEMYEEHYDESVDVYAFGMCMLEMATSEYPYSeCQNAAQIYRKVTCGikPASFEKVTDP-- 232
                       250       260       270
                ....*....|....*....|....*....|..
gi 15230288 376 sfEAKDFVKRLLYKDPRKRMTASQALMHPWIA 407
Cdd:cd14032 233 --EIKEIIGECICKNKEERYEIKDLLSHAFFA 262
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
145-342 9.73e-10

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: 60.43  E-value: 9.73e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAkFKKGelKDQEVAVKVI---PKSKMTSAIsiedvrrEVKILRALSGHQ----NLVQFYDAFED 217
Cdd:cd14229   3 EVLDFLGRGTFGQVVKC-WKRG--TNEIVAVKILknhPSYARQGQI-------EVGILARLSNENadefNFVRAYECFQH 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 218 NANVYIVMELCGGgELLDriLARGGKYSEDDAK---AVLIQILNVVAFCHLQGVVHRDLKPENFLYTSK-EENSMLKVID 293
Cdd:cd14229  73 RNHTCLVFEMLEQ-NLYD--FLKQNKFSPLPLKvirPILQQVATALKKLKSLGLIHADLKPENIMLVDPvRQPYRVKVID 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15230288 294 FGLSDFVRpDERLNDIVGSAYYVAPEV-LHRSYTTEADVWSIG-VIAYILL 342
Cdd:cd14229 150 FGSASHVS-KTVCSTYLQSRYYRAPEIiLGLPFCEAIDMWSLGcVIAELFL 199
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
145-342 1.07e-09

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: 60.15  E-value: 1.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAkFKKGelKDQEVAVKVIpKSKMTSAISIEDvrrEVKILRALSGHQ----NLVQFYDAFEDNAN 220
Cdd:cd14211   2 EVLEFLGRGTFGQVVKC-WKRG--TNEIVAIKIL-KNHPSYARQGQI---EVSILSRLSQENadefNFVRAYECFQHKNH 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 VYIVMELcgggelLDRIL---ARGGKYSEDDAK---AVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSM-LKVID 293
Cdd:cd14211  75 TCLVFEM------LEQNLydfLKQNKFSPLPLKyirPILQQVLTALLKLKSLGLIHADLKPENIMLVDPVRQPYrVKVID 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15230288 294 FGLSDFVRpDERLNDIVGSAYYVAPEVLHRSYTTEA-DVWSIG-VIAYILL 342
Cdd:cd14211 149 FGSASHVS-KAVCSTYLQSRYYRAPEIILGLPFCEAiDMWSLGcVIAELFL 198
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
149-348 1.41e-09

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: 59.19  E-value: 1.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 149 EIGRGHFGYTCSAKFKKgELKDQEVAVKVIpKSKMTSAISiEDVRREVKILRALSgHQNLVQFYDAFEDNAnVYIVMELC 228
Cdd:cd05115  11 ELGSGNFGCVKKGVYKM-RKKQIDVAIKVL-KQGNEKAVR-DEMMREAQIMHQLD-NPYIVRMIGVCEAEA-LMLVMEMA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 229 GGGELlDRILarGGKYSEddakavlIQILNVVAFCH--------LQG--VVHRDLKPENFLYTSKEensMLKVIDFGLSD 298
Cdd:cd05115  86 SGGPL-NKFL--SGKKDE-------ITVSNVVELMHqvsmgmkyLEEknFVHRDLAARNVLLVNQH---YAKISDFGLSK 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15230288 299 FVRPDErlndivgsAYY------------VAPEVLH-RSYTTEADVWSIGVIAYILLC-GSRPF 348
Cdd:cd05115 153 ALGADD--------SYYkarsagkwplkwYAPECINfRKFSSRSDVWSYGVTMWEAFSyGQKPY 208
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
194-343 1.98e-09

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: 58.67  E-value: 1.98e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 194 REVKILRALSgHQNLVQFYDAFEDNANVYIVMELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDL 273
Cdd:cd14154  39 KEVKVMRSLD-HPNVLKFIGVLYKDKKLNLITEYIPGGTLKDVLKDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDL 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 274 KPENFLYtsKEENSMLkVIDFGLSDFVRpDERLND----------------------IVGSAYYVAPEVLH-RSYTTEAD 330
Cdd:cd14154 118 NSHNCLV--REDKTVV-VADFGLARLIV-EERLPSgnmspsetlrhlkspdrkkrytVVGNPYWMAPEMLNgRSYDEKVD 193
                       170
                ....*....|...
gi 15230288 331 VWSIGviayILLC 343
Cdd:cd14154 194 IFSFG----IVLC 202
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
149-339 2.30e-09

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: 58.44  E-value: 2.30e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 149 EIGRGHFGYTCSA--KFKKGElkdQEVAVKVIPKSKMTSAISiEDVRREVKILRALSgHQNLVQFYDAFEDNaNVYIVME 226
Cdd:cd05116   2 ELGSGNFGTVKKGyyQMKKVV---KTVAVKILKNEANDPALK-DELLREANVMQQLD-NPYIVRMIGICEAE-SWMLVME 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 227 LCGGGELlDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEensMLKVIDFGLSDFVRPDERL 306
Cdd:cd05116  76 MAELGPL-NKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQH---YAKISDFGLSKALRADENY 151
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 15230288 307 NDIVGSAYY----VAPEVL-HRSYTTEADVWSIGVIAY 339
Cdd:cd05116 152 YKAQTHGKWpvkwYAPECMnYYKFSSKSDVWSFGVLMW 189
STKc_CK1_fungal cd14127
Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 1; ...
143-348 3.50e-09

Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 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. This subfamily is composed of fungal CK1 homolog 1 proteins, also called Yck1 in Saccharomyces cerevisiae and Cki1 in Schizosaccharomyces pombe. Yck1 (or Yck1p) and Cki1 are plasma membrane-anchored proteins. Yck1 phosphorylates and regulates Khd1p, a RNA-binding protein that represses translation of bud-localized mRNA. Cki1 phosphorylates and regulates phosphatidylinositol (PI)-(4)P-5-kinase, which catalyzes the last step in the sythesis of PI(4,5)P2, which is involved in actin cytoskeleton remodeling and membrane traffic. The fungal 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: 271029 [Multi-domain]  Cd Length: 277  Bit Score: 58.27  E-value: 3.50e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFGytcsAKFKKGE-LKDQEVAVKVIPKSkmTSAISIEDVRREVKILRALSGHQNLvqFYDAFEDNANV 221
Cdd:cd14127   1 HYKVGKKIGEGSFG----VIFEGTNlLNGQQVAIKFEPRK--SDAPQLRDEYRTYKLLAGCPGIPNV--YYFGQEGLHNI 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 222 yIVMELCGGgELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLY---TSKEENsMLKVIDFGLSD 298
Cdd:cd14127  73 -LVIDLLGP-SLEDLFDLCGRKFSVKTVVMVAKQMLTRVQTIHEKNLIYRDIKPDNFLIgrpGTKNAN-VIHVVDFGMAK 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15230288 299 FVR--------PDERLNDIVGSAYYVAPEV-LHRSYTTEADVWSIGVIAYILLCGSRPF 348
Cdd:cd14127 150 QYRdpktkqhiPYREKKSLSGTARYMSINThLGREQSRRDDLEALGHVFMYFLRGSLPW 208
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
194-343 3.53e-09

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: 58.03  E-value: 3.53e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 194 REVKILRALSgHQNLVQFYDAFEDNANVYIVMELCGGGELLDRIlaRGGKYSEDDAKAVLIQ-ILNVVAFCHLQGVVHRD 272
Cdd:cd14222  39 TEVKVMRSLD-HPNVLKFIGVLYKDKRLNLLTEFIEGGTLKDFL--RADDPFPWQQKVSFAKgIASGMAYLHSMSIIHRD 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 273 LKPENFLYtsKEENSMLkVIDFGLSDFVRPDE---------------RLND------IVGSAYYVAPEVLH-RSYTTEAD 330
Cdd:cd14222 116 LNSHNCLI--KLDKTVV-VADFGLSRLIVEEKkkpppdkpttkkrtlRKNDrkkrytVVGNPYWMAPEMLNgKSYDEKVD 192
                       170
                ....*....|...
gi 15230288 331 VWSIGviayILLC 343
Cdd:cd14222 193 IFSFG----IVLC 201
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
188-399 3.88e-09

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-2D is allso called Retinal Guanylyl Cyclase 1 (RETGC-1) or Rod Outer Segment membrane Guanylate Cyclase (ROS-GC). It is found in the photoreceptors of the retina where it anchors the reciprocal feedback loop between calcium and cGMP, which regulates the dark, light, and recovery phases in phototransduction. It is also found in other sensory neurons and may be a universal transduction component that plays a role in the perception of all senses. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-2D subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270945 [Multi-domain]  Cd Length: 267  Bit Score: 57.80  E-value: 3.88e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 188 SIEDVRREVKILRalsgHQNLVQFYDAFEDNANVYIVMELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQG 267
Cdd:cd14043  42 STKNVFSKLRELR----HENVNLFLGLFVDCGILAIVSEHCSRGSLEDLLRNDDMKLDWMFKSSLLLDLIKGMRYLHHRG 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 268 VVHRDLKPENFLYTSKeenSMLKVIDFGLSDFV------RPDERLNDIvgsaYYVAPEVLH-----RSYTTEADVWSIGV 336
Cdd:cd14043 118 IVHGRLKSRNCVVDGR---FVLKITDYGYNEILeaqnlpLPEPAPEEL----LWTAPELLRdprleRRGTFPGDVFSFAI 190
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15230288 337 IAYILLCGSRPF--WARTESGIFRAVLKADP------SFDEPPWpslsfEAKDFVKRLLYKDPRKRMTASQ 399
Cdd:cd14043 191 IMQEVIVRGAPYcmLGLSPEEIIEKVRSPPPlcrpsvSMDQAPL-----ECIQLMKQCWSEAPERRPTFDQ 256
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
219-348 5.88e-09

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 57.34  E-value: 5.88e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 219 ANVYIVMELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsmLKVIDFGLSD 298
Cdd:cd05109  81 STVQLVTQLMPYGCLLDYVRENKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNH---VKITDFGLAR 157
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15230288 299 FVRPDERLNDIVGSAY---YVAPE-VLHRSYTTEADVWSIGVIAYILLC-GSRPF 348
Cdd:cd05109 158 LLDIDETEYHADGGKVpikWMALEsILHRRFTHQSDVWSYGVTVWELMTfGAKPY 212
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
144-346 5.93e-09

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: 57.39  E-value: 5.93e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 144 IELGEEIGRGHFGYTCSAKFKKgelkDQEVAVKVIPKSKMtsaiSIEDVRREVKILRALSgHQNLVQFYdAFEDNANVYI 223
Cdd:cd05070  11 LQLIKRLGNGQFGEVWMGTWNG----NTKVAIKTLKPGTM----SPESFLEEAQIMKKLK-HDKLVQLY-AVVSEEPIYI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDRIL-ARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSkeeNSMLKVIDFGLSDFVRp 302
Cdd:cd05070  81 VTEYMSKGSLLDFLKdGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGN---GLICKIADFGLARLIE- 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15230288 303 DERLNDIVGSAY---YVAPEV-LHRSYTTEADVWSIGVIAYILLCGSR 346
Cdd:cd05070 157 DNEYTARQGAKFpikWTAPEAaLYGRFTIKSDVWSFGILLTELVTKGR 204
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
240-342 7.33e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 57.96  E-value: 7.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  240 RGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYtskEENSMLKVIDFGLSDFVRPDERLNDIVGSAYYVAPE 319
Cdd:PHA03209 150 RSRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFI---NDVDQVCIGDLGAAQFPVVAPAFLGLAGTVETNAPE 226
                         90       100
                 ....*....|....*....|....
gi 15230288  320 VLHRS-YTTEADVWSIGVIAYILL 342
Cdd:PHA03209 227 VLARDkYNSKADIWSAGIVLFEML 250
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
254-371 7.54e-09

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: 57.34  E-value: 7.54e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 254 IQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsmLKVIDFGLSDFVRPDERLNDIVGSAY---YVAPE-VLHRSYTTEA 329
Cdd:cd05108 116 VQIAKGMNYLEDRRLVHRDLAARNVLVKTPQH---VKITDFGLAKLLGAEEKEYHAEGGKVpikWMALEsILHRIYTHQS 192
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15230288 330 DVWSIGVIAYILLC-GSRPFWARTESGIfRAVLKADPSFDEPP 371
Cdd:cd05108 193 DVWSYGVTVWELMTfGSKPYDGIPASEI-SSILEKGERLPQPP 234
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
145-425 9.25e-09

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: 57.30  E-value: 9.25e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAKFKKgeLKDQE-VAVKvipKSKMTSAISiEDVRR---EVKILRALSgHQNLVQFYDAFEDNAN 220
Cdd:cd08216   1 ELLYEIGKCFKGGGVVHLAKH--KPTNTlVAVK---KINLESDSK-EDLKFlqqEILTSRQLQ-HPNILPYVTSFVVDND 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 VYIVMELCGGG---ELLDRILARGgkYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEensmlKVIDFGLS 297
Cdd:cd08216  74 LYVVTPLMAYGscrDLLKTHFPEG--LPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDG-----KVVLSGLR 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 298 D---FVRPDERLN-------DIVGSAYYVAPEVLHRS---YTTEADVWSIGVIAYILLCGSRPF---------------- 348
Cdd:cd08216 147 YaysMVKHGKRQRvvhdfpkSSEKNLPWLSPEVLQQNllgYNEKSDIYSVGITACELANGVVPFsdmpatqmllekvrgt 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 349 ----WART-------------ESGIFRAVlkADPSFDEPPWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWiagykk 411
Cdd:cd08216 227 tpqlLDCStypleedsmsqseDSSTEHPN--NRDTRDIPYQRTFSEAFHQFVELCLQRDPELRPSASQLLAHSF------ 298
                       330
                ....*....|....
gi 15230288 412 idipfdiliFKQIK 425
Cdd:cd08216 299 ---------FKQCR 303
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
141-399 1.12e-08

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: 57.22  E-value: 1.12e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 141 QSRIELGEEIGRGHFGYTCSAKfKKGELKDQE---VAVKVI-PKSKMTSAisiEDVRREVKILRALSGHQNLVQFYDAFE 216
Cdd:cd05104  34 RDRLRFGKTLGAGAFGKVVEAT-AYGLAKADSamtVAVKMLkPSAHSTER---EALMSELKVLSYLGNHINIVNLLGACT 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 217 DNANVYIVMELCGGGELLD---------------------------------------------------------RILA 239
Cdd:cd05104 110 VGGPTLVITEYCCYGDLLNflrrkrdsficpkfedlaeaalyrnllhqremacdslneymdmkpsvsyvvptkadkRRGV 189
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 240 RGGKYSEDDAKAVLI-----------------QILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLSDFVRP 302
Cdd:cd05104 190 RSGSYVDQDVTSEILeedelaldtedllsfsyQVAKGMEFLASKNCIHRDLAARNILLT---HGRITKICDFGLARDIRN 266
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 303 DErlNDIV-GSAY----YVAPE-VLHRSYTTEADVWSIGVIAY-ILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSL 375
Cdd:cd05104 267 DS--NYVVkGNARlpvkWMAPEsIFECVYTFESDVWSYGILLWeIFSLGSSPYPGMPVDSKFYKMIKEGYRMDSPEFAPS 344
                       330       340
                ....*....|....*....|....
gi 15230288 376 sfEAKDFVKRLLYKDPRKRMTASQ 399
Cdd:cd05104 345 --EMYDIMRSCWDADPLKRPTFKQ 366
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
144-352 1.60e-08

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: 56.38  E-value: 1.60e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 144 IELGEEIGRGHFGYTCSAKfKKGELKDQE---VAVKVIPKSkmTSAISIEDVRREVKILRALSgHQNLVQFYDAFEDNAN 220
Cdd:cd05050   7 IEYVRDIGQGAFGRVFQAR-APGLLPYEPftmVAVKMLKEE--ASADMQADFQREAALMAEFD-HPNIVKLLGVCAVGKP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 VYIVMELCGGGEL--------------LDRILARGGKYSED-------DAKAVLIQILNVVAFCHLQGVVHRDLKPENFL 279
Cdd:cd05050  83 MCLLFEYMAYGDLneflrhrspraqcsLSHSTSSARKCGLNplplsctEQLCIAKQVAAGMAYLSERKFVHRDLATRNCL 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 280 YTskeENSMLKVIDFGLS------DFVRPDErlNDIVgSAYYVAPE-VLHRSYTTEADVWSIGVIAY-ILLCGSRPFWAR 351
Cdd:cd05050 163 VG---ENMVVKIADFGLSrniysaDYYKASE--NDAI-PIRWMPPEsIFYNRYTTESDVWAYGVVLWeIFSYGMQPYYGM 236

                .
gi 15230288 352 T 352
Cdd:cd05050 237 A 237
pknD PRK13184
serine/threonine-protein kinase PknD;
252-401 1.75e-08

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 57.47  E-value: 1.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  252 VLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEEnsmLKVIDFGLSDFVRPDE-------------------RLNDIVGS 312
Cdd:PRK13184 118 IFHKICATIEYVHSKGVLHRDLKPDNILLGLFGE---VVILDWGAAIFKKLEEedlldidvdernicyssmtIPGKIVGT 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  313 AYYVAPEVLHRSYTTEA-DVWSIGVIAYILLCGSRPFwaRTESG---IFRAVLkADPS----FDEPPwPSLSfeakDFVK 384
Cdd:PRK13184 195 PDYMAPERLLGVPASEStDIYALGVILYQMLTLSFPY--RRKKGrkiSYRDVI-LSPIevapYREIP-PFLS----QIAM 266
                        170
                 ....*....|....*..
gi 15230288  385 RLLYKDPRKRMTASQAL 401
Cdd:PRK13184 267 KALAVDPAERYSSVQEL 283
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
149-403 2.76e-08

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


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 55.44  E-value: 2.76e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 149 EIGRGHFgytcsAKFKKGelKDQEVAVKV----IPKSKMTSAiSIEDVRREVKILRALSgHQNLVQFYDAFEDNAN---- 220
Cdd:cd14030  32 EIGRGSF-----KTVYKG--LDTETTVEVawceLQDRKLSKS-ERQRFKEEAGMLKGLQ-HPNIVRFYDSWESTVKgkkc 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 221 VYIVMELCGGGELlDRILARGGKYSEDDAKAVLIQILNVVAFCHLQG--VVHRDLKPENFLYTSKeeNSMLKVIDFGLSD 298
Cdd:cd14030 103 IVLVTELMTSGTL-KTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGP--TGSVKIGDLGLAT 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 299 FVRPdERLNDIVGSAYYVAPEVLHRSYTTEADVWSIGVIAYILLCGSRPFW-ARTESGIFRAVLKA--DPSFDEPPWPsl 375
Cdd:cd14030 180 LKRA-SFAKSVIGTPEFMAPEMYEEKYDESVDVYAFGMCMLEMATSEYPYSeCQNAAQIYRRVTSGvkPASFDKVAIP-- 256
                       250       260
                ....*....|....*....|....*...
gi 15230288 376 sfEAKDFVKRLLYKDPRKRMTASQALMH 403
Cdd:cd14030 257 --EVKEIIEGCIRQNKDERYAIKDLLNH 282
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
138-348 3.53e-08

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: 55.02  E-value: 3.53e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 138 KELQ-SRIELGEEIGRGHFGytcsaKFKKGEL-------KDQEVAVKVIpKSKMTSAISiEDVRREVkILRALSGHQNLV 209
Cdd:cd05091   1 KEINlSAVRFMEELGEDRFG-----KVYKGHLfgtapgeQTQAVAIKTL-KDKAEGPLR-EEFRHEA-MLRSRLQHPNIV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 210 QFYDAFEDNANVYIVMELCGGGELLDRILARGGKY---SEDDAKAV------------LIQILNVVAFCHLQGVVHRDLK 274
Cdd:cd05091  73 CLLGVVTKEQPMSMIFSYCSHGDLHEFLVMRSPHSdvgSTDDDKTVkstlepadflhiVTQIAAGMEYLSSHHVVHKDLA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 275 PENFLYTSKEEnsmLKVIDFGLsdfvrpderLNDIVGSAYY------------VAPE-VLHRSYTTEADVWSIGVIAY-I 340
Cdd:cd05091 153 TRNVLVFDKLN---VKISDLGL---------FREVYAADYYklmgnsllpirwMSPEaIMYGKFSIDSDIWSYGVVLWeV 220

                ....*...
gi 15230288 341 LLCGSRPF 348
Cdd:cd05091 221 FSYGLQPY 228
PLN03225 PLN03225
Serine/threonine-protein kinase SNT7; Provisional
146-408 4.08e-08

Serine/threonine-protein kinase SNT7; Provisional


Pssm-ID: 215638 [Multi-domain]  Cd Length: 566  Bit Score: 55.95  E-value: 4.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  146 LGEEIGRGHFGYTCSAKFKKGELKDQEVAVkvIPKSKMTSAISI---EDVRREV--KILRALSGHQNLVQFYDA------ 214
Cdd:PLN03225 136 LGKKLGEGAFGVVYKASLVNKQSKKEGKYV--LKKATEYGAVEIwmnERVRRACpnSCADFVYGFLEPVSSKKEdeywlv 213
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  215 --FEDNANVYIVME-----------LCGGGELLDRILARGGKYseddAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYT 281
Cdd:PLN03225 214 wrYEGESTLADLMQskefpynvepyLLGKVQDLPKGLERENKI----IQTIMRQILFALDGLHSTGIVHRDVKPQNIIFS 289
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  282 skEENSMLKVIDFGLSDFVR------PDERLNDivgsAYYVAPE-VLHRSYTTEA----------------------DVW 332
Cdd:PLN03225 290 --EGSGSFKIIDLGAAADLRvginyiPKEFLLD----PRYAAPEqYIMSTQTPSApsapvatalspvlwqlnlpdrfDIY 363
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288  333 SIGVIaYILLCGSRpfwARTESGI--FRAVLKaDPSFDEPPWPSL-----------SFEAKD--------FVKRLLYKDP 391
Cdd:PLN03225 364 SAGLI-FLQMAFPN---LRSDSNLiqFNRQLK-RNDYDLVAWRKLvepraspdlrrGFEVLDldggagweLLKSMMRFKG 438
                        330
                 ....*....|....*..
gi 15230288  392 RKRMTASQALMHPWIAG 408
Cdd:PLN03225 439 RQRISAKAALAHPYFDR 455
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
149-339 4.18e-08

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: 55.05  E-value: 4.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 149 EIGRGHFGytcsaKFKKGELKDQEVAVKVIPKSKMTSAIsiedvrREVKILRA-LSGHQNLVQFYDA----FEDNANVYI 223
Cdd:cd14220   2 QIGKGRYG-----EVWMGKWRGEKVAVKVFFTTEEASWF------RETEIYQTvLMRHENILGFIAAdikgTGSWTQLYL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 224 VMELCGGGELLDRIlarggKYSEDDAKAVL-IQILNVVAFCHL-------QG---VVHRDLKPENFLYtskEENSMLKVI 292
Cdd:cd14220  71 ITDYHENGSLYDFL-----KCTTLDTRALLkLAYSAACGLCHLhteiygtQGkpaIAHRDLKSKNILI---KKNGTCCIA 142
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15230288 293 DFGL-----SDFVRPDERLNDIVGSAYYVAPEVLHRSYTTE-------ADVWSIGVIAY 339
Cdd:cd14220 143 DLGLavkfnSDTNEVDVPLNTRVGTKRYMAPEVLDESLNKNhfqayimADIYSFGLIIW 201
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
245-348 4.23e-08

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: 55.79  E-value: 4.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 245 SEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTskeENSMLKVIDFGLS-DFVRPDERLNDivGSAY----YVAPE 319
Cdd:cd05107 237 SYMDLVGFSYQVANGMEFLASKNCVHRDLAARNVLIC---EGKLVKICDFGLArDIMRDSNYISK--GSTFlplkWMAPE 311
                        90       100       110
                ....*....|....*....|....*....|.
gi 15230288 320 -VLHRSYTTEADVWSIGVIAY-ILLCGSRPF 348
Cdd:cd05107 312 sIFNNLYTTLSDVWSFGILLWeIFTLGGTPY 342
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
143-297 5.73e-08

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; 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. The delta and epsilon isoforms of CK1 play important roles in circadian rhythm and cell growth. They phosphorylate PERIOD proteins (PER1-3), which are circadian clock proteins that fulfill negative regulatory functions. PER phosphorylation leads to its degradation. However, CRY proteins form a complex with PER and CK1delta/epsilon that protects PER from degradation and leads to nuclear accummulation of the complex, which inhibits BMAL1-CLOCK dependent transcription activation. CK1delta/epsilon also phosphorylate the tumor suppressor p53 and the cellular oncogene Mdm2, which are key regulators of cell growth, genome integrity, and the development of cancer. This subfamily also includes the CK1 fungal proteins Saccharomyces cerevisiae HRR25 and Schizosaccharomyces pombe HHP1. These fungal proteins are involved in DNA repair. The CK1 delta/epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271027 [Multi-domain]  Cd Length: 275  Bit Score: 54.30  E-value: 5.73e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 143 RIELGEEIGRGHFG--YTcSAKFKKGElkdqEVAVKvipkskmtsaisIEDVRR-------EVKILRALSGHQNL--VQF 211
Cdd:cd14125   1 KYRLGRKIGSGSFGdiYL-GTNIQTGE----EVAIK------------LESVKTkhpqllyESKLYKILQGGVGIpnVRW 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 212 YdAFEDNANVyIVMELCGGgELLDRILARGGKYSeddAKAVLI---QILNVVAFCHLQGVVHRDLKPENFLYTSKEENSM 288
Cdd:cd14125  64 Y-GVEGDYNV-MVMDLLGP-SLEDLFNFCSRKFS---LKTVLMladQMISRIEYVHSKNFIHRDIKPDNFLMGLGKKGNL 137

                ....*....
gi 15230288 289 LKVIDFGLS 297
Cdd:cd14125 138 VYIIDFGLA 146
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
144-397 5.90e-08

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: 54.75  E-value: 5.90e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 144 IELGEEIGRGHFGytcsaKFKKGELKDQEVAVKVIpkskmtSAISIEDVRREVKILRA-LSGHQNLVQFY--DAFEDNA- 219
Cdd:cd14142   7 ITLVECIGKGRYG-----EVWRGQWQGESVAVKIF------SSRDEKSWFRETEIYNTvLLRHENILGFIasDMTSRNSc 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 220 -NVYIVMELCGGGELLDRIlargGKYSEDDAKAVLIQILNVVAFCHL-------QG---VVHRDLKPENFLYTSkeeNSM 288
Cdd:cd14142  76 tQLWLITHYHENGSLYDYL----QRTTLDHQEMLRLALSAASGLVHLhteifgtQGkpaIAHRDLKSKNILVKS---NGQ 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 289 LKVIDFGLSDFVRPDERLNDI-----VGSAYYVAPEVLHRSYTTE-------ADVWSIGVIayillcgsrpFWA---RTE 353
Cdd:cd14142 149 CCIADLGLAVTHSQETNQLDVgnnprVGTKRYMAPEVLDETINTDcfesykrVDIYAFGLV----------LWEvarRCV 218
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 354 S-GI-------FRAVLKADPSFDE-----------P--P--W---PSLSFEAKdFVKRLLYKDPRKRMTA 397
Cdd:cd14142 219 SgGIveeykppFYDVVPSDPSFEDmrkvvcvdqqrPniPnrWssdPTLTAMAK-LMKECWYQNPSARLTA 287
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
145-342 8.30e-08

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


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 54.71  E-value: 8.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 145 ELGEEIGRGHFGYTCSAkFKKGelKDQEVAVKVI---PKSKMTSAIsiedvrrEVKILRALSGHQ----NLVQFYDAFED 217
Cdd:cd14227  18 EVLEFLGRGTFGQVVKC-WKRG--TNEIVAIKILknhPSYARQGQI-------EVSILARLSTESaddyNFVRAYECFQH 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 218 NANVYIVMELCGGgELLDriLARGGKYSEDDAK---AVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSM-LKVID 293
Cdd:cd14227  88 KNHTCLVFEMLEQ-NLYD--FLKQNKFSPLPLKyirPILQQVATALMKLKSLGLIHADLKPENIMLVDPSRQPYrVKVID 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15230288 294 FGLSDFVRpDERLNDIVGSAYYVAPE-VLHRSYTTEADVWSIG-VIAYILL 342
Cdd:cd14227 165 FGSASHVS-KAVCSTYLQSRYYRAPEiILGLPFCEAIDMWSLGcVIAELFL 214
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
138-339 8.36e-08

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


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 54.29  E-value: 8.36e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 138 KELQSRIELGEEIGRGHFGytcsaKFKKGELKDQEVAVKVIPKSKMTSAIsiedvrREVKILRA-LSGHQNLVQFYDAFE 216
Cdd:cd14219   1 RTIAKQIQMVKQIGKGRYG-----EVWMGKWRGEKVAVKVFFTTEEASWF------RETEIYQTvLMRHENILGFIAADI 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 217 DNA----NVYIVMELCGGGELLDRIlarggKYSEDDAKAVL-IQILNVVAFCHL-------QG---VVHRDLKPENFLYt 281
Cdd:cd14219  70 KGTgswtQLYLITDYHENGSLYDYL-----KSTTLDTKAMLkLAYSSVSGLCHLhteifstQGkpaIAHRDLKSKNILV- 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 282 skEENSMLKVIDFGL-----SDFVRPDERLNDIVGSAYYVAPEVLHRSYTTE-------ADVWSIGVIAY 339
Cdd:cd14219 144 --KKNGTCCIADLGLavkfiSDTNEVDIPPNTRVGTKRYMPPEVLDESLNRNhfqsyimADMYSFGLILW 211
STKc_CK1_gamma cd14126
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; STKs catalyze ...
146-303 1.08e-07

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; 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. CK1gamma proteins are unique within the CK1 subfamily in that they are palmitoylated at the C-termini and are anchored to the plasma membrane. CK1gamma is involved in transducing the signaling of LDL-receptor-related protein 6 (LRP6) through direct phosphorylation following Wnt stimulation, resulting in the recruitment of the scaffold protein Axin. In Xenopus embryos, CK1gamma is required during anterio-posterior patterning. In higher vertebrates, three CK1gamma (gamma1-3) isoforms exist. In mammalian cells, CK1gamma2 has been implicated in regulating the synthesis of sphingomyelin, a phospholipid that is found in the outer leaflet of the plasma membrane, by hyperphosphorylating and inactivating the ceramide transfer protein CERT. CK1gamma2 also phosphorylates the transcription factor Smad-3 resulting in its ubiquitination and degradation. It inhibits Smad-3 mediated responses of Transforming Growth Factor-beta (TGF-beta) including cell growth arrest. The CK1 gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271028 [Multi-domain]  Cd Length: 288  Bit Score: 53.58  E-value: 1.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 146 LGEEIGRGHFGytcSAKFKKGELKDQEVAVKVIPKSKMTSAISIEdvRREVKILRALSGHQNLVQFYDAFEDNAnvyIVM 225
Cdd:cd14126   4 VGKKIGCGNFG---ELRLGKNLYNNEHVAIKLEPMKSRAPQLHLE--YRFYKLLGQAEGLPQVYYFGPCGKYNA---MVL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230288 226 ELCGGG-----ELLDRilarggKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLY--TSKEENSMLKVIDFGLS- 297
Cdd:cd14126  76 ELLGPSledlfDLCDR------TFSLKTVLMIAIQLISRIEYVHSKHLIYRDVKPENFLIgrQSTKKQHVIHIIDFGLAk 149

                ....*.
gi 15230288 298 DFVRPD 303
Cdd:cd14126 150 EYIDPE 155
 
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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