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Conserved domains on  [gi|34098881|gb|AAQ56823|]
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At5g66210 [Arabidopsis thaliana]

Protein Classification

CAMK family serine/threonine-protein kinase( domain architecture ID 11563077)

CAMK family serine/threonine-protein kinase (STK) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates, and is a multifunctional calcium and calmodulin (CaM) stimulated STK involved in cell cycle; contains EF-hand calcium binding motif(s)

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 ...
61-321 2.92e-125

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: 366.42  E-value: 2.92e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKmVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVM 140
Cdd:cd05117   1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKK-LKSEDEEMLRREIEILKRLD-HPNIVKLYEVFEDDKNLYLVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCEGGELLDRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLSDFIKPGK 220
Cdd:cd05117  79 ELCTGGELFDRIVKKG--SFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPIKIIDFGLAKIFEEGE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 221 RFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDSAKDFV 299
Cdd:cd05117 157 KLKTVCGTPYYVAPEVLKGKGyGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPEWKNVSEEAKDLI 236
                       250       260
                ....*....|....*....|..
gi 34098881 300 KKLLVKDPRARLTAAQALSHAW 321
Cdd:cd05117 237 KRLLVVDPKKRLTAAEALNHPW 258
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
369-504 8.89e-19

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 82.53  E-value: 8.89e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 369 DLRDQFDAIDVDKNGVISLEEMRQALAKDLpwklkdsrvAEILEAIDSNTDGLVDFTEFVAAALHVHQLEEHDsekwqlR 448
Cdd:COG5126   6 KLDRRFDLLDADGDGVLERDDFEALFRRLW---------ATLFSEADTDGDGRISREEFVAGMESLFEATVEP------F 70
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 449 SRAAFEKFDLDKDGYITPEELRMH-TGLRGS---IDPLLDEADIDRDGKISLHEFRRLLR 504
Cdd:COG5126  71 ARAAFDLLDTDGDGKISADEFRRLlTALGVSeeeADELFARLDTDGDGKISFEEFVAAVR 130
 
Name Accession Description Interval E-value
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
61-321 2.92e-125

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: 366.42  E-value: 2.92e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKmVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVM 140
Cdd:cd05117   1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKK-LKSEDEEMLRREIEILKRLD-HPNIVKLYEVFEDDKNLYLVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCEGGELLDRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLSDFIKPGK 220
Cdd:cd05117  79 ELCTGGELFDRIVKKG--SFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPIKIIDFGLAKIFEEGE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 221 RFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDSAKDFV 299
Cdd:cd05117 157 KLKTVCGTPYYVAPEVLKGKGyGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPEWKNVSEEAKDLI 236
                       250       260
                ....*....|....*....|..
gi 34098881 300 KKLLVKDPRARLTAAQALSHAW 321
Cdd:cd05117 237 KRLLVVDPKKRLTAAEALNHPW 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
62-322 4.59e-96

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 291.74  E-value: 4.59e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881     62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMvlPIAVEDVKREVQILIALsGHENVVQFHNAFEDDDYVYIVME 141
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI--KKDRERILREIKILKKL-KHPNIVRLYDVFEDEDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881    142 LCEGGELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKPGKR 221
Cdd:smart00220  78 YCEGGDLFDLL--KKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDE---DGHVKLADFGLARQLDPGEK 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881    222 FHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDG-IFKEVLRNKPDFSRKPWaTISDSAKDFV 299
Cdd:smart00220 153 LTTFVGTPEYMAPEVLLGKGyGKAVDIWSLGVILYELLTGKPPFPGDDQLLeLFKKIGKPKPPFPPPEW-DISPEAKDLI 231
                          250       260
                   ....*....|....*....|...
gi 34098881    300 KKLLVKDPRARLTAAQALSHAWV 322
Cdd:smart00220 232 RKLLVKDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
62-322 2.82e-67

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 215.96  E-value: 2.82e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881    62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVlPIAVEDVKREVQILiALSGHENVVQFHNAFEDDDYVYIVME 141
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIK-KKKDKNILREIKIL-KKLNHPNIVRLYDAFEDKDNLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881   142 LCEGGELLDRIlSKKGnRYSEKDAAVVVRQMLKVagechlhglvhrdmkpenflfksaqldsplkatdfglsdfIKPGKR 221
Cdd:pfam00069  79 YVEGGSLFDLL-SEKG-AFSEREAKFIMKQILEG----------------------------------------LESGSS 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881   222 FHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNkPDFSRKPWATISDSAKDFVK 300
Cdd:pfam00069 117 LTTFVGTPWYMAPEVLGGNPyGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQ-PYAFPELPSNLSEEAKDLLK 195
                         250       260
                  ....*....|....*....|..
gi 34098881   301 KLLVKDPRARLTAAQALSHAWV 322
Cdd:pfam00069 196 KLLKKDPSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
55-323 1.27e-54

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 190.99  E-value: 1.27e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  55 SKDFHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDD 134
Cdd:COG0515   2 SALLLGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREARALARLN-HPNIVRVYDVGEEDG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 135 YVYIVMELCEGGELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSD 214
Cdd:COG0515  81 RPYLVMEYVEGESLADLL--RRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTP---DGRVKLIDFGIAR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 215 FIKPG--KRFHDIVGSAYYVAPEVLK-RRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATI 291
Cdd:COG0515 156 ALGGAtlTQTGTVVGTPGYMAPEQARgEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDL 235
                       250       260       270
                ....*....|....*....|....*....|..
gi 34098881 292 SDSAKDFVKKLLVKDPRARLTAAQALSHAWVR 323
Cdd:COG0515 236 PPALDAIVLRALAKDPEERYQSAAELAAALRA 267
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
64-311 3.05e-33

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 129.17  E-value: 3.05e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881   64 IGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELC 143
Cdd:PTZ00263  22 MGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELS-HPFIVNMMCSFQDENRVYFLLEFV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  144 EGGELLDRIlsKKGNRYSeKDAAVVVRQMLKVAGEcHLH--GLVHRDMKPENFLFKSaqlDSPLKATDFGLSDfiKPGKR 221
Cdd:PTZ00263 101 VGGELFTHL--RKAGRFP-NDVAKFYHAELVLAFE-YLHskDIIYRDLKPENLLLDN---KGHVKVTDFGFAK--KVPDR 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  222 FHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRkpWatISDSAKDFVK 300
Cdd:PTZ00263 172 TFTLCGTPEYLAPEVIQSKGhGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPN--W--FDGRARDLVK 247
                        250
                 ....*....|.
gi 34098881  301 KLLVKDPRARL 311
Cdd:PTZ00263 248 GLLQTDHTKRL 258
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
62-264 1.56e-23

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 104.11  E-value: 1.56e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881   62 YTIGKLLGHGQFGYTYVA----IHRPngdrVAVKRL------DkskmvlPIAVEDVKREVQILIALSgHENVVQFHNAFE 131
Cdd:NF033483   9 YEIGERIGRGGMAEVYLAkdtrLDRD----VAVKVLrpdlarD------PEFVARFRREAQSAASLS-HPNIVSVYDVGE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  132 DDDYVYIVMELCEGGELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFG 211
Cdd:NF033483  78 DGGIPYIVMEYVDGRTLKDYI--REHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITK---DGRVKVTDFG 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34098881  212 LSdfikpgkRF---------HDIVGSAYYVAPE------VLKRrsgpeSDVWSIGVITYILLCGRRPF 264
Cdd:NF033483 153 IA-------RAlssttmtqtNSVLGTVHYLSPEqarggtVDAR-----SDIYSLGIVLYEMLTGRPPF 208
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
369-504 8.89e-19

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 82.53  E-value: 8.89e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 369 DLRDQFDAIDVDKNGVISLEEMRQALAKDLpwklkdsrvAEILEAIDSNTDGLVDFTEFVAAALHVHQLEEHDsekwqlR 448
Cdd:COG5126   6 KLDRRFDLLDADGDGVLERDDFEALFRRLW---------ATLFSEADTDGDGRISREEFVAGMESLFEATVEP------F 70
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 449 SRAAFEKFDLDKDGYITPEELRMH-TGLRGS---IDPLLDEADIDRDGKISLHEFRRLLR 504
Cdd:COG5126  71 ARAAFDLLDTDGDGKISADEFRRLlTALGVSeeeADELFARLDTDGDGKISFEEFVAAVR 130
PTZ00184 PTZ00184
calmodulin; Provisional
358-503 2.63e-16

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 75.95  E-value: 2.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  358 LASTLDEAEISDLRDQFDAIDVDKNGVISLEEMRQALaKDLPWKLKDSRVAEILEAIDSNTDGLVDFTEFVAaaLHVHQL 437
Cdd:PTZ00184   1 MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVM-RSLGQNPTEAELQDMINEVDADGNGTIDFPEFLT--LMARKM 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34098881  438 EEHDSEKwqlRSRAAFEKFDLDKDGYITPEELR---MHTGLRGS---IDPLLDEADIDRDGKISLHEFRRLL 503
Cdd:PTZ00184  78 KDTDSEE---EIKEAFKVFDRDGNGFISAAELRhvmTNLGEKLTdeeVDEMIREADVDGDGQINYEEFVKMM 146
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
85-317 4.92e-14

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: 75.27  E-value: 4.92e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881     85 GDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFE-DDDYVYIVMELCEGGELLDRiLSKKGnrysEK 163
Cdd:TIGR03903    3 GHEVAIKLLRTDAPEEEHQRARFRRETALCARLY-HPNIVALLDSGEaPPGLLFAVFEYVPGRTLREV-LAADG----AL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881    164 DAAVVVRQMLKV--AGEC-HLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLSDFIkPG---------KRFHDIVGSAYY 231
Cdd:TIGR03903   77 PAGETGRLMLQVldALACaHNQGIVHRDLKPQNIMVSQTGVRPHAKVLDFGIGTLL-PGvrdadvatlTRTTEVLGTPTY 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881    232 VAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLrNKPDFSRKPWATiSDSAKDFVKKLLVKDPRAR 310
Cdd:TIGR03903  156 CAPEQLRGEPvTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQL-SPVDVSLPPWIA-GHPLGQVLRKALNKDPRQR 233

                   ....*..
gi 34098881    311 LTAAQAL 317
Cdd:TIGR03903  234 AASAPAL 240
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
369-513 4.80e-12

EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein (ALG-2); The family includes some homologs of mammalian apoptosis-linked gene 2 protein (ALG-2) mainly found in lower eukaryotes, such as a parasitic protist Leishmarua major and a cellular slime mold Dictyostelium discoideum. These homologs contains five EF-hand motifs. Due to the presence of unfavorable residues at the Ca2+-coordinating positions, their non-canonical EF4 and EF5 hands may not bind Ca2+. Two Dictyostelium PEF proteins are the prototypes of this family. They may bind to cytoskeletal proteins and/or signal-transducing proteins localized to detergent-resistant membranes named lipid rafts, and occur as monomers or weak homo- or heterodimers like ALG-2. They can serve as a mediator for Ca2+ signaling-related Dictyostehum programmed cell death (PCD).


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 64.16  E-value: 4.80e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 369 DLRDQFDAIDVDKNGVISLEEMRQALAKDLPwKLKDSRVAEILEAIDSNTDGLVDFTEFvaAALHvhqleehdseKWQLR 448
Cdd:cd16185   1 ELRQWFRAVDRDRSGSIDVNELQKALAGGGL-LFSLATAEKLIRMFDRDGNGTIDFEEF--AALH----------QFLSN 67
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34098881 449 SRAAFEKFDLDKDGYITPEELRMHTGLRG-SIDP-----LLDEADIDRDGKISLHEFRRLlrTASISSQRA 513
Cdd:cd16185  68 MQNGFEQRDTSRSGRLDANEVHEALAASGfQLDPpafqaLFRKFDPDRGGSLGFDDYIEL--CIFLASARN 136
EF-hand_7 pfam13499
EF-hand domain pair;
367-432 1.50e-09

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 54.18  E-value: 1.50e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34098881   367 ISDLRDQFDAIDVDKNGVISLEEMRQALAK-DLPWKLKDSRVAEILEAIDSNTDGLVDFTEFVAAAL 432
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKlEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
 
Name Accession Description Interval E-value
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
61-321 2.92e-125

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: 366.42  E-value: 2.92e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKmVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVM 140
Cdd:cd05117   1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKK-LKSEDEEMLRREIEILKRLD-HPNIVKLYEVFEDDKNLYLVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCEGGELLDRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLSDFIKPGK 220
Cdd:cd05117  79 ELCTGGELFDRIVKKG--SFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPIKIIDFGLAKIFEEGE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 221 RFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDSAKDFV 299
Cdd:cd05117 157 KLKTVCGTPYYVAPEVLKGKGyGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPEWKNVSEEAKDLI 236
                       250       260
                ....*....|....*....|..
gi 34098881 300 KKLLVKDPRARLTAAQALSHAW 321
Cdd:cd05117 237 KRLLVVDPKKRLTAAEALNHPW 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
62-322 4.59e-96

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 291.74  E-value: 4.59e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881     62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMvlPIAVEDVKREVQILIALsGHENVVQFHNAFEDDDYVYIVME 141
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI--KKDRERILREIKILKKL-KHPNIVRLYDVFEDEDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881    142 LCEGGELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKPGKR 221
Cdd:smart00220  78 YCEGGDLFDLL--KKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDE---DGHVKLADFGLARQLDPGEK 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881    222 FHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDG-IFKEVLRNKPDFSRKPWaTISDSAKDFV 299
Cdd:smart00220 153 LTTFVGTPEYMAPEVLLGKGyGKAVDIWSLGVILYELLTGKPPFPGDDQLLeLFKKIGKPKPPFPPPEW-DISPEAKDLI 231
                          250       260
                   ....*....|....*....|...
gi 34098881    300 KKLLVKDPRARLTAAQALSHAWV 322
Cdd:smart00220 232 RKLLVKDPEKRLTAEEALQHPFF 254
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
61-321 1.04e-83

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: 259.76  E-value: 1.04e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVlPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVM 140
Cdd:cd14003   1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLK-EEIEEKIKREIEIMKLLN-HPNIIKLYEVIETENKIYLVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCEGGELLDRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLfksaqLDSP--LKATDFGLSDFIKP 218
Cdd:cd14003  79 EYASGGELFDYIVNNG--RLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENIL-----LDKNgnLKIIDFGLSNEFRG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 GKRFHDIVGSAYYVAPEVLKRRS--GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRkpwaTISDSAK 296
Cdd:cd14003 152 GSLLKTFCGTPAYAAPEVLLGRKydGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPS----HLSPDAR 227
                       250       260
                ....*....|....*....|....*
gi 34098881 297 DFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd14003 228 DLIRRMLVVDPSKRITIEEILNHPW 252
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
59-321 3.98e-79

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: 248.44  E-value: 3.98e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  59 HDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKmvLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYI 138
Cdd:cd14083   2 RDKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKA--LKGKEDSLENEIAVLRKIK-HPNIVQLLDIYESKSHLYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 139 VMELCEGGELLDRILSKkGNrYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLSDFIKP 218
Cdd:cd14083  79 VMELVTGGELFDRIVEK-GS-YTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSPDEDSKIMISDFGLSKMEDS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 GkrfhdIVGSAY----YVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISD 293
Cdd:cd14083 157 G-----VMSTACgtpgYVAPEVLAQKPyGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEYEFDSPYWDDISD 231
                       250       260
                ....*....|....*....|....*...
gi 34098881 294 SAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd14083 232 SAKDFIRHLMEKDPNKRYTCEQALEHPW 259
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
58-359 8.21e-72

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: 230.87  E-value: 8.21e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  58 FHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSkmvlpIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVY 137
Cdd:cd14085   1 LEDFFEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKT-----VDKKIVRTEIGVLLRLS-HPNIIKLKEIFETPTEIS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 138 IVMELCEGGELLDRILSKkgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLSDFIK 217
Cdd:cd14085  75 LVLELVTGGELFDRIVEK--GYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPDAPLKIADFGLSKIVD 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 218 PGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWD-RTEDGIFKEVLRNKPDFSRKPWATISDSA 295
Cdd:cd14085 153 QQVTMKTVCGTPGYCAPEILRGCAyGPEVDMWSVGVITYILLCGFEPFYDeRGDQYMFKRILNCDYDFVSPWWDDVSLNA 232
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34098881 296 KDFVKKLLVKDPRARLTAAQALSHAWVREGGNATDIPVdiSVLNNLRQFVRYSRLKQFALRALA 359
Cdd:cd14085 233 KDLVKKLIVLDPKKRLTTQQALQHPWVTGKAANFAHMD--TAQKKLQEFNARRKLKAAVKAVVA 294
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
57-323 6.52e-68

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: 218.88  E-value: 6.52e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  57 DFHdhytIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYV 136
Cdd:cd14007   1 DFE----IGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQKSGLEHQLRREIEIQSHLR-HPNILRLYGYFEDKKRI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 137 YIVMELCEGGELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLdspLKATDFGLSDFI 216
Cdd:cd14007  76 YLILEYAPNGELYKEL--KKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGE---LKLADFGWSVHA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 217 KPGKRfHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFsrkpWATISDSA 295
Cdd:cd14007 151 PSNRR-KTFCGTLDYLPPEMVEGKEyDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKF----PSSVSPEA 225
                       250       260
                ....*....|....*....|....*...
gi 34098881 296 KDFVKKLLVKDPRARLTAAQALSHAWVR 323
Cdd:cd14007 226 KDLISKLLQKDPSKRLSLEQVLNHPWIK 253
Pkinase pfam00069
Protein kinase domain;
62-322 2.82e-67

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 215.96  E-value: 2.82e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881    62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVlPIAVEDVKREVQILiALSGHENVVQFHNAFEDDDYVYIVME 141
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIK-KKKDKNILREIKIL-KKLNHPNIVRLYDAFEDKDNLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881   142 LCEGGELLDRIlSKKGnRYSEKDAAVVVRQMLKVagechlhglvhrdmkpenflfksaqldsplkatdfglsdfIKPGKR 221
Cdd:pfam00069  79 YVEGGSLFDLL-SEKG-AFSEREAKFIMKQILEG----------------------------------------LESGSS 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881   222 FHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNkPDFSRKPWATISDSAKDFVK 300
Cdd:pfam00069 117 LTTFVGTPWYMAPEVLGGNPyGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQ-PYAFPELPSNLSEEAKDLLK 195
                         250       260
                  ....*....|....*....|..
gi 34098881   301 KLLVKDPRARLTAAQALSHAWV 322
Cdd:pfam00069 196 KLLKKDPSKRLTATQALQHPWF 217
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
66-322 3.41e-67

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: 218.32  E-value: 3.41e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDvkrEVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd14166   9 EVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSSLEN---EIAVLKRIK-HENIVTLEDIYESTTHYYLVMQLVSG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRILSKkgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLSDFIKPGKrFHDI 225
Cdd:cd14166  85 GELFDRILER--GVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTPDENSKIMITDFGLSKMEQNGI-MSTA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 226 VGSAYYVAPEVLKRRsgPES---DVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDSAKDFVKKL 302
Cdd:cd14166 162 CGTPGYVAPEVLAQK--PYSkavDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFESPFWDDISESAKDFIRHL 239
                       250       260
                ....*....|....*....|
gi 34098881 303 LVKDPRARLTAAQALSHAWV 322
Cdd:cd14166 240 LEKNPSKRYTCEKALSHPWI 259
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
62-330 1.19e-66

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: 217.12  E-value: 1.19e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKmvlpiavEDVKREVQILIALSGHENVVQFHNAFEDDDYVYIVME 141
Cdd:cd14091   2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSK-------RDPSEEIEILLRYGQHPNIITLRDVYDDGNSVYLVTE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELLDRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLD-SPLKATDFGLSdfikpgK 220
Cdd:cd14091  75 LLRGGELLDRILRQK--FFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGDpESLRICDFGFA------K 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 221 RFHDIVG-------SAYYVAPEVLKRRSGPES-DVWSIGVITYILLCGRRPFW---DRTEDGIFKEVLRNKPDFSRKPWA 289
Cdd:cd14091 147 QLRAENGllmtpcyTANFVAPEVLKKQGYDAAcDIWSLGVLLYTMLAGYTPFAsgpNDTPEVILARIGSGKIDLSGGNWD 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 34098881 290 TISDSAKDFVKKLLVKDPRARLTAAQALSHAWVREGGNATD 330
Cdd:cd14091 227 HVSDSAKDLVRKMLHVDPSQRPTAAQVLQHPWIRNRDSLPQ 267
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
56-322 5.99e-65

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: 212.25  E-value: 5.99e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  56 KDFHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVE-----DVKREVQILIALSgHENVVQFHNAF 130
Cdd:cd14084   2 KELRKKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKFTIGSRREinkprNIETEIEILKKLS-HPCIIKIEDFF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 131 EDDDYVYIVMELCEGGELLDRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLKATDF 210
Cdd:cd14084  81 DAEDDYYIVLELMEGGELFDRVVSNK--RLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEECLIKITDF 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 211 GLSDFIKPGKRFHDIVGSAYYVAPEVLKRRS----GPESDVWSIGVITYILLCGRRPFWD-RTEDGIFKEVLRNKPDFSR 285
Cdd:cd14084 159 GLSKILGETSLMKTLCGTPTYLAPEVLRSFGtegyTRAVDCWSLGVILFICLSGYPPFSEeYTQMSLKEQILSGKYTFIP 238
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 34098881 286 KPWATISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14084 239 KAWKNVSEEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
62-337 6.75e-65

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: 212.06  E-value: 6.75e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVedVKREVQILIALSgHENVVQFHNAFEDDDYVYIVME 141
Cdd:cd14169   5 YELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEAM--VENEIAVLRRIN-HENIVSLEDIYESPTHLYLAME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELLDRILSKkgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLSDfIKPGKR 221
Cdd:cd14169  82 LVTGGELFDRIIER--GSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATPFEDSKIMISDFGLSK-IEAQGM 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 222 FHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDSAKDFVK 300
Cdd:cd14169 159 LSTACGTPGYVAPELLEQKPyGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYEFDSPYWDDISESAKDFIR 238
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 34098881 301 KLLVKDPRARLTAAQALSHAWVrEGGNATDIPVDISV 337
Cdd:cd14169 239 HLLERDPEKRFTCEQALQHPWI-SGDTALDRDIHGSV 274
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
60-322 1.04e-64

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: 211.04  E-value: 1.04e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLdkSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIV 139
Cdd:cd14167   3 DIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCI--AKKALEGKETSIENEIAVLHKIK-HPNIVALDDIYESGGHLYLI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGELLDRILSKkgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLSDFIKPG 219
Cdd:cd14167  80 MQLVSGGELFDRIVEK--GFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSLDEDSKIMISDFGLSKIEGSG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 220 KRFHDIVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDSAKDF 298
Cdd:cd14167 158 SVMSTACGTPGYVAPEVLAQKPYSKAvDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDSPYWDDISDSAKDF 237
                       250       260
                ....*....|....*....|....
gi 34098881 299 VKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14167 238 IQHLMEKDPEKRFTCEQALQHPWI 261
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
68-321 3.04e-64

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: 209.43  E-value: 3.04e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLpiavEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEGGE 147
Cdd:cd14006   1 LGRGRFGVVKRCIEKATGREFAAKFIPKRDKKK----EAVLREISILNQLQ-HPRIIQLHEAYESPTELVLILELCSGGE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 148 LLDRILSKkgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSpLKATDFGLSDFIKPGKRFHDIVG 227
Cdd:cd14006  76 LLDRLAER--GSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSPQ-IKIIDFGLARKLNPGEELKEIFG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 228 SAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDSAKDFVKKLLVKD 306
Cdd:cd14006 153 TPEFVAPEIVNGEPvSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDFSEEYFSSVSQEAKDFIRKLLVKE 232
                       250
                ....*....|....*
gi 34098881 307 PRARLTAAQALSHAW 321
Cdd:cd14006 233 PRKRPTAQEALQHPW 247
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
58-321 6.59e-63

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: 206.82  E-value: 6.59e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  58 FHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIA-----VEDVKREVQILIALSGHENVVQFHNAFED 132
Cdd:cd14093   1 FYAKYEPKEILGRGVSSTVRRCIEKETGQEFAVKIIDITGEKSSENeaeelREATRREIEILRQVSGHPNIIELHDVFES 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 133 DDYVYIVMELCEGGELLDRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLfksaqLDSPL--KATDF 210
Cdd:cd14093  81 PTFIFLVFELCRKGELFDYLTEVV--TLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENIL-----LDDNLnvKISDF 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 211 GLSDFIKPGKRFHDIVGSAYYVAPEVLKRRSGP-------ESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDF 283
Cdd:cd14093 154 GFATRLDEGEKLRELCGTPGYLAPEVLKCSMYDnapgygkEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKYEF 233
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 34098881 284 SRKPWATISDSAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd14093 234 GSPEWDDISDTAKDLISKLLVVDPKKRLTAEEALEHPF 271
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
58-332 2.09e-62

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: 206.77  E-value: 2.09e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  58 FHDHYTIG---KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKmvlpiaveDVKREVQILIALSGHENVVQFHNAFEDDD 134
Cdd:cd14092   1 FFQNYELDlreEALGDGSFSVCRKCVHKKTGQEFAVKIVSRRL--------DTSREVQLLRLCQGHPNIVKLHEVFQDEL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 135 YVYIVMELCEGGELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLSD 214
Cdd:cd14092  73 HTYLVMELLRGGELLERI--RKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDDAEIKIVDFGFAR 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 215 fIKPG-KRFHDIVGSAYYVAPEVLKRRSGP----ES-DVWSIGVITYILLCGRRPFWDRTEDG----IFKEVLRNKPDFS 284
Cdd:cd14092 151 -LKPEnQPLKTPCFTLPYAAPEVLKQALSTqgydEScDLWSLGVILYTMLSGQVPFQSPSRNEsaaeIMKRIKSGDFSFD 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 34098881 285 RKPWATISDSAKDFVKKLLVKDPRARLTAAQALSHAWVREGGNATDIP 332
Cdd:cd14092 230 GEEWKNVSSEAKSLIQGLLTVDPSKRLTMSELRNHPWLQGSSSPSSTP 277
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
60-321 2.90e-62

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: 204.32  E-value: 2.90e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIV 139
Cdd:cd14099   1 KRYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTKPKQREKLKSEIKIHRSLK-HPNIVKFHDCFEDEENVYIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGELLDriLSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLfksaqLDSP--LKATDFGLSDFIK 217
Cdd:cd14099  80 LELCSNGSLME--LLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLF-----LDENmnVKIGDFGLAARLE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 218 -PGKRFHDIVGSAYYVAPEVLKRRSG--PESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPwaTISDS 294
Cdd:cd14099 153 yDGERKKTLCGTPNYIAPEVLEKKKGhsFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPSHL--SISDE 230
                       250       260
                ....*....|....*....|....*..
gi 34098881 295 AKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd14099 231 AKDLIRSMLQPDPTKRPSLDEILSHPF 257
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
61-321 6.42e-62

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: 203.71  E-value: 6.42e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMvlpIAVED-VKREVQILIALSgHENVVQFHNAFEDDDYVYIV 139
Cdd:cd14095   1 KYDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKC---KGKEHmIENEVAILRRVK-HPNIVQLIEEYDTDTELYLV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGELLDRILSkkGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDS-PLKATDFGLSDFIKp 218
Cdd:cd14095  77 MELVKGGDLFDAITS--STKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEDGSkSLKLADFGLATEVK- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 gKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFW--DRTEDGIFKEVLRNKPDFSRKPWATISDSA 295
Cdd:cd14095 154 -EPLFTVCGTPTYVAPEILAETGyGLKVDIWAAGVITYILLCGFPPFRspDRDQEELFDLILAGEFEFLSPYWDNISDSA 232
                       250       260
                ....*....|....*....|....*.
gi 34098881 296 KDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd14095 233 KDLISRMLVVDPEKRYSAGQVLDHPW 258
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
60-324 1.02e-61

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: 204.19  E-value: 1.02e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVlPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIV 139
Cdd:cd14086   1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLS-ARDHQKLEREARICRLLK-HPNIVRLHDSISEEGFHYLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGELLDRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLSDFIKPG 219
Cdd:cd14086  79 FDLVTGGELFEDIVARE--FYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEVQGD 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 220 K-RFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDSAKD 297
Cdd:cd14086 157 QqAWFGFAGTPGYLSPEVLRKDPyGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPEWDTVTPEAKD 236
                       250       260
                ....*....|....*....|....*..
gi 34098881 298 FVKKLLVKDPRARLTAAQALSHAWVRE 324
Cdd:cd14086 237 LINQMLTVNPAKRITAAEALKHPWICQ 263
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
61-322 1.22e-61

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: 202.82  E-value: 1.22e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVlpiAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVM 140
Cdd:cd05122   1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKE---KKESILNEIAILKKCK-HPNIVKYYGSYLKKDELWIVM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCEGGELLDrILSKKGNRYSEKDAAVVVRQMLKvaGECHLH--GLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKP 218
Cdd:cd05122  77 EFCSGGSLKD-LLKNTNKTLTEQQIAYVCKEVLK--GLEYLHshGIIHRDIKAANILLTS---DGEVKLIDFGLSAQLSD 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 GKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFwdrTEDGIFK---EVLRNKPDFSRKPWaTISDS 294
Cdd:cd05122 151 GKTRNTFVGTPYWMAPEVIQGKPyGFKADIWSLGITAIEMAEGKPPY---SELPPMKalfLIATNGPPGLRNPK-KWSKE 226
                       250       260
                ....*....|....*....|....*...
gi 34098881 295 AKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd05122 227 FKDFLKKCLQKDPEKRPTAEQLLKHPFI 254
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
61-321 2.56e-60

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: 199.42  E-value: 2.56e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILiALSGHENVVQFHNAFEDDDYVYIVM 140
Cdd:cd14079   3 NYILGKTLGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSLDMEEKIRREIQIL-KLFRHPHIIRLYEVIETPTDIFMVM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCEGGELLDRIlSKKGnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLfksaqLDSPL--KATDFGLSDFIKP 218
Cdd:cd14079  82 EYVSGGELFDYI-VQKG-RLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLL-----LDSNMnvKIADFGLSNIMRD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 GKRFHDIVGSAYYVAPEVL--KRRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNK---PDFsrkpwatISD 293
Cdd:cd14079 155 GEFLKTSCGSPNYAAPEVIsgKLYAGPEVDVWSCGVILYALLCGSLPFDDEHIPNLFKKIKSGIytiPSH-------LSP 227
                       250       260
                ....*....|....*....|....*...
gi 34098881 294 SAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd14079 228 GARDLIKRMLVVDPLKRITIPEIRQHPW 255
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
60-322 1.83e-59

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: 197.71  E-value: 1.83e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMV---LPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYV 136
Cdd:cd14105   5 DFYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKasrRGVSREDIEREVSILRQVL-HPNIITLHDVFENKTDV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 137 YIVMELCEGGELLDRILSKKGnrYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSP-LKATDFGLSDF 215
Cdd:cd14105  84 VLILELVAGGELFDFLAEKES--LSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVPIPrIKLIDFGLAHK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 216 IKPGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDS 294
Cdd:cd14105 162 IEDGNEFKNIFGTPEFVAPEIVNYEPlGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVNYDFDDEYFSNTSEL 241
                       250       260
                ....*....|....*....|....*...
gi 34098881 295 AKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14105 242 AKDFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
60-322 2.16e-59

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: 198.02  E-value: 2.16e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTI-GKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVlpiAVEDVKREVQILIALSGHENVVQFHNAFEDDDYVYI 138
Cdd:cd14090   1 DLYKLtGELLGEGAYASVQTCINLYTGKEYAVKIIEKHPGH---SRSRVFREVETLHQCQGHPNILQLIEYFEDDERFYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 139 VMELCEGGELLDRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLSDFIKP 218
Cdd:cd14090  78 VFEKMRGGPLLSHIEKRV--HFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVSPVKICDFDLGSGIKL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 GKRFHD---------IVGSAYYVAPEVLKRRSGPES------DVWSIGVITYILLCGRRPF---------WDRTE----- 269
Cdd:cd14090 156 SSTSMTpvttpelltPVGSAEYMAPEVVDAFVGEALsydkrcDLWSLGVILYIMLCGYPPFygrcgedcgWDRGEacqdc 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 34098881 270 -DGIFKEVLRNKPDFSRKPWATISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14090 236 qELLFHSIQEGEYEFPEKEWSHISAEAKDLISHLLVRDASQRYTAEQVLQHPWV 289
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
62-321 2.62e-59

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: 197.13  E-value: 2.62e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTI-GKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSkmvlPIAvedvKREVQILIALSGHENVVQ----FHNAFEDDDYV 136
Cdd:cd14089   2 YTIsKQVLGLGINGKVLECFHKKTGEKFALKVLRDN----PKA----RREVELHWRASGCPHIVRiidvYENTYQGRKCL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 137 YIVMELCEGGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLSdfi 216
Cdd:cd14089  74 LVVMECMEGGELFSRIQERADSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPNAILKLTDFGFA--- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 217 kpgKRFHDIVG------SAYYVAPEVLkrrsGPES-----DVWSIGVITYILLCGRRPFWDRTEDGI---FKEVLRN-KP 281
Cdd:cd14089 151 ---KETTTKKSlqtpcyTPYYVAPEVL----GPEKydkscDMWSLGVIMYILLCGYPPFYSNHGLAIspgMKKRIRNgQY 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 34098881 282 DFSRKPWATISDSAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd14089 224 EFPNPEWSNVSEEAKDLIRGLLKTDPSERLTIEEVMNHPW 263
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
62-321 2.65e-59

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: 196.86  E-value: 2.65e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVME 141
Cdd:cd14663   2 YELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREGMVEQIKREIAIMKLLR-HPNIVELHEVMATKTKIFFVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELLDRILskKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLS---DFIKP 218
Cdd:cd14663  81 LVTGGELFSKIA--KNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDE---DGNLKISDFGLSalsEQFRQ 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 GKRFHDIVGSAYYVAPEVLKRRS--GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRkpWatISDSAK 296
Cdd:cd14663 156 DGLLHTTCGTPNYVAPEVLARRGydGAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEYPR--W--FSPGAK 231
                       250       260
                ....*....|....*....|....*
gi 34098881 297 DFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd14663 232 SLIKRILDPNPSTRITVEQIMASPW 256
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
56-352 3.40e-58

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: 195.27  E-value: 3.40e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  56 KDFHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSkmVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDY 135
Cdd:cd14168   6 EDIKKIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKK--ALKGKESSIENEIAVLRKIK-HENIVALEDIYESPNH 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 136 VYIVMELCEGGELLDRILSKkgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLSDF 215
Cdd:cd14168  83 LYLVMQLVSGGELFDRIVEK--GFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQDEESKIMISDFGLSKM 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 216 IKPGKRFHDIVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDS 294
Cdd:cd14168 161 EGKGDVMSTACGTPGYVAPEVLAQKPYSKAvDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFDSPYWDDISDS 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 34098881 295 AKDFVKKLLVKDPRARLTAAQALSHAWVrEGGNATDIPVDISVLNNLRQFVRYSRLKQ 352
Cdd:cd14168 241 AKDFIRNLMEKDPNKRYTCEQALRHPWI-AGDTALCKNIHESVSAQIRKNFAKSKWRQ 297
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
62-322 5.94e-58

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: 193.13  E-value: 5.94e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMvlpiAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVME 141
Cdd:cd14087   3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKCR----GREVCESELNVLRRVR-HTNIIQLIEVFETKERVYMVME 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELLDRILSKkgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLSDFIK--PG 219
Cdd:cd14087  78 LATGGELFDRIIAK--GSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPDSKIMITDFGLASTRKkgPN 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 220 KRFHDIVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDSAKDF 298
Cdd:cd14087 156 CLMKTTCGTPEYIAPEILLRKPYTQSvDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSGEPWPSVSNLAKDF 235
                       250       260
                ....*....|....*....|....
gi 34098881 299 VKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14087 236 IDRLLTVNPGERLSATQALKHPWI 259
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
68-321 3.91e-57

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: 190.90  E-value: 3.91e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKmvlPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEGGE 147
Cdd:cd14103   1 LGRGKFGTVYRCVEKATGKELAAKFIKCRK---AKDREDVRNEIEIMNQLR-HPRLLQLYDAFETPREMVLVMEYVAGGE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 148 LLDRILSKKGNrYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaQLDSPLKATDFGLSDFIKPGKRFHDIVG 227
Cdd:cd14103  77 LFERVVDDDFE-LTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVS-RTGNQIKIIDFGLARKYDPDKKLKVLFG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 228 SAYYVAPEVLK-RRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDSAKDFVKKLLVKD 306
Cdd:cd14103 155 TPEFVAPEVVNyEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKWDFDDEAFDDISDEAKDFISKLLVKD 234
                       250
                ....*....|....*
gi 34098881 307 PRARLTAAQALSHAW 321
Cdd:cd14103 235 PRKRMSAAQCLQHPW 249
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
68-316 4.84e-57

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: 190.42  E-value: 4.84e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEGGE 147
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVEHTLNERNILERVN-HPFIVKLHYAFQTEEKLYLVLDYVPGGE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 148 LLDRiLSKKGnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLS-DFIKPGKRFHDIV 226
Cdd:cd05123  80 LFSH-LSKEG-RFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDS---DGHIKLTDFGLAkELSSDGDRTYTFC 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 227 GSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKpwatISDSAKDFVKKLLVK 305
Cdd:cd05123 155 GTPEYLAPEVLLGKGyGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPEY----VSPEAKSLISGLLQK 230
                       250
                ....*....|.
gi 34098881 306 DPRARLTAAQA 316
Cdd:cd05123 231 DPTKRLGSGGA 241
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
62-322 8.84e-57

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: 190.16  E-value: 8.84e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILiALSGHENVVQFHNAFEDDDYVYIVME 141
Cdd:cd14081   3 YRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESVLMKVEREIAIM-KLIEHPNVLKLYDVYENKKYLYLVLE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELLDrILSKKGnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQldsPLKATDFGLSDFIKPGKR 221
Cdd:cd14081  82 YVSGGELFD-YLVKKG-RLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKN---NIKIADFGMASLQPEGSL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 222 FHDIVGSAYYVAPEVLKRRS--GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNK---PDFsrkpwatISDSAK 296
Cdd:cd14081 157 LETSCGSPHYACPEVIKGEKydGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVfhiPHF-------ISPDAQ 229
                       250       260
                ....*....|....*....|....*.
gi 34098881 297 DFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14081 230 DLLRRMLEVNPEKRITIEEIKKHPWF 255
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
68-322 1.10e-56

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: 190.07  E-value: 1.10e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKM-----------VLPIAVEDVKREVQILIALSgHENVVQFHNAFEDD--D 134
Cdd:cd14008   1 LGRGSFGKVKLALDTETGQLYAIKIFNKSRLrkrregkndrgKIKNALDDVRREIAIMKKLD-HPNIVRLYEVIDDPesD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 135 YVYIVMELCEGGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSD 214
Cdd:cd14008  80 KLYLVLEYCEGGPVMELDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTA---DGTVKISDFGVSE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 215 FIKPGK-RFHDIVGSAYYVAPEVL----KRRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPwa 289
Cdd:cd14008 157 MFEDGNdTLQKTAGTPAFLAPELCdgdsKTYSGKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDEFPIPP-- 234
                       250       260       270
                ....*....|....*....|....*....|...
gi 34098881 290 TISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14008 235 ELSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
62-322 1.62e-56

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: 189.70  E-value: 1.62e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHR--PNGDRVAVKRLDKSKmvlpiAVEDVK-----REVQILIALSgHENVVQFHNAFEDDD 134
Cdd:cd14080   2 YRLGKTIGEGSYSKVKLAEYTksGLKEKVACKIIDKKK-----APKDFLekflpRELEILRKLR-HPNIIQVYSIFERGS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 135 YVYIVMELCEGGELLDRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLfksaqLDSP--LKATDFGL 212
Cdd:cd14080  76 KVFIFMEYAEHGDLLEYIQKRG--ALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENIL-----LDSNnnVKLSDFGF 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 213 SDFIKPGKRFH---DIVGSAYYVAPEVLKRR--SGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKP 287
Cdd:cd14080 149 ARLCPDDDGDVlskTFCGSAAYAAPEILQGIpyDPKKYDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVRFPSSV 228
                       250       260       270
                ....*....|....*....|....*....|....*
gi 34098881 288 WaTISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14080 229 K-KLSPECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
61-317 4.02e-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: 188.56  E-value: 4.02e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVM 140
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLS-HPNIVRVYDVGEDDGRPYIVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCEGGELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKPGK 220
Cdd:cd14014  80 EYVEGGSLADLL--RERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTE---DGRVKLTDFGIARALGDSG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 221 --RFHDIVGSAYYVAPEVLK-RRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDSAKD 297
Cdd:cd14014 155 ltQTGSVLGTPAYMAPEQARgGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPALDA 234
                       250       260
                ....*....|....*....|
gi 34098881 298 FVKKLLVKDPRARLTAAQAL 317
Cdd:cd14014 235 IILRALAKDPEERPQSAAEL 254
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
61-322 6.87e-56

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: 188.14  E-value: 6.87e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKmVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVM 140
Cdd:cd14097   2 IYTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREK-AGSSAVKLLEREVDILKHVN-HAHIIHLEEVFETPKRMYLVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCEGGELlDRILSKKGnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSP----LKATDFGLSdfI 216
Cdd:cd14097  80 ELCEDGEL-KELLLRKG-FFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIIDNNdklnIKVTDFGLS--V 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 217 KPGKR----FHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATI 291
Cdd:cd14097 156 QKYGLgedmLQETCGTPIYMAPEVISAHGySQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTQSVWQSV 235
                       250       260       270
                ....*....|....*....|....*....|.
gi 34098881 292 SDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14097 236 SDAAKNVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
61-321 4.20e-55

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: 186.14  E-value: 4.20e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPI-AVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIV 139
Cdd:cd14098   1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNDkNLQLFQREINILKSLE-HPGIVRLIDWYEDDQHIYLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGELLDRILSKKGnrYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSP--LKATDFGLSDFIK 217
Cdd:cd14098  80 MEYVEGGDLMDFIMAWGA--IPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQ---DDPviVKISDFGLAKVIH 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 218 PGKRFHDIVGSAYYVAPEVLKRRSGPES-------DVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKpdFSRKPWAT 290
Cdd:cd14098 155 TGTFLVTFCGTMAYLAPEILMSKEQNLQggysnlvDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGR--YTQPPLVD 232
                       250       260       270
                ....*....|....*....|....*....|...
gi 34098881 291 --ISDSAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd14098 233 fnISEEAIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
55-322 5.56e-55

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: 185.63  E-value: 5.56e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  55 SKDFHDHYTI-GKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEdVKREVQILIALSGHENVVQFHNAFEDD 133
Cdd:cd14106   2 TENINEVYTVeSTPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDCRNE-ILHEIAVLELCKDCPRVVNLHEVYETR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 134 DYVYIVMELCEGGELLDRILSkkGNRYSEKDAAVVVRQMLKvaGECHLH--GLVHRDMKPENFLFKSAQLDSPLKATDFG 211
Cdd:cd14106  81 SELILILELAAGGELQTLLDE--EECLTEADVRRLMRQILE--GVQYLHerNIVHLDLKPQNILLTSEFPLGDIKLCDFG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 212 LSDFIKPGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWAT 290
Cdd:cd14106 157 ISRVIGEGEEIREILGTPDYVAPEILSYEPiSLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPEELFKD 236
                       250       260       270
                ....*....|....*....|....*....|..
gi 34098881 291 ISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14106 237 VSPLAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
55-323 1.27e-54

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 190.99  E-value: 1.27e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  55 SKDFHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDD 134
Cdd:COG0515   2 SALLLGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREARALARLN-HPNIVRVYDVGEEDG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 135 YVYIVMELCEGGELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSD 214
Cdd:COG0515  81 RPYLVMEYVEGESLADLL--RRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTP---DGRVKLIDFGIAR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 215 FIKPG--KRFHDIVGSAYYVAPEVLK-RRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATI 291
Cdd:COG0515 156 ALGGAtlTQTGTVVGTPGYMAPEQARgEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDL 235
                       250       260       270
                ....*....|....*....|....*....|..
gi 34098881 292 SDSAKDFVKKLLVKDPRARLTAAQALSHAWVR 323
Cdd:COG0515 236 PPALDAIVLRALAKDPEERYQSAAELAAALRA 267
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
56-322 2.52e-54

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: 184.07  E-value: 2.52e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  56 KDFHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLP---IAVEDVKREVQILIALSgHENVVQFHNAFED 132
Cdd:cd14194   1 ENVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSrrgVSREDIEREVSILKEIQ-HPNVITLHEVYEN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 133 DDYVYIVMELCEGGELLDRILSKKGnrYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSP-LKATDFG 211
Cdd:cd14194  80 KTDVILILELVAGGELFDFLAEKES--LTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKPrIKIIDFG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 212 LSDFIKPGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWAT 290
Cdd:cd14194 158 LAHKIDFGNEFKNIFGTPEFVAPEIVNYEPlGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSN 237
                       250       260       270
                ....*....|....*....|....*....|..
gi 34098881 291 ISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14194 238 TSALAKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
59-322 6.27e-54

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: 182.78  E-value: 6.27e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  59 HDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKmvlPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYI 138
Cdd:cd14114   1 YDHYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPH---ESDKETVRKEIQIMNQLH-HPKLINLHDAFEDDNEMVL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 139 VMELCEGGELLDRIlSKKGNRYSEKDAAVVVRQMLKvaGECHLH--GLVHRDMKPENFLFKSAQlDSPLKATDFGLSDFI 216
Cdd:cd14114  77 ILEFLSGGELFERI-AAEHYKMSEAEVINYMRQVCE--GLCHMHenNIVHLDIKPENIMCTTKR-SNEVKLIDFGLATHL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 217 KPGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDSA 295
Cdd:cd14114 153 DPKESVKVTTGTAEFAAPEIVEREPvGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDDSAFSGISEEA 232
                       250       260
                ....*....|....*....|....*..
gi 34098881 296 KDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14114 233 KDFIRKLLLADPNKRMTIHQALEHPWL 259
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
61-321 2.60e-53

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: 180.91  E-value: 2.60e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVlpiAVED-VKREVQILIALSgHENVVQFHNAFEDDDYVYIV 139
Cdd:cd14185   1 HYEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLK---GKEDmIESEILIIKSLS-HPNIVKLFEVYETEKEIYLI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGELLDRILskKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFK-SAQLDSPLKATDFGLSDFIKp 218
Cdd:cd14185  77 LEYVRGGDLFDAII--ESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQhNPDKSTTLKLADFGLAKYVT- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 gKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFW--DRTEDGIFKEVLRNKPDFSRKPWATISDSA 295
Cdd:cd14185 154 -GPIFTVCGTPTYVAPEILSEKGyGLEVDMWAAGVILYILLCGFPPFRspERDQEELFQIIQLGHYEFLPPYWDNISEAA 232
                       250       260
                ....*....|....*....|....*.
gi 34098881 296 KDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd14185 233 KDLISRLLVVDPEKRYTAKQVLQHPW 258
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
68-319 2.68e-53

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: 179.39  E-value: 2.68e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIavEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEGGE 147
Cdd:cd00180   1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLL--EELLREIEILKKLN-HPNIVKLYDVFETENFLYLVMEYCEGGS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 148 LLDrILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKPGKRFHDIVG 227
Cdd:cd00180  78 LKD-LLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDS---DGTVKLADFGLAKDLDSDDSLLKTTG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 228 ---SAYYVAPEVLKRRS-GPESDVWSIGVITYILlcgrrpfwdrtedgifkevlrnkpdfsrkpwatisDSAKDFVKKLL 303
Cdd:cd00180 154 gttPPYYAPPELLGGRYyGPKVDIWSLGVILYEL-----------------------------------EELKDLIRRML 198
                       250
                ....*....|....*.
gi 34098881 304 VKDPRARLTAAQALSH 319
Cdd:cd00180 199 QYDPKKRPSAKELLEH 214
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
58-322 2.75e-53

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: 182.14  E-value: 2.75e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  58 FHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKmvlpiavEDVKREVQILIALSGHENVVQFHNAFEDDDYVY 137
Cdd:cd14178   1 FTDGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSK-------RDPSEEIEILLRYGQHPNIITLKDVYDDGKFVY 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 138 IVMELCEGGELLDRILSKKGnrYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLF--KSAQLDSpLKATDFGLSDF 215
Cdd:cd14178  74 LVMELMRGGELLDRILRQKC--FSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYmdESGNPES-IRICDFGFAKQ 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 216 IKPGK-RFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFW---DRTEDGIFKEVLRNKPDFSRKPWAT 290
Cdd:cd14178 151 LRAENgLLMTPCYTANFVAPEVLKRQGyDAACDIWSLGILLYTMLAGFTPFAngpDDTPEEILARIGSGKYALSGGNWDS 230
                       250       260       270
                ....*....|....*....|....*....|..
gi 34098881 291 ISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14178 231 ISDAAKDIVSKMLHVDPHQRLTAPQVLRHPWI 262
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
56-323 6.10e-53

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: 180.58  E-value: 6.10e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  56 KDFHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLP---IAVEDVKREVQILIALSgHENVVQFHNAFED 132
Cdd:cd14195   1 SMVEDHYEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSrrgVSREEIEREVNILREIQ-HPNIITLHDIFEN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 133 DDYVYIVMELCEGGELLDRILSKKGnrYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSP-LKATDFG 211
Cdd:cd14195  80 KTDVVLILELVSGGELFDFLAEKES--LTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVPNPrIKLIDFG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 212 LSDFIKPGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWAT 290
Cdd:cd14195 158 IAHKIEAGNEFKNIFGTPEFVAPEIVNYEPlGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSN 237
                       250       260       270
                ....*....|....*....|....*....|...
gi 34098881 291 ISDSAKDFVKKLLVKDPRARLTAAQALSHAWVR 323
Cdd:cd14195 238 TSELAKDFIRRLLVKDPKKRMTIAQSLEHSWIK 270
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
60-322 8.54e-53

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: 179.50  E-value: 8.54e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMV--LPiaveDVKREVQILIALSgHENVVQFHNAFEDDDYVY 137
Cdd:cd14078   3 KYYELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKALGddLP----RVKTEIEALKNLS-HQHICRLYHVIETDNKIF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 138 IVMELCEGGELLDRILSKkgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIK 217
Cdd:cd14078  78 MVLEYCPGGELFDYIVAK--DRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDE---DQNLKLIDFGLCAKPK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 218 PGKRFH--DIVGSAYYVAPEVLKRRS--GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKpdFSRKPWatISD 293
Cdd:cd14078 153 GGMDHHleTCCGSPAYAAPELIQGKPyiGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGK--YEEPEW--LSP 228
                       250       260
                ....*....|....*....|....*....
gi 34098881 294 SAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14078 229 SSKLLLDQMLQVDPKKRITVKELLNHPWV 257
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
58-324 7.15e-52

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: 178.50  E-value: 7.15e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  58 FHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLP--IAVEDVKREVQILIALSgHENVVQFHNAFEDDDY 135
Cdd:cd14094   1 FEDVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSpgLSTEDLKREASICHMLK-HPHIVELLETYSSDGM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 136 VYIVMELCEGGELLDRILSK--KGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLS 213
Cdd:cd14094  80 LYMVFEFMDGADLCFEIVKRadAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 214 -DFIKPGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDgIFKEVLRNKPDFSRKPWATI 291
Cdd:cd14094 160 iQLGESGLVAGGRVGTPHFMAPEVVKREPyGKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYKMNPRQWSHI 238
                       250       260       270
                ....*....|....*....|....*....|...
gi 34098881 292 SDSAKDFVKKLLVKDPRARLTAAQALSHAWVRE 324
Cdd:cd14094 239 SESAKDLVRRMLMLDPAERITVYEALNHPWIKE 271
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
60-322 1.32e-51

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: 177.07  E-value: 1.32e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLP---IAVEDVKREVQILIALSgHENVVQFHNAFEDDDYV 136
Cdd:cd14196   5 DFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASrrgVSREEIEREVSILRQVL-HPNIITLHDVYENRTDV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 137 YIVMELCEGGELLDRILSKKGnrYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSP-LKATDFGLSDF 215
Cdd:cd14196  84 VLILELVSGGELFDFLAQKES--LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPhIKLIDFGLAHE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 216 IKPGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDS 294
Cdd:cd14196 162 IEDGVEFKNIFGTPEFVAPEIVNYEPlGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSHTSEL 241
                       250       260
                ....*....|....*....|....*...
gi 34098881 295 AKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14196 242 AKDFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
61-322 3.60e-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: 175.11  E-value: 3.60e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVlPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVM 140
Cdd:cd06627   1 NYQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIP-KSDLKSVMGEIDLLKKLN-HPNIVKYIGSVKTKDSLYIIL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCEGGELLDRIlsKKGNRYSEKDAAVVVRQMLKvaGECHLH--GLVHRDMKPENFLFKSAQLdspLKATDFGLSDFIKP 218
Cdd:cd06627  79 EYVENGSLASII--KKFGKFPESLVAVYIYQVLE--GLAYLHeqGVIHRDIKGANILTTKDGL---VKLADFGVATKLNE 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 -GKRFHDIVGSAYYVAPEVLkRRSGP--ESDVWSIGVITYILLCGRRPFWDRTE-DGIFKEVLRNKPDFsrkPwATISDS 294
Cdd:cd06627 152 vEKDENSVVGTPYWMAPEVI-EMSGVttASDIWSVGCTVIELLTGNPPYYDLQPmAALFRIVQDDHPPL---P-ENISPE 226
                       250       260
                ....*....|....*....|....*...
gi 34098881 295 AKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd06627 227 LRDFLLQCFQKDPTLRPSAKELLKHPWL 254
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
60-322 9.68e-51

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: 175.22  E-value: 9.68e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKmvlpiavEDVKREVQILIALSGHENVVQFHNAFEDDDYVYIV 139
Cdd:cd14175   1 DGYVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSK-------RDPSEEIEILLRYGQHPNIITLKDVYDDGKHVYLV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGELLDRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLF--KSAQLDSpLKATDFGLSDFIK 217
Cdd:cd14175  74 TELMRGGELLDKILRQK--FFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYvdESGNPES-LRICDFGFAKQLR 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 218 PGK-RFHDIVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCGRRPFWDRTEDG---IFKEVLRNKPDFSRKPWATIS 292
Cdd:cd14175 151 AENgLLMTPCYTANFVAPEVLKRQGYDEGcDIWSLGILLYTMLAGYTPFANGPSDTpeeILTRIGSGKFTLSGGNWNTVS 230
                       250       260       270
                ....*....|....*....|....*....|
gi 34098881 293 DSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14175 231 DAAKDLVSKMLHVDPHQRLTAKQVLQHPWI 260
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
66-323 1.25e-50

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: 174.83  E-value: 1.25e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKmvlPIAVEDVKREVQILIALSGHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd14174   8 ELLGEGAYAKVQGCVSLQNGKEYAVKIIEKNA---GHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLRG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLSDFIKPGKRFHDI 225
Cdd:cd14174  85 GSILAHIQKRK--HFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKVSPVKICDFDLGSGVKLNSACTPI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 226 V--------GSAYYVAPEVLKRRSGPES------DVWSIGVITYILLCGRRPF---------WDRTE------DGIFKEV 276
Cdd:cd14174 163 TtpelttpcGSAEYMAPEVVEVFTDEATfydkrcDLWSLGVILYIMLSGYPPFvghcgtdcgWDRGEvcrvcqNKLFESI 242
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 34098881 277 LRNKPDFSRKPWATISDSAKDFVKKLLVKDPRARLTAAQALSHAWVR 323
Cdd:cd14174 243 QEGKYEFPDKDWSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWVQ 289
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
51-321 3.79e-50

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: 173.23  E-value: 3.79e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  51 DFGYSKDFHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLD-KSKMVLPIAVEDVK----REVQILIALSGHENVVQ 125
Cdd:cd14181   1 DWAGAKEFYQKYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEvTAERLSPEQLEEVRsstlKEIHILRQVSGHPSIIT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 126 FHNAFEDDDYVYIVMELCEGGELLDRILSKKGnrYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPL 205
Cdd:cd14181  81 LIDSYESSTFIFLVFDLMRRGELFDYLTEKVT--LSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDD---QLHI 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 206 KATDFGLSDFIKPGKRFHDIVGSAYYVAPEVLK-------RRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLR 278
Cdd:cd14181 156 KLSDFGFSCHLEPGEKLRELCGTPGYLAPEILKcsmdethPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIME 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 34098881 279 NKPDFSRKPWATISDSAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd14181 236 GRYQFSSPEWDDRSSTVKDLISRLLVVDPEIRLTAEQALQHPF 278
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
58-324 4.06e-50

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: 173.18  E-value: 4.06e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  58 FHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLD--KSKMVLPIAVEDVK----REVQILIALSGHENVVQFHNAFE 131
Cdd:cd14182   1 FYEKYEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDitGGGSFSPEEVQELReatlKEIDILRKVSGHPNIIQLKDTYE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 132 DDDYVYIVMELCEGGELLDRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFG 211
Cdd:cd14182  81 TNTFFFLVFDLMKKGELFDYLTEKV--TLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDD---DMNIKLTDFG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 212 LSDFIKPGKRFHDIVGSAYYVAPEVLK-------RRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFS 284
Cdd:cd14182 156 FSCQLDPGEKLREVCGTPGYLAPEIIEcsmddnhPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFG 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 34098881 285 RKPWATISDSAKDFVKKLLVKDPRARLTAAQALSHAWVRE 324
Cdd:cd14182 236 SPEWDDRSDTVKDLISRFLVVQPQKRYTAEEALAHPFFQQ 275
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
62-322 4.43e-49

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: 169.82  E-value: 4.43e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVlPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVME 141
Cdd:cd14069   3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAP-GDCPENIKKEVCIQKMLS-HKNVVRFYGHRREGEFQYLFLE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELLDRILSKKGnrYSEKDAAVVVRQMLkvAGECHLH--GLVHRDMKPENFLfksaqLDSP--LKATDFGL-SDFI 216
Cdd:cd14069  81 YASGGELFDKIEPDVG--MPEDVAQFYFQQLM--AGLKYLHscGITHRDIKPENLL-----LDENdnLKISDFGLaTVFR 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 217 KPGKR--FHDIVGSAYYVAPEVLKRRS--GPESDVWSIGVITYILLCGRRPfWDR-TEDGIFKEVLRNKPDFSRKPWATI 291
Cdd:cd14069 152 YKGKErlLNKMCGTLPYVAPELLAKKKyrAEPVDVWSCGIVLFAMLAGELP-WDQpSDSCQEYSDWKENKKTYLTPWKKI 230
                       250       260       270
                ....*....|....*....|....*....|.
gi 34098881 292 SDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14069 231 DTAALSLLRKILTENPNKRITIEDIKKHPWY 261
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
55-322 7.52e-49

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: 171.74  E-value: 7.52e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  55 SKDFHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKmvlpiavEDVKREVQILIALSGHENVVQFHNAFEDDD 134
Cdd:cd14176  14 SIQFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK-------RDPTEEIEILLRYGQHPNIITLKDVYDDGK 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 135 YVYIVMELCEGGELLDRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLF--KSAQLDSpLKATDFGL 212
Cdd:cd14176  87 YVYVVTELMKGGELLDKILRQK--FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdESGNPES-IRICDFGF 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 213 SDFIKP-GKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDG---IFKEVLRNKPDFSRKP 287
Cdd:cd14176 164 AKQLRAeNGLLMTPCYTANFVAPEVLERQGyDAACDIWSLGVLLYTMLTGYTPFANGPDDTpeeILARIGSGKFSLSGGY 243
                       250       260       270
                ....*....|....*....|....*....|....*
gi 34098881 288 WATISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14176 244 WNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 278
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
60-322 9.58e-49

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: 169.95  E-value: 9.58e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTI--GKLLGHGQFGYTYVAIHRPNGDRVAVKRL-DKSKmvlpiavedVKREVQILIALSGHENVVQFHNAFEDD--- 133
Cdd:cd14171   4 EEYEVnwTQKLGTGISGPVRVCVKKSTGERFALKILlDRPK---------ARTEVRLHMMCSGHPNIVQIYDVYANSvqf 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 134 -------DYVYIVMELCEGGELLDRILSKKGnrYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLK 206
Cdd:cd14171  75 pgessprARLLIVMELMEGGELFDRISQHRH--FTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEDAPIK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 207 ATDFGLS-----DFIKPgkRFhdivgSAYYVAPEVL-------KRRSGPES-----------DVWSIGVITYILLCGRRP 263
Cdd:cd14171 153 LCDFGFAkvdqgDLMTP--QF-----TPYYVAPQVLeaqrrhrKERSGIPTsptpytydkscDMWSLGVIIYIMLCGYPP 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34098881 264 FWDRT-----EDGIFKEVLRNKPDFSRKPWATISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14171 226 FYSEHpsrtiTKDMKRKIMTGSYEFPEEEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
60-321 2.99e-48

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: 167.90  E-value: 2.99e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVedVKREVQILIALSgHENVVQFHNAFEDDDYVYIV 139
Cdd:cd14184   1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEHL--IENEVSILRRVK-HPNIIMLIEEMDTPAELYLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGELLDRILSKkgNRYSEKDAAVVVRQMlkVAGECHLHGL--VHRDMKPENFLF-KSAQLDSPLKATDFGLSDFI 216
Cdd:cd14184  78 MELVKGGDLFDAITSS--TKYTERDASAMVYNL--ASALKYLHGLciVHRDIKPENLLVcEYPDGTKSLKLGDFGLATVV 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 217 KpgKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFwdRTEDGI----FKEVLRNKPDFSRKPWATI 291
Cdd:cd14184 154 E--GPLYTVCGTPTYVAPEIIAETGyGLKVDIWAAGVITYILLCGFPPF--RSENNLqedlFDQILLGKLEFPSPYWDNI 229
                       250       260       270
                ....*....|....*....|....*....|
gi 34098881 292 SDSAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd14184 230 TDSAKELISHMLQVNVEARYTAEQILSHPW 259
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
58-333 4.06e-48

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: 169.07  E-value: 4.06e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  58 FHDHYTIG---KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKsKMVlpiavEDVKREVQILIALSGHENVVQFHNAFEDDD 134
Cdd:cd14179   2 FYQHYELDlkdKPLGEGSFSICRKCLHKKTNQEYAVKIVSK-RME-----ANTQREIAALKLCEGHPNIVKLHEVYHDQL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 135 YVYIVMELCEGGELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLSD 214
Cdd:cd14179  76 HTFLVMELLKGGELLERI--KKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESDNSEIKIIDFGFAR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 215 FIKPGKR-FHDIVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCGRRPFWDR-------TEDGIFKEVLRNKPDFSR 285
Cdd:cd14179 154 LKPPDNQpLKTPCFTLHYAAPELLNYNGYDEScDLWSLGVILYTMLSGQVPFQCHdksltctSAEEIMKKIKQGDFSFEG 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 34098881 286 KPWATISDSAKDFVKKLLVKDPRARLTAAQALSHAWVREGGNATDIPV 333
Cdd:cd14179 234 EAWKNVSQEAKDLIQGLLTVDPNKRIKMSGLRYNEWLQDGSQLSSNPL 281
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
62-313 6.67e-48

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: 167.39  E-value: 6.67e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVME 141
Cdd:cd05581   3 FKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRHIIKEKKVKYVTIEKEVLSRLA-HPGIVKLYYTFQDESKLYFVLE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELLDRIlsKKGNRYSEKDAAVVVRQMLkVAGEcHLH--GLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKPG 219
Cdd:cd05581  82 YAPNGDLLEYI--RKYGSLDEKCTRFYTAEIV-LALE-YLHskGIIHRDLKPENILLDE---DMHIKITDFGTAKVLGPD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 220 KRFHDI------------------VGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNK 280
Cdd:cd05581 155 SSPESTkgdadsqiaynqaraasfVGTAEYVSPELLNEKPaGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLE 234
                       250       260       270
                ....*....|....*....|....*....|...
gi 34098881 281 PDFSRKpwatISDSAKDFVKKLLVKDPRARLTA 313
Cdd:cd05581 235 YEFPEN----FPPDAKDLIQKLLVLDPSKRLGV 263
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
71-313 7.17e-48

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: 167.01  E-value: 7.17e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  71 GQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEGGELLd 150
Cdd:cd05579   4 GAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKNQVDSVLAERNILSQAQ-NPFVVKLYYSFQGKKNLYLVMEYLPGGDLY- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 151 RILSKKGnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDF--------------- 215
Cdd:cd05579  82 SLLENVG-ALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDA---NGHLKLTDFGLSKVglvrrqiklsiqkks 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 216 -IKPGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPwaTISD 293
Cdd:cd05579 158 nGAPEKEDRRIVGTPDYLAPEILLGQGhGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEWPEDP--EVSD 235
                       250       260
                ....*....|....*....|
gi 34098881 294 SAKDFVKKLLVKDPRARLTA 313
Cdd:cd05579 236 EAKDLISKLLTPDPEKRLGA 255
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
66-322 7.29e-48

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: 167.51  E-value: 7.29e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSkmvlPIAVED-VKREVQILIALSGHENVVQFHNAFEDDDYVYIVMELCE 144
Cdd:cd14173   8 EVLGEGAYARVQTCINLITNKEYAVKIIEKR----PGHSRSrVFREVEMLYQCQGHRNVLELIEFFEEEDKFYLVFEKMR 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 145 GGELLDRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLSDFIKPGKRFHD 224
Cdd:cd14173  84 GGSILSHIHRRR--HFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVSPVKICDFDLGSGIKLNSDCSP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 225 I--------VGSAYYVAPEVLKRRSGPES------DVWSIGVITYILLCGRRPF---------WDRTE------DGIFKE 275
Cdd:cd14173 162 IstpelltpCGSAEYMAPEVVEAFNEEASiydkrcDLWSLGVILYIMLSGYPPFvgrcgsdcgWDRGEacpacqNMLFES 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 34098881 276 VLRNKPDFSRKPWATISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14173 242 IQEGKYEFPEKDWAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
66-321 1.19e-47

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: 166.05  E-value: 1.19e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKmvLPIAVED-VKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCE 144
Cdd:cd14082   9 EVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLR--FPTKQESqLRNEVAILQQLS-HPGVVNLECMFETPERVFVVMEKLH 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 145 GgELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLSDFIkPGKRFH- 223
Cdd:cd14082  86 G-DMLEMILSSEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPFPQVKLCDFGFARII-GEKSFRr 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 224 DIVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCGRRPFwdrTEDGIFKEVLRNKP-DFSRKPWATISDSAKDFVKK 301
Cdd:cd14082 164 SVVGTPAYLAPEVLRNKGYNRSlDMWSVGVIIYVSLSGTFPF---NEDEDINDQIQNAAfMYPPNPWKEISPDAIDLINN 240
                       250       260
                ....*....|....*....|
gi 34098881 302 LLVKDPRARLTAAQALSHAW 321
Cdd:cd14082 241 LLQVKMRKRYSVDKSLSHPW 260
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
61-319 2.62e-47

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: 164.94  E-value: 2.62e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVlPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVM 140
Cdd:cd08215   1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMS-EKEREEALNEVKLLSKLK-HPNIVKYYESFEENGKLCIVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCEGGELLDRILSKKGNR--YSEKDAAVVVRQMLkvAGECHLHG--LVHRDMKPEN-FLFKsaqlDSPLKATDFGLSDF 215
Cdd:cd08215  79 EYADGGDLAQKIKKQKKKGqpFPEEQILDWFVQIC--LALKYLHSrkILHRDLKTQNiFLTK----DGVVKLGDFGISKV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 216 IKPGKRF-HDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPdfsrkpwATI-- 291
Cdd:cd08215 153 LESTTDLaKTVVGTPYYLSPELCENKPyNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQY-------PPIps 225
                       250       260       270
                ....*....|....*....|....*....|
gi 34098881 292 --SDSAKDFVKKLLVKDPRARLTAAQALSH 319
Cdd:cd08215 226 qySSELRDLVNSMLQKDPEKRPSANEILSS 255
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
62-322 3.96e-47

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: 164.51  E-value: 3.96e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMvlpiavEDVKR-----EVQILiALSGHENVVQFHNAFEDDDYV 136
Cdd:cd14074   5 YDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKL------DDVSKahlfqEVRCM-KLVQHPNVVRLYEVIDTQTKL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 137 YIVMELCEGGELLDRILsKKGNRYSEKDAAVVVRQMLKVAGECH-LHgLVHRDMKPENFLFKSAQldSPLKATDFGLSDF 215
Cdd:cd14074  78 YLILELGDGGDMYDYIM-KHENGLNEDLARKYFRQIVSAISYCHkLH-VVHRDLKPENVVFFEKQ--GLVKLTDFGFSNK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 216 IKPGKRFHDIVGSAYYVAPEVLKRRS--GPESDVWSIGVITYILLCGRRPFwDRTEDgifKEVLRNKPDFSRKPWATISD 293
Cdd:cd14074 154 FQPGEKLETSCGSLAYSAPEILLGDEydAPAVDIWSLGVILYMLVCGQPPF-QEAND---SETLTMIMDCKYTVPAHVSP 229
                       250       260
                ....*....|....*....|....*....
gi 34098881 294 SAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14074 230 ECKDLIRRMLIRDPKKRASLEEIENHPWL 258
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
58-322 4.62e-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: 165.57  E-value: 4.62e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  58 FHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKmvlpiavEDVKREVQILIALSGHENVVQFHNAFEDDDYVY 137
Cdd:cd14177   2 FTDVYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSK-------RDPSEEIEILMRYGQHPNIITLKDVYDDGRYVY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 138 IVMELCEGGELLDRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLF--KSAQLDSpLKATDFGLSdf 215
Cdd:cd14177  75 LVTELMKGGELLDRILRQK--FFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYmdDSANADS-IRICDFGFA-- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 216 ikpgKRFHDIVG-------SAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLR---NKPDFS 284
Cdd:cd14177 150 ----KQLRGENGllltpcyTANFVAPEVLMRQGyDAACDIWSLGVLLYTMLAGYTPFANGPNDTPEEILLRigsGKFSLS 225
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 34098881 285 RKPWATISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14177 226 GGNWDTVSDAAKDLLSHMLHVDPHQRYTAEQVLKHSWI 263
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
62-322 6.06e-47

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: 165.30  E-value: 6.06e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPN-GDRVAVKRLDKSKM----VLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYV 136
Cdd:cd14096   3 YRLINKIGEGAFSNVYKAVPLRNtGKPVAIKVVRKADLssdnLKGSSRANILKEVQIMKRLS-HPNIVKLLDFQESDEYY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 137 YIVMELCEGGELLDRILskKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLF----------KSAQLDSP-- 204
Cdd:cd14096  82 YIVLELADGGEIFHQIV--RLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFepipfipsivKLRKADDDet 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 205 ------------------LKATDFGLSDFIKPgKRFHDIVGSAYYVAPEVLK-RRSGPESDVWSIGVITYILLCGRRPFW 265
Cdd:cd14096 160 kvdegefipgvggggigiVKLADFGLSKQVWD-SNTKTPCGTVGYTAPEVVKdERYSKKVDMWALGCVLYTLLCGFPPFY 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 34098881 266 DRTEDGIFKEVLRNKPDFSRKPWATISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14096 239 DESIETLTEKISRGDYTFLSPWWDEISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
62-322 7.41e-47

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: 163.84  E-value: 7.41e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVlPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVME 141
Cdd:cd14072   2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLN-PSSLQKLFREVRIMKILN-HPNIVKLFEVIETEKTLYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELLDRILSKkgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKPGKR 221
Cdd:cd14072  80 YASGGEVFDYLVAH--GRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDA---DMNIKIADFGFSNEFTPGNK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 222 FHDIVGSAYYVAPEVL--KRRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKpdfSRKPWaTISDSAKDFV 299
Cdd:cd14072 155 LDTFCGSPPYAAPELFqgKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGK---YRIPF-YMSTDCENLL 230
                       250       260
                ....*....|....*....|...
gi 34098881 300 KKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14072 231 KKFLVLNPSKRGTLEQIMKDRWM 253
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
62-321 1.45e-46

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: 162.95  E-value: 1.45e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVlPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVME 141
Cdd:cd14071   2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLD-EENLKKIYREVQIMKMLN-HPHIIKLYQVMETKDMLYLVTE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELLDrILSKKGnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLfksaqLDSPL--KATDFGLSDFIKPG 219
Cdd:cd14071  80 YASNGEIFD-YLAQHG-RMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLL-----LDANMniKIADFGFSNFFKPG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 220 KRFHDIVGSAYYVAPEVL--KRRSGPESDVWSIGVITYILLCGRRPFwdrteDGIFKEVLRNK--------PDFsrkpwa 289
Cdd:cd14071 153 ELLKTWCGSPPYAAPEVFegKEYEGPQLDIWSLGVVLYVLVCGALPF-----DGSTLQTLRDRvlsgrfriPFF------ 221
                       250       260       270
                ....*....|....*....|....*....|..
gi 34098881 290 tISDSAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd14071 222 -MSTDCEHLIRRMLVLDPSKRLTIEQIKKHKW 252
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
62-322 2.73e-46

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: 162.17  E-value: 2.73e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVME 141
Cdd:cd14073   3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQDMVRIRREIEIMSSLN-HPHIIRIYEVFENKDKIVIVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELLDRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKPGKR 221
Cdd:cd14073  82 YASGGELYDYISERR--RLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQ---NGNAKIADFGLSNLYSKDKL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 222 FHDIVGSAYYVAPEVLKRR--SGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKpdfSRKPwATISDsAKDFV 299
Cdd:cd14073 157 LQTFCGSPLYASPEIVNGTpyQGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGD---YREP-TQPSD-ASGLI 231
                       250       260
                ....*....|....*....|...
gi 34098881 300 KKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14073 232 RWMLTVNPKRRATIEDIANHWWV 254
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
64-324 9.39e-46

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: 161.22  E-value: 9.39e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  64 IGKLLGHGQFGYTYVAIHRPNGDRVAVKrldkskmVLPIAVEDVKR-----EVQILIAlSGHENVVQFHNAFEDDDYVYI 138
Cdd:cd06623   5 RVKVLGQGSSGVVYKVRHKPTGKIYALK-------KIHVDGDEEFRkqllrELKTLRS-CESPYVVKCYGAFYKEGEISI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 139 VMELCEGGELlDRILSKKGNrYSEKDAAVVVRQMLKvaGECHLHG---LVHRDMKPENFLFKSaqlDSPLKATDFGLSDF 215
Cdd:cd06623  77 VLEYMDGGSL-ADLLKKVGK-IPEPVLAYIARQILK--GLDYLHTkrhIIHRDIKPSNLLINS---KGEVKIADFGISKV 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 216 IKPG-KRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFkEVLRNKPDFSRKPW--ATI 291
Cdd:cd06623 150 LENTlDQCNTFVGTVTYMSPERIQGESySYAADIWSLGLTLLECALGKFPFLPPGQPSFF-ELMQAICDGPPPSLpaEEF 228
                       250       260       270
                ....*....|....*....|....*....|...
gi 34098881 292 SDSAKDFVKKLLVKDPRARLTAAQALSHAWVRE 324
Cdd:cd06623 229 SPEFRDFISACLQKDPKKRPSAAELLQHPFIKK 261
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
60-322 1.28e-45

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: 160.93  E-value: 1.28e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGK-LLGHGQFGYTYVAIHRPNGDRVAVKRLDKSkmvlPIAvedvKREVQILIALSGHENVVQ----FHNAFEDDD 134
Cdd:cd14172   3 DDYKLSKqVLGLGVNGKVLECFHRRTGQKCALKLLYDS----PKA----RREVEHHWRASGGPHIVHildvYENMHHGKR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 135 YVYIVMELCEGGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLSD 214
Cdd:cd14172  75 CLLIIMECMEGGELFSRIQERGDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKDAVLKLTDFGFAK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 215 FIKPGKRFHDIVGSAYYVAPEVLkrrsGPES-----DVWSIGVITYILLCGRRPFWDRT----EDGIFKEVLRNKPDFSR 285
Cdd:cd14172 155 ETTVQNALQTPCYTPYYVAPEVL----GPEKydkscDMWSLGVIMYILLCGFPPFYSNTgqaiSPGMKRRIRMGQYGFPN 230
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 34098881 286 KPWATISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14172 231 PEWAEVSEEAKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
68-321 1.41e-45

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: 160.08  E-value: 1.41e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKmVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEGGE 147
Cdd:cd14009   1 IGRGSFATVWKGRHKQTGEVVAIKEISRKK-LNKKLQENLESEIAILKSIK-HPNIVRLYDVQKTEDFIYLVLEYCAGGD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 148 LLDRIlsKKGNRYSEKDAAVVVRQM---LKVageCHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLSDFIKPGKRFHD 224
Cdd:cd14009  79 LSQYI--RKRGRLPEAVARHFMQQLasgLKF---LRSKNIIHRDLKPQNLLLSTSGDDPVLKIADFGFARSLQPASMAET 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 225 IVGSAYYVAPEVLK-RRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDSAKDFVKKLL 303
Cdd:cd14009 154 LCGSPLYMAPEILQfQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSDAVIPFPIAAQLSPDCKDLLRRLL 233
                       250
                ....*....|....*...
gi 34098881 304 VKDPRARLTAAQALSHAW 321
Cdd:cd14009 234 RRDPAERISFEEFFAHPF 251
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
57-322 1.52e-45

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: 160.86  E-value: 1.52e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  57 DFHDHYTIGKL-LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEdVKREVQILIALSGHENVVQFHNAFEDDDY 135
Cdd:cd14198   4 NFNNFYILTSKeLGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAE-ILHEIAVLELAKSNPRVVNLHEVYETTSE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 136 VYIVMELCEGGELLDRILSKKGNRYSEKDAAVVVRQMLKvaGECHLH--GLVHRDMKPENFLFKSAQLDSPLKATDFGLS 213
Cdd:cd14198  83 IILILEYAAGGEIFNLCVPDLAEMVSENDIIRLIRQILE--GVYYLHqnNIVHLDLKPQNILLSSIYPLGDIKIVDFGMS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 214 DFIKPGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATIS 292
Cdd:cd14198 161 RKIGHACELREIMGTPEYLAPEILNYDPiTTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNVDYSEETFSSVS 240
                       250       260       270
                ....*....|....*....|....*....|
gi 34098881 293 DSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14198 241 QLATDFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
58-333 1.78e-45

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: 161.96  E-value: 1.78e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  58 FHDHYTI---GKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKsKMVlpiavEDVKREVQILIALSGHENVVQFHNAFEDDD 134
Cdd:cd14180   1 FFQCYELdleEPALGEGSFSVCRKCRHRQSGQEYAVKIISR-RME-----ANTQREVAALRLCQSHPNIVALHEVLHDQY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 135 YVYIVMELCEGGELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLSD 214
Cdd:cd14180  75 HTYLVMELLRGGELLDRI--KKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDGAVLKVIDFGFAR 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 215 FIKPGKR-FHDIVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCGRRPFWDRTEDG-------IFKEVLRNKPDFSR 285
Cdd:cd14180 153 LRPQGSRpLQTPCFTLQYAAPELFSNQGYDEScDLWSLGVILYTMLSGQVPFQSKRGKMfhnhaadIMHKIKEGDFSLEG 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 34098881 286 KPWATISDSAKDFVKKLLVKDPRARLTAAQALSHAWVREGGNATDIPV 333
Cdd:cd14180 233 EAWKGVSEEAKDLVRGLLTVDPAKRLKLSELRESDWLQGGSALSSTPL 280
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
60-324 2.17e-45

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 160.82  E-value: 2.17e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIV 139
Cdd:cd05580   1 DDFEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIIKLKQVEHVLNEKRILSEVR-HPFIVNLLGSFQDDRNLYMV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGELLDRIlsKKGNRYSEKDAAVVVRQMLkVAGEcHLH--GLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIK 217
Cdd:cd05580  80 MEYVPGGELFSLL--RRSGRFPNDVAKFYAAEVV-LALE-YLHslDIVYRDLKPENLLLDS---DGHIKITDFGFAKRVK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 218 pgKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRkpwaTISDSAK 296
Cdd:cd05580 153 --DRTYTLCGTPEYLAPEIILSKGhGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFPS----FFDPDAK 226
                       250       260       270
                ....*....|....*....|....*....|...
gi 34098881 297 DFVKKLLVKDPRARL-----TAAQALSHAWVRE 324
Cdd:cd05580 227 DLIKRLLVVDLTKRLgnlknGVEDIKNHPWFAG 259
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
62-322 3.87e-45

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: 159.38  E-value: 3.87e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKmvlpiAVEDV-----KREVQILIALSgHENVVQFHNAFEDDDYV 136
Cdd:cd14162   2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKK-----APEDYlqkflPREIEVIKGLK-HPNLICFYEAIETTSRV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 137 YIVMELCEGGELLDRILSKKGnrYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGL---S 213
Cdd:cd14162  76 YIIMELAENGDLLDYIRKNGA--LPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDK---NNNLKITDFGFargV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 214 DFIKPGKRF--HDIVGSAYYVAPEVLkrRSGPE----SDVWSIGVITYILLCGRRPFWDRTEDGIFKEVlRNKPDFSRKP 287
Cdd:cd14162 151 MKTKDGKPKlsETYCGSYAYASPEIL--RGIPYdpflSDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQV-QRRVVFPKNP 227
                       250       260       270
                ....*....|....*....|....*....|....*
gi 34098881 288 waTISDSAKDFVKKLLVKDPRaRLTAAQALSHAWV 322
Cdd:cd14162 228 --TVSEECKDLILRMLSPVKK-RITIEEIKRDPWF 259
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
58-322 4.42e-45

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: 159.21  E-value: 4.42e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  58 FHDHYTIG-KLLGHGQFGYTYVAIHRPNGDRVAVKrldkskmVLPIAvEDVKREVQILIALSgHENVVQFHNAFEDDDY- 135
Cdd:cd14109   1 VRELYEIGeEDEKRAAQGAPFHVTERSTGRNFLAQ-------LRYGD-PFLMREVDIHNSLD-HPNIVQMHDAYDDEKLa 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 136 VYIVMELCEGGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKsaqlDSPLKATDFGLSDF 215
Cdd:cd14109  72 VTVIDNLASTIELVRDNLLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQ----DDKLKLADFGQSRR 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 216 IKPGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDS 294
Cdd:cd14109 148 LLRGKLTTLIYGSPEFVSPEIVNSYPvTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKWSFDSSPLGNISDD 227
                       250       260
                ....*....|....*....|....*...
gi 34098881 295 AKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14109 228 ARDFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
66-322 4.93e-45

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: 159.36  E-value: 4.93e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVlpiAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd14192  10 EVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAK---EREEVKNEINIMNQLN-HVNLIQLYDAFESKTNLTLIMEYVDG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRILSKKGNrYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaQLDSPLKATDFGLSDFIKPGKRFHDI 225
Cdd:cd14192  86 GELFDRITDESYQ-LTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVN-STGNQIKIIDFGLARRYKPREKLKVN 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 226 VGSAYYVAPEVLKRR--SGPeSDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDSAKDFVKKLL 303
Cdd:cd14192 164 FGTPEFLAPEVVNYDfvSFP-TDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDAEAFENLSEEAKDFISRLL 242
                       250
                ....*....|....*....
gi 34098881 304 VKDPRARLTAAQALSHAWV 322
Cdd:cd14192 243 VKEKSCRMSATQCLKHEWL 261
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
60-322 5.65e-45

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: 158.92  E-value: 5.65e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGK--LLGHGQFGYTYVAIHRPNGDRVAVKRLdksKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVY 137
Cdd:cd14193   2 SYYNVNKeeILGGGRFGQVHKCEEKSSGLKLAAKII---KARSQKEKEEVKNEIEVMNQLN-HANLIQLYDAFESRNDIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 138 IVMELCEGGELLDRILSKKGNrYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSpLKATDFGLSDFIK 217
Cdd:cd14193  78 LVMEYVDGGELFDRIIDENYN-LTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSREANQ-VKIIDFGLARRYK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 218 PGKRFHDIVGSAYYVAPEVLKRR--SGPeSDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDSA 295
Cdd:cd14193 156 PREKLRVNFGTPEFLAPEVVNYEfvSFP-TDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFEDEEFADISEEA 234
                       250       260
                ....*....|....*....|....*..
gi 34098881 296 KDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14193 235 KDFISKLLIKEKSWRMSASEALKHPWL 261
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
60-319 5.93e-45

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: 159.06  E-value: 5.93e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMvlPIAVEDVKREVQILiALSGHENVVQFHNAFEDDDYVYIV 139
Cdd:cd06610   1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLEKC--QTSMDELRKEIQAM-SQCNHPNVVSYYTSFVVGDELWLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGELLDRILSK-KGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFI-K 217
Cdd:cd06610  78 MPLLSGGSLLDIMKSSyPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGE---DGSVKIADFGVSASLaT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 218 PG----KRFHDIVGSAYYVAPEVLKRRSG--PESDVWSIGvITYI-LLCGRRPFWDRTEDGIFKEVLRNKP-----DFSR 285
Cdd:cd06610 155 GGdrtrKVRKTFVGTPCWMAPEVMEQVRGydFKADIWSFG-ITAIeLATGAAPYSKYPPMKVLMLTLQNDPpsletGADY 233
                       250       260       270
                ....*....|....*....|....*....|....
gi 34098881 286 KPWatiSDSAKDFVKKLLVKDPRARLTAAQALSH 319
Cdd:cd06610 234 KKY---SKSFRKMISLCLQKDPSKRPTAEELLKH 264
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
62-322 1.05e-44

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: 157.93  E-value: 1.05e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVED-----VKREVQILIAL--SGHENVVQFHNAFEDDD 134
Cdd:cd14004   2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERILVDTWVRDrklgtVPLEIHILDTLnkRSHPNIVKLLDFFEDDE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 135 YVYIVMEL-CEGGELLDRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLS 213
Cdd:cd14004  82 FYYLVMEKhGSGMDLFDFIERKP--NMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDG---NGTIKLIDFGSA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 214 DFIKPGKrFHDIVGSAYYVAPEVL--KRRSGPESDVWSIGVITYILLCGRRPFWDrtedgiFKEVLrnKPDFsrKPWATI 291
Cdd:cd14004 157 AYIKSGP-FDTFVGTIDYAAPEVLrgNPYGGKEQDIWALGVLLYTLVFKENPFYN------IEEIL--EADL--RIPYAV 225
                       250       260       270
                ....*....|....*....|....*....|.
gi 34098881 292 SDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14004 226 SEDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
62-322 4.39e-44

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: 156.52  E-value: 4.39e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAV-EDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVM 140
Cdd:cd14070   4 YLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKDSYVtKNLRREGRIQQMIR-HPNITQLLDILETENSYYLVM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCEGGELLDRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSD---FIK 217
Cdd:cd14070  83 ELCPGGNLMHRIYDKK--RLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDE---NDNIKLIDFGLSNcagILG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 218 PGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFwdRTEDGIFKEVLRNKPDFSRKPWAT-ISDSA 295
Cdd:cd14070 158 YSDPFSTQCGSPAYAAPELLARKKyGPKVDVWSIGVNMYAMLTGTLPF--TVEPFSLRALHQKMVDKEMNPLPTdLSPGA 235
                       250       260
                ....*....|....*....|....*..
gi 34098881 296 KDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14070 236 ISFLRSLLEPDPLKRPNIKQALANRWL 262
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
68-311 6.51e-44

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


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 156.23  E-value: 6.51e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEGGE 147
Cdd:cd05572   1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQQEHIFSEKEILEECN-SPFIVKLYRTFKDKKYLYMLMEYCLGGE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 148 LLDrILSKKGNrYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLfksaqLDSP--LKATDFGLSDFIKPGKRFHDI 225
Cdd:cd05572  80 LWT-ILRDRGL-FDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLL-----LDSNgyVKLVDFGFAKKLGSGRKTWTF 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 226 VGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTED--GIFKEVLR--NKPDFSRKpwatISDSAKDFVK 300
Cdd:cd05572 153 CGTPEYVAPEIILNKGyDFSVDYWSLGILLYELLTGRPPFGGDDEDpmKIYNIILKgiDKIEFPKY----IDKNAKNLIK 228
                       250
                ....*....|.
gi 34098881 301 KLLVKDPRARL 311
Cdd:cd05572 229 QLLRRNPEERL 239
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
62-322 7.15e-44

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: 155.79  E-value: 7.15e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVME 141
Cdd:cd14186   3 FKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAGMVQRVRNEVEIHCQLK-HPSILELYNYFEDSNYVYLVLE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGElLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIK-PGK 220
Cdd:cd14186  82 MCHNGE-MSRYLKNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTR---NMNIKIADFGLATQLKmPHE 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 221 RFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPF-WDRTEDGIFKEVLRN--KPDFsrkpwatISDSAK 296
Cdd:cd14186 158 KHFTMCGTPNYISPEIATRSAhGLESDVWSLGCMFYTLLVGRPPFdTDTVKNTLNKVVLADyeMPAF-------LSREAQ 230
                       250       260
                ....*....|....*....|....*.
gi 34098881 297 DFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14186 231 DLIHQLLRKNPADRLSLSSVLDHPFM 256
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
55-322 1.12e-43

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: 155.86  E-value: 1.12e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  55 SKDFHDHYTI--GKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEdVKREVQILIALSGHENVVQFHNAFED 132
Cdd:cd14197   2 SEPFQERYSLspGRELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDCRME-IIHEIAVLELAQANPWVINLHEVYET 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 133 DDYVYIVMELCEGGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPL---KATD 209
Cdd:cd14197  81 ASEMILVLEYAAGGEIFNQCVADREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTS---ESPLgdiKIVD 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 210 FGLSDFIKPGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPW 288
Cdd:cd14197 158 FGLSRILKNSEELREIMGTPEYVAPEILSYEPiSTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSEEEF 237
                       250       260       270
                ....*....|....*....|....*....|....
gi 34098881 289 ATISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14197 238 EHLSESAIDFIKTLLIKKPENRATAEDCLKHPWL 271
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
60-322 1.12e-43

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: 155.92  E-value: 1.12e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVedVKREVQILIALSgHENVVQFHNAFEDDDYVYIV 139
Cdd:cd14183   6 ERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEHM--IQNEVSILRRVK-HPNIVLLIEEMDMPTELYLV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGELLDRILSkkGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDS-PLKATDFGLSDFIKp 218
Cdd:cd14183  83 MELVKGGDLFDAITS--TNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQDGSkSLKLGDFGLATVVD- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 gKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTED--GIFKEVLRNKPDFSRKPWATISDSA 295
Cdd:cd14183 160 -GPLYTVCGTPTYVAPEIIAETGyGLKVDIWAAGVITYILLCGFPPFRGSGDDqeVLFDQILMGQVDFPSPYWDNVSDSA 238
                       250       260
                ....*....|....*....|....*..
gi 34098881 296 KDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14183 239 KELITMMLQVDVDQRYSALQVLEHPWV 265
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
56-321 3.53e-43

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: 156.68  E-value: 3.53e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  56 KDFHdhytIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSGhENVVQFHNAFEDDDY 135
Cdd:cd05573   1 DDFE----VIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREQIAHVRAERDILADADS-PWIVRLHYAFQDEDH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 136 VYIVMELCEGGELLdRILSKKGnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLS-D 214
Cdd:cd05573  76 LYLVMEYMPGGDLM-NLLIKYD-VFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDA---DGHIKLADFGLCtK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 215 FIKPGKR-----------------------------FHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPF 264
Cdd:cd05573 151 MNKSGDResylndsvntlfqdnvlarrrphkqrrvrAYSAVGTPDYIAPEVLRGTGyGPECDWWSLGVILYEMLYGFPPF 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 34098881 265 WDRTEDGIFKEVLRNKPDFSRKPWATISDSAKDFVKKLLvKDPRARLT-AAQALSHAW 321
Cdd:cd05573 231 YSDSLVETYSKIMNWKESLVFPDDPDVSPEAIDLIRRLL-CDPEDRLGsAEEIKAHPF 287
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
60-322 4.81e-43

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: 154.03  E-value: 4.81e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDK--SKMVLPIAvedvKREVQILiALSGHENVVQFHNAFEDDDYVY 137
Cdd:cd14088   1 DRYDLGQVIKTEEFCEIFRAKDKTTGKLYTCKKFLKrdGRKVRKAA----KNEINIL-KMVKHPNILQLVDVFETRKEYF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 138 IVMELCEGGELLDRILSKkgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLSDFik 217
Cdd:cd14088  76 IFLELATGREVFDWILDQ--GYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYNRLKNSKIVISDFHLAKL-- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 218 PGKRFHDIVGSAYYVAPEVLKR-RSGPESDVWSIGVITYILLCGRRPFWDRTED--------GIFKEVLRNKPDFSRKPW 288
Cdd:cd14088 152 ENGLIKEPCGTPEYLAPEVVGRqRYGRPVDCWAIGVIMYILLSGNPPFYDEAEEddyenhdkNLFRKILAGDYEFDSPYW 231
                       250       260       270
                ....*....|....*....|....*....|....
gi 34098881 289 ATISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14088 232 DDISQAAKDLVTRLMEVEQDQRITAEEAISHEWI 265
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
62-322 1.92e-42

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: 152.22  E-value: 1.92e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVK----------RLDKSKMVLPIAVEDVK--REVqILIALSGHENVVQFHNA 129
Cdd:cd14077   3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKiiprasnaglKKEREKRLEKEISRDIRtiREA-ALSSLLNHPHICRLRDF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 130 FEDDDYVYIVMELCEGGELLDRILSKkgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAqldSPLKATD 209
Cdd:cd14077  82 LRTPNHYYMLFEYVDGGQLLDYIISH--GKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKS---GNIKIID 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 210 FGLSDFIKPGKRFHDIVGSAYYVAPEVLKRR--SGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSrkp 287
Cdd:cd14077 157 FGLSNLYDPRRLLRTFCGSLYFAAPELLQAQpyTGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVEYP--- 233
                       250       260       270
                ....*....|....*....|....*....|....*
gi 34098881 288 wATISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14077 234 -SYLSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
62-321 3.83e-42

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: 151.92  E-value: 3.83e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLdKSK-------MVLpiavedvkREVQILIALSGHENVVQFHNAFEDDD 134
Cdd:cd07830   1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKM-KKKfysweecMNL--------REVKSLRKLNEHPNIVKLKEVFREND 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 135 YVYIVMELCEgGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLdspLKATDFGLSD 214
Cdd:cd07830  72 ELYFVFEYME-GNLYQLMKDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEV---VKIADFGLAR 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 215 FIKPGKRFHDIVGSAYYVAPEVLKRRSGPES--DVWSIGVITYILLCGRRPFWDRTE-DGIFK--EVL--RNKPDFSR-- 285
Cdd:cd07830 148 EIRSRPPYTDYVSTRWYRAPEILLRSTSYSSpvDIWALGCIMAELYTLRPLFPGSSEiDQLYKicSVLgtPTKQDWPEgy 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 34098881 286 -------------------KPWATISDSAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd07830 228 klasklgfrfpqfaptslhQLIPNASPEAIDLIKDMLRWDPKKRPTASQALQHPY 282
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
65-322 4.78e-42

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: 151.30  E-value: 4.78e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  65 GKLLGHGQFGYTYVAIHRPNGDRVAVK--RLDKSKmvlPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMEL 142
Cdd:cd06626   5 GNKIGEGTFGKVYTAVNLDTGELMAMKeiRFQDND---PKTIKEIADEMKVLEGLD-HPNLVRYYGVEVHREEVYIFMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 143 CEGGELLDriLSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKPGK-- 220
Cdd:cd06626  81 CQEGTLEE--LLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDS---NGLIKLGDFGSAVKLKNNTtt 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 221 ----RFHDIVGSAYYVAPEVLK--RRSGPE--SDVWSIGVITYILLCGRRPfWDRTEDG---IFKEVLRNKPDFSrkPWA 289
Cdd:cd06626 156 mapgEVNSLVGTPAYMAPEVITgnKGEGHGraADIWSLGCVVLEMATGKRP-WSELDNEwaiMYHVGMGHKPPIP--DSL 232
                       250       260       270
                ....*....|....*....|....*....|...
gi 34098881 290 TISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd06626 233 QLSPEGKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
66-323 2.38e-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: 149.17  E-value: 2.38e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSGHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd05611   2 KPISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQVTNVKAERAIMMIQGESPYVAKLYYSFQSKDYLYLVMEYLNG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELldRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAqldSPLKATDFGLSDFIKPGKRFHDI 225
Cdd:cd05611  82 GDC--ASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQT---GHLKLTDFGLSRNGLEKRHNKKF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 226 VGSAYYVAPEVLKRRSGPE-SDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDSAKDFVKKLLV 304
Cdd:cd05611 157 VGTPDYLAPETILGVGDDKmSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPEEVKEFCSPEAVDLINRLLC 236
                       250       260
                ....*....|....*....|..
gi 34098881 305 KDPRARLTA---AQALSHAWVR 323
Cdd:cd05611 237 MDPAKRLGAngyQEIKSHPFFK 258
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
66-322 3.85e-41

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: 148.53  E-value: 3.85e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKmvlPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd14190  10 EVLGGGKFGKVHTCTEKRTGLKLAAKVINKQN---SKDKEMVLLEIQVMNQLN-HRNLIQLYEAIETPNEIVLFMEYVEG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRILSKKgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQlDSPLKATDFGLSDFIKPGKRFHDI 225
Cdd:cd14190  86 GELFERIVDED-YHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRT-GHQVKIIDFGLARRYNPREKLKVN 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 226 VGSAYYVAPEVLK-RRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDSAKDFVKKLLV 304
Cdd:cd14190 164 FGTPEFLSPEVVNyDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMGNWYFDEETFEHVSDEAKDFVSNLII 243
                       250
                ....*....|....*...
gi 34098881 305 KDPRARLTAAQALSHAWV 322
Cdd:cd14190 244 KERSARMSATQCLKHPWL 261
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
62-325 4.72e-41

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: 148.86  E-value: 4.72e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVK--RLDKSKMVLpiavedVKREVQILIALSgHENVVQFHNAFEDDDYVYIV 139
Cdd:cd14104   2 YMIAEELGRGQFGIVHRCVETSSKKTYMAKfvKVKGADQVL------VKKEISILNIAR-HRNILRLHESFESHEELVMI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGELLDRIlSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaQLDSPLKATDFGLSDFIKPG 219
Cdd:cd14104  75 FEFISGVDIFERI-TTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCT-RRGSYIKIIEFGQSRQLKPG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 220 KRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDSAKDF 298
Cdd:cd14104 153 DKFRLQYTSAEFYAPEVHQHESvSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDDEAFKNISIEALDF 232
                       250       260
                ....*....|....*....|....*..
gi 34098881 299 VKKLLVKDPRARLTAAQALSHAWVREG 325
Cdd:cd14104 233 VDRLLVKERKSRMTAQEALNHPWLKQG 259
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
68-313 8.58e-41

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: 147.88  E-value: 8.58e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVK----REVQILIALSGHENVVQFHNAFEDDDYVYIVMELC 143
Cdd:cd13993   8 IGEGAYGVVYLAVDLRTGRKYAIKCLYKSGPNSKDGNDFQKlpqlREIDLHRRVSRHPNIITLHDVFETEVAIYIVLEYC 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 144 EGGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFksAQLDSPLKATDFGLS--DFIKPGKR 221
Cdd:cd13993  88 PNGDLFEAITENRIYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILL--SQDEGTVKLCDFGLAttEKISMDFG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 222 fhdiVGSAYYVAPEVL--KRRSGPE-----SDVWSIGVITYILLCGRRPFWDRTE-DGIFKEVLRNKPDFSRKpWATISD 293
Cdd:cd13993 166 ----VGSEFYMAPECFdeVGRSLKGypcaaGDIWSLGIILLNLTFGRNPWKIASEsDPIFYDYYLNSPNLFDV-ILPMSD 240
                       250       260
                ....*....|....*....|
gi 34098881 294 SAKDFVKKLLVKDPRARLTA 313
Cdd:cd13993 241 DFYNLLRQIFTVNPNNRILL 260
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
60-336 1.27e-40

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: 148.64  E-value: 1.27e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSkmvlPIAvedvKREVQILIALSGHENVVQ----FHNAFEDDDY 135
Cdd:cd14170   2 DYKVTSQVLGLGINGKVLQIFNKRTQEKFALKMLQDC----PKA----RREVELHWRASQCPHIVRivdvYENLYAGRKC 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 136 VYIVMELCEGGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLSDF 215
Cdd:cd14170  74 LLIVMECLDGGELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGFAKE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 216 IKPGKRFHDIVGSAYYVAPEVLkrrsGPES-----DVWSIGVITYILLCGRRPFWDR----TEDGIFKEVLRNKPDFSRK 286
Cdd:cd14170 154 TTSHNSLTTPCYTPYYVAPEVL----GPEKydkscDMWSLGVIMYILLCGYPPFYSNhglaISPGMKTRIRMGQYEFPNP 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 34098881 287 PWATISDSAKDFVKKLLVKDPRARLTAAQALSHAWVREGGNATDIPVDIS 336
Cdd:cd14170 230 EWSEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQSTKVPQTPLHTS 279
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
60-322 1.42e-40

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: 147.07  E-value: 1.42e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLdksKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIV 139
Cdd:cd14191   2 DFYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFF---KAYSAKEKENIRQEISIMNCLH-HPKLVQCVDAFEEKANIVMV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGELLDRILSKKgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaQLDSPLKATDFGLSDFIKPG 219
Cdd:cd14191  78 LEMVSGGELFERIIDED-FELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVN-KTGTKIKLIDFGLARRLENA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 220 KRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDSAKDF 298
Cdd:cd14191 156 GSLKVLFGTPEFVAPEVINYEPiGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDF 235
                       250       260
                ....*....|....*....|....
gi 34098881 299 VKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14191 236 ISNLLKKDMKARLTCTQCLQHPWL 259
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
62-319 1.07e-39

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: 144.68  E-value: 1.07e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVME 141
Cdd:cd14189   3 YCKGRLLGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKPHQREKIVNEIELHRDLH-HKHVVKFSHHFEDAENIYIFLE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELLDriLSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKPG-K 220
Cdd:cd14189  82 LCSRKSLAH--IWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINE---NMELKVGDFGLAARLEPPeQ 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 221 RFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFwdRTEDgiFKEVLRNKPDFSRKPWATISDSAKDFV 299
Cdd:cd14189 157 RKKTICGTPNYLAPEVLLRQGhGPESDVWSLGCVMYTLLCGNPPF--ETLD--LKETYRCIKQVKYTLPASLSLPARHLL 232
                       250       260
                ....*....|....*....|
gi 34098881 300 KKLLVKDPRARLTAAQALSH 319
Cdd:cd14189 233 AGILKRNPGDRLTLDQILEH 252
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
61-322 1.93e-39

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: 143.92  E-value: 1.93e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKR---EVQILIALS--GHENVVQFHNAFEDDDY 135
Cdd:cd14005   1 QYEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVTEWAMINGPVPvplEIALLLKASkpGVPGVIRLLDWYERPDG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 136 VYIVMELCEGGELLDRILSKKGnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDspLKATDFGLSDF 215
Cdd:cd14005  81 FLLIMERPEPCQDLFDFITERG-ALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRTGE--VKLIDFGCGAL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 216 IKPgKRFHDIVGSAYYVAPEVLKRRS--GPESDVWSIGVITYILLCGRRPFwdRTEDGIfkevLRNKPDFsrkpWATISD 293
Cdd:cd14005 158 LKD-SVYTDFDGTRVYSPPEWIRHGRyhGRPATVWSLGILLYDMLCGDIPF--ENDEQI----LRGNVLF----RPRLSK 226
                       250       260
                ....*....|....*....|....*....
gi 34098881 294 SAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14005 227 ECCDLISRCLQFDPSKRPSLEQILSHPWF 255
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
61-322 3.76e-39

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


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 143.25  E-value: 3.76e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMvlpiaveDVK------REVQILIALSgHENVVQFHNAFEDDD 134
Cdd:cd14075   3 FYRIRGELGSGNFSQVKLGIHQLTKEKVAIKILDKTKL-------DQKtqrllsREISSMEKLH-HPNIIRLYEVVETLS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 135 YVYIVMELCEGGELLDRILSkkGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLdspLKATDFGLSD 214
Cdd:cd14075  75 KLHLVMEYASGGELYTKIST--EGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNC---VKVGDFGFST 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 215 FIKPGKRFHDIVGSAYYVAPEVLKRRS--GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNK---PDFsrkpwa 289
Cdd:cd14075 150 HAKRGETLNTFCGSPPYAAPELFKDEHyiGIYVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTytiPSY------ 223
                       250       260       270
                ....*....|....*....|....*....|...
gi 34098881 290 tISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14075 224 -VSEPCQELIRGILQPVPSDRYSIDEIKNSEWL 255
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
60-322 5.09e-39

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


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 142.79  E-value: 5.09e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIV 139
Cdd:cd14116   5 EDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRREVEIQSHLR-HPNILRLYGYFHDATRVYLI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAqldSPLKATDFGLSdFIKPG 219
Cdd:cd14116  84 LEYAPLGTVYREL--QKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSA---GELKIADFGWS-VHAPS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 220 KRFHDIVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCGRRPFWDRTEDGIFKEVlrNKPDFSRKPWatISDSAKDF 298
Cdd:cd14116 158 SRRTTLCGTLDYLPPEMIEGRMHDEKvDLWSLGVLCYEFLVGKPPFEANTYQETYKRI--SRVEFTFPDF--VTEGARDL 233
                       250       260
                ....*....|....*....|....
gi 34098881 299 VKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14116 234 ISRLLKHNPSQRPMLREVLEHPWI 257
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
62-322 6.97e-38

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: 139.70  E-value: 6.97e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRpNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVME 141
Cdd:cd14161   5 YEFLETLGKGTYGRVKKARDS-SGRLVAIKSIRKDRIKDEQDLLHIRREIEIMSSLN-HPHIISVYEVFENSSKIVIVME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELLDRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKPGKR 221
Cdd:cd14161  83 YASRGDLYDYISERQ--RLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDA---NGNIKIADFGLSNLYNQDKF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 222 FHDIVGSAYYVAPEVLKRR--SGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKpdfSRKPwaTISDSAKDFV 299
Cdd:cd14161 158 LQTYCGSPLYASPEIVNGRpyIGPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGA---YREP--TKPSDACGLI 232
                       250       260
                ....*....|....*....|...
gi 34098881 300 KKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14161 233 RWLLMVNPERRATLEDVASHWWV 255
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
62-321 1.10e-37

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: 139.53  E-value: 1.10e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFE-DDDYVYIVM 140
Cdd:cd14165   3 YILGINLGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPDDFVEKFLPRELEILARLN-HKSIIKTYEIFEtSDGKVYIVM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCEGGELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKPGK 220
Cdd:cd14165  82 ELGVQGDLLEFI--KLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDK---DFNIKLTDFGFSKRCLRDE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 221 RFHDIV-----GSAYYVAPEVLKRRS-GPE-SDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKpwATISD 293
Cdd:cd14165 157 NGRIVLsktfcGSAAYAAPEVLQGIPyDPRiYDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFPRS--KNLTS 234
                       250       260
                ....*....|....*....|....*...
gi 34098881 294 SAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd14165 235 ECKDLIYRLLQPDVSQRLCIDEVLSHPW 262
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
66-323 1.20e-37

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: 140.84  E-value: 1.20e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMvlpIAVEDVKR---EVQILiALSGHENVVQFHNAFEDDDYVYIVMEL 142
Cdd:cd05574   7 KLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEM---IKRNKVKRvltEREIL-ATLDHPFLPTLYASFQTSTHLCFVMDY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 143 CEGGELLDRILSKKGNRYSEKD----AAVVVrqmlkVAGEcHLH--GLVHRDMKPENFLFKSaqlDSPLKATDFGLS--- 213
Cdd:cd05574  83 CPGGELFRLLQKQPGKRLPEEVarfyAAEVL-----LALE-YLHllGFVYRDLKPENILLHE---SGHIMLTDFDLSkqs 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 214 -------------------------DFI--KPGKRFHDIVGSAYYVAPEVLKrRSGPESDV--WSIGVITYILLCGRRPF 264
Cdd:cd05574 154 svtpppvrkslrkgsrrssvksiekETFvaEPSARSNSFVGTEEYIAPEVIK-GDGHGSAVdwWTLGILLYEMLYGTTPF 232
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34098881 265 WDRTEDGIFKEVLRNKPDFSRKPwaTISDSAKDFVKKLLVKDPRARL----TAAQALSHAWVR 323
Cdd:cd05574 233 KGSNRDETFSNILKKELTFPESP--PVSSEAKDLIRKLLVKDPSKRLgskrGASEIKRHPFFR 293
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
61-319 1.89e-37

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: 138.50  E-value: 1.89e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDRVAVK--RLDKSKMvlpiavEDVKREVQILIALSgHENVVQFHNAFEDDDYVYI 138
Cdd:cd06614   1 LYKNLEKIGEGASGEVYKATDRATGKEVAIKkmRLRKQNK------ELIINEILIMKECK-HPNIVDYYDSYLVGDELWV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 139 VMELCEGGELLDrILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKP 218
Cdd:cd06614  74 VMEYMDGGSLTD-IITQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSK---DGSVKLADFGFAAQLTK 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 GK-RFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRT-EDGIFKEVLRNKPDFsRKPWaTISDSA 295
Cdd:cd06614 150 EKsKRNSVVGTPYWMAPEVIKRKDyGPKVDIWSLGIMCIEMAEGEPPYLEEPpLRALFLITTKGIPPL-KNPE-KWSPEF 227
                       250       260
                ....*....|....*....|....
gi 34098881 296 KDFVKKLLVKDPRARLTAAQALSH 319
Cdd:cd06614 228 KDFLNKCLVKDPEKRPSAEELLQH 251
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
62-321 5.75e-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: 138.47  E-value: 5.75e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVK--RLDKSKM----VLPIAVedvkREVQILIALSgHENVVQFHNAFEDDDY 135
Cdd:cd07841   2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKkiKLGERKEakdgINFTAL----REIKLLQELK-HPNIIGLLDVFGHKSN 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 136 VYIVMELCEGGelLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLS-D 214
Cdd:cd07841  77 INLVFEFMETD--LEKVIKDKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIAS---DGVLKLADFGLArS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 215 FIKPGKRFHDIVGSAYYVAPEVL--KRRSGPESDVWSIGVItYILLCGRRPFWDRTED-----GIFkEVL-----RNKPD 282
Cdd:cd07841 152 FGSPNRKMTHQVVTRWYRAPELLfgARHYGVGVDMWSVGCI-FAELLLRVPFLPGDSDidqlgKIF-EALgtpteENWPG 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 34098881 283 FSR------------KPWATI----SDSAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd07841 230 VTSlpdyvefkpfppTPLKQIfpaaSDDALDLLQRLLTLNPNKRITARQALEHPY 284
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
60-323 6.52e-37

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: 137.69  E-value: 6.52e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIV 139
Cdd:cd14117   6 DDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEGVEHQLRREIEIQSHLR-HPNILRLYNYFHDRKRIYLI 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKsaqLDSPLKATDFGLSdFIKPG 219
Cdd:cd14117  85 LEYAPRGELYKEL--QKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMG---YKGELKIADFGWS-VHAPS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 220 KRFHDIVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSrkpwATISDSAKDF 298
Cdd:cd14117 159 LRRRTMCGTLDYLPPEMIEGRTHDEKvDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFP----PFLSDGSRDL 234
                       250       260
                ....*....|....*....|....*
gi 34098881 299 VKKLLVKDPRARLTAAQALSHAWVR 323
Cdd:cd14117 235 ISKLLRYHPSERLPLKGVMEHPWVK 259
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
61-321 1.80e-36

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: 135.85  E-value: 1.80e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVM 140
Cdd:cd05578   1 HFQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDSVRNVLNELEILQELE-HPFLVNLWYSFQDEEDMYMVV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCEGGELldRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLfksaqLDSP--LKATDFGLSDFIKP 218
Cdd:cd05578  80 DLLLGGDL--RYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNIL-----LDEQghVHITDFNIATKLTD 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 GKRFHDIVGSAYYVAPEVLKRR-SGPESDVWSIGVITYILLCGRRPFWDRTEDGIfKEVLRNKPDFSRKPWATISDSAKD 297
Cdd:cd05578 153 GTLATSTSGTKPYMAPEVFMRAgYSFAVDWWSLGVTAYEMLRGKRPYEIHSRTSI-EEIRAKFETASVLYPAGWSEEAID 231
                       250       260
                ....*....|....*....|....*
gi 34098881 298 FVKKLLVKDPRARLTAAQALS-HAW 321
Cdd:cd05578 232 LINKLLERDPQKRLGDLSDLKnHPY 256
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
62-321 1.83e-36

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: 136.68  E-value: 1.83e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRL---DKSKMVLPIAVedvkREVQILIALSgHENVVQFHNAFEDDDYVYI 138
Cdd:cd07833   3 YEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFkesEDDEDVKKTAL----REVKVLRQLR-HENIVNLKEAFRRKGRLYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 139 VMELCEGG--ELLDRilSKKGnryseKDAAVVVR---QMLKVAGECHLHGLVHRDMKPENFLFKSAqldSPLKATDFGLS 213
Cdd:cd07833  78 VFEYVERTllELLEA--SPGG-----LPPDAVRSyiwQLLQAIAYCHSHNIIHRDIKPENILVSES---GVLKLCDFGFA 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 214 DFI--KPGKRFHDIVGSAYYVAPEVLKRRS--GPESDVWSIGVITYILLCGRRPFWDRTE-DGIFK-------------E 275
Cdd:cd07833 148 RALtaRPASPLTDYVATRWYRAPELLVGDTnyGKPVDVWAIGCIMAELLDGEPLFPGDSDiDQLYLiqkclgplppshqE 227
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 276 VLRNKPDFS--------------RKPWATISDSAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd07833 228 LFSSNPRFAgvafpepsqpesleRRYPGKVSSPALDFLKACLRMDPKERLTCDELLQHPY 287
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
56-322 1.87e-36

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: 136.28  E-value: 1.87e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  56 KDFHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDkskmVLPIAVEDVKREVQILIALSGHENVVQFHNAF----- 130
Cdd:cd06608   2 PDPAGIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMD----IIEDEEEEIKLEINILRKFSNHPNIATFYGAFikkdp 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 131 -EDDDYVYIVMELCEGGELLD--RILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKA 207
Cdd:cd06608  78 pGGDDQLWLVMEYCGGGSVTDlvKGLRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTE---EAEVKL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 208 TDFGLSDFIKP--GKRfHDIVGSAYYVAPEVLKRRSGPE------SDVWSIGvITYILLC-GRRPFWD----RTedgIFK 274
Cdd:cd06608 155 VDFGVSAQLDStlGRR-NTFIGTPYWMAPEVIACDQQPDasydarCDVWSLG-ITAIELAdGKPPLCDmhpmRA---LFK 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 34098881 275 eVLRNKPD--FSRKPWatiSDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd06608 230 -IPRNPPPtlKSPEKW---SKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
60-331 3.46e-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: 135.64  E-value: 3.46e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLD-KSKMVLpiavEDVKREVQILiALSGHENVVQFHNAFEDDDYVYI 138
Cdd:cd06611   5 DIWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQiESEEEL----EDFMVEIDIL-SECKHPNIVGLYEAYFYENKLWI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 139 VMELCEGGELlDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKsaqLDSPLKATDFGLSDFIKP 218
Cdd:cd06611  80 LIEFCDGGAL-DSIMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLT---LDGDVKLADFGVSAKNKS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 GKRFHD-IVGSAYYVAPEVL---KRRSGP---ESDVWSIGvITYILLCGRRPFWDRTEDG--IFKeVLRNKPDFSRKP-- 287
Cdd:cd06611 156 TLQKRDtFIGTPYWMAPEVVaceTFKDNPydyKADIWSLG-ITLIELAQMEPPHHELNPMrvLLK-ILKSEPPTLDQPsk 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 34098881 288 WatiSDSAKDFVKKLLVKDPRARLTAAQALSHAWVREGGNATDI 331
Cdd:cd06611 234 W---SSSFNDFLKSCLVKDPDDRPTAAELLKHPFVSDQSDNKAI 274
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
59-321 3.66e-36

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: 135.02  E-value: 3.66e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  59 HDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKrldkskmVLPIAVEDVKREVQ---ILIALSgHENVVQFHNAFEDDDY 135
Cdd:cd14107   1 HSVYEVKEEIGRGTFGFVKRVTHKGNGECCAAK-------FIPLRSSTRARAFQerdILARLS-HRRLTCLLDQFETRKT 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 136 VYIVMELCEGGELLDRiLSKKGNrYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSpLKATDFGLSDF 215
Cdd:cd14107  73 LILILELCSSEELLDR-LFLKGV-VTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTRED-IKICDFGFAQE 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 216 IKPGKRFHDIVGSAYYVAPEVLKRRSGPE-SDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDS 294
Cdd:cd14107 150 ITPSEHQFSKYGSPEFVAPEIVHQEPVSAaTDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVSWDTPEITHLSED 229
                       250       260
                ....*....|....*....|....*..
gi 34098881 295 AKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd14107 230 AKDFIKRVLQPDPEKRPSASECLSHEW 256
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
68-321 6.96e-36

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: 133.95  E-value: 6.96e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDR-VAVKRLDKSKMVlPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEGG 146
Cdd:cd14121   3 LGSGTYATVYKAYRKSGAREvVAVKCVSKSSLN-KASTENLLTEIELLKKLK-HPHIVELKDFQWDEEHIYLIMEYCSGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 147 ELLDRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFkSAQLDSPLKATDFGLSDFIKPGKRFHDIV 226
Cdd:cd14121  81 DLSRFIRSRR--TLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLL-SSRYNPVLKLADFGFAQHLKPNDEAHSLR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 227 GSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTedgiFKE----VLRNKPdFSRKPWATISDSAKDFVKK 301
Cdd:cd14121 158 GSPLYMAPEMILKKKyDARVDLWSVGVILYECLFGRAPFASRS----FEEleekIRSSKP-IEIPTRPELSADCRDLLLR 232
                       250       260
                ....*....|....*....|
gi 34098881 302 LLVKDPRARLTAAQALSHAW 321
Cdd:cd14121 233 LLQRDPDRRISFEEFFAHPF 252
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
62-321 7.64e-36

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: 133.90  E-value: 7.64e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKrldksKMVLPIAVEDV-KREVQILIALS---GHENVVQFHNAFED--DDY 135
Cdd:cd05118   1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIK-----KIKNDFRHPKAaLREIKLLKHLNdveGHPNIVKLLDVFEHrgGNH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 136 VYIVMELCegGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKsaQLDSPLKATDFGLSDF 215
Cdd:cd05118  76 LCLVFELM--GMNLYELIKDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILIN--LELGQLKLADFGLARS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 216 IKPGKRFHDIVgSAYYVAPEVL--KRRSGPESDVWSIGVITYILLCGRRPFWDRTE-DGIFK--EVLRNKPdfsrkpwat 290
Cdd:cd05118 152 FTSPPYTPYVA-TRWYRAPEVLlgAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEvDQLAKivRLLGTPE--------- 221
                       250       260       270
                ....*....|....*....|....*....|.
gi 34098881 291 isdsAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd05118 222 ----ALDLLSKMLKYDPAKRITASQALAHPY 248
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
65-322 1.44e-35

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: 133.30  E-value: 1.44e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  65 GKLLGHGQFGYTYVAIHRPNGDRVAVK--RLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMEL 142
Cdd:cd06632   5 GQLLGSGSFGSVYEGFNGDTGDFFAVKevSLVDDDKKSRESVKQLEQEIALLSKLR-HPNIVQYYGTEREEDNLYIFLEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 143 CEGGELLDriLSKKGNRYSEKDAAVVVRQMLKvaGECHLH--GLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKPGK 220
Cdd:cd06632  84 VPGGSIHK--LLQRYGAFEEPVIRLYTRQILS--GLAYLHsrNTVHRDIKGANILVDT---NGVVKLADFGMAKHVEAFS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 221 RFHDIVGSAYYVAPEVLKRRSGP---ESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNK-----PDfsrkpwaTIS 292
Cdd:cd06632 157 FAKSFKGSPYWMAPEVIMQKNSGyglAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSGelppiPD-------HLS 229
                       250       260       270
                ....*....|....*....|....*....|
gi 34098881 293 DSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd06632 230 PDAKDFIRLCLQRDPEDRPTASQLLEHPFV 259
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
65-322 1.97e-35

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: 133.25  E-value: 1.97e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  65 GKLLGHGQFGYTYVAIHRPNGDRVAVKR--LDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMEL 142
Cdd:cd06625   5 GKLLGQGAFGQVYLCYDADTGRELAVKQveIDPINTEASKEVKALECEIQLLKNLQ-HERIVQYYGCLQDEKSLSIFMEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 143 CEGGELLDRIlsKKGNRYSEKDAAVVVRQMLKvaGECHLHG--LVHRDMKPENFLFKSAqldSPLKATDFGLS---DFIK 217
Cdd:cd06625  84 MPGGSVKDEI--KAYGALTENVTRKYTRQILE--GLAYLHSnmIVHRDIKGANILRDSN---GNVKLGDFGASkrlQTIC 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 218 PGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGViTYILLCGRRPFWDRTED--GIFKEVLRN-KPDFSrkpwATISD 293
Cdd:cd06625 157 SSTGMKSVTGTPYWMSPEVINGEGyGRKADIWSVGC-TVVEMLTTKPPWAEFEPmaAIFKIATQPtNPQLP----PHVSE 231
                       250       260
                ....*....|....*....|....*....
gi 34098881 294 SAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd06625 232 DARDFLSLIFVRNKKQRPSAEELLSHSFV 260
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
62-321 2.34e-35

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: 133.38  E-value: 2.34e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVK--RLDKSKMVLPI-AVedvkREVQILIALSgHENVVQFHNAFEDDDYVYI 138
Cdd:cd07829   1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKkiRLDNEEEGIPStAL----REISLLKELK-HPNIVKLLDVIHTENKLYL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 139 VMELCEggELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLdspLKATDFGLS-DFIK 217
Cdd:cd07829  76 VFEYCD--QDLKKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGV---LKLADFGLArAFGI 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 218 PGKRF-HDIVgSAYYVAPEVL--KRRSGPESDVWSIGVITYILLCGRRPFWDRTE----DGIFK-----------EVLRN 279
Cdd:cd07829 151 PLRTYtHEVV-TLWYRAPEILlgSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEidqlFKIFQilgtpteeswpGVTKL 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 34098881 280 K------PDFSRKPWA----TISDSAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd07829 230 PdykptfPKWPKNDLEkvlpRLDPEGIDLLSKMLQYNPAKRISAKEALKHPY 281
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
54-318 2.95e-35

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: 133.19  E-value: 2.95e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  54 YSKDFHDHytigKLLGHGQFGYTYVAIHRPNGDRVAVKRL---DKSkmvlpIAVEDVKREVQILIALSgHENVVQFHNAF 130
Cdd:cd13996   4 YLNDFEEI----ELLGSGGFGSVYKVRNKVDGVTYAIKKIrltEKS-----SASEKVLREVKALAKLN-HPNIVRYYTAW 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 131 EDDDYVYIVMELCEGGELLDRILSKKGNRYSEKDAAV-VVRQMLKVAGECHLHGLVHRDMKPEN-FLFKSAQLdspLKAT 208
Cdd:cd13996  74 VEEPPLYIQMELCEGGTLRDWIDRRNSSSKNDRKLALeLFKQILKGVSYIHSKGIVHRDLKPSNiFLDNDDLQ---VKIG 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 209 DFGLSDFIKPGKRFHDI---------------VGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEdgI 272
Cdd:cd13996 151 DFGLATSIGNQKRELNNlnnnnngntsnnsvgIGTPLYASPEQLDGENyNEKADIYSLGIILFEMLHPFKTAMERST--I 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 34098881 273 FKEVLRNK--PDFSRKPwatisDSAKDFVKKLLVKDPRARLTAAQALS 318
Cdd:cd13996 229 LTDLRNGIlpESFKAKH-----PKEADLIQSLLSKNPEERPSAEQLLR 271
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
68-310 5.15e-35

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: 131.51  E-value: 5.15e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRpnGDRVAVKRLDKSKMVlPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEGGE 147
Cdd:cd13999   1 IGSGSFGEVYKGKWR--GTDVAIKKLKVEDDN-DELLKEFRREVSILSKLR-HPNIVQFIGACLSPPPLCIVTEYMPGGS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 148 LLDRILSKKGNRysekDAAVVVRQMLKVA-GECHLH--GLVHRDMKPENFLfksaqLDSPLKA--TDFGLSDFIKPGKRF 222
Cdd:cd13999  77 LYDLLHKKKIPL----SWSLRLKIALDIArGMNYLHspPIIHRDLKSLNIL-----LDENFTVkiADFGLSRIKNSTTEK 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 223 HD-IVGSAYYVAPEVLK-RRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPdfsRKPwatISDSAKDFVK 300
Cdd:cd13999 148 MTgVVGTPRWMAPEVLRgEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGL---RPP---IPPDCPPELS 221
                       250
                ....*....|....
gi 34098881 301 KLLVK----DPRAR 310
Cdd:cd13999 222 KLIKRcwneDPEKR 235
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
67-319 6.83e-35

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: 131.35  E-value: 6.83e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  67 LLGHGQFGYTYVAIHRPNGDRVAVKRLdKSKMVLPIAVEDVKREVQILIALSGHENVVQFHNAFEDDDYVYIVMELCEGG 146
Cdd:cd13997   7 QIGSGSFSEVFKVRSKVDGCLYAVKKS-KKPFRGPKERARALREVEAHAALGQHPNIVRYYSSWEEGGHLYIQMELCENG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 147 ElLDRILSKKG--NRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSdfIKPGKRFHD 224
Cdd:cd13997  86 S-LQDALEELSpiSKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISN---KGTCKIGDFGLA--TRLETSGDV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 225 IVGSAYYVAPEVL--KRRSGPESDVWSIGVITYILLCG-----RRPFWDRTEDGIFkevlrnkPDFsrkPWATISDSAKD 297
Cdd:cd13997 160 EEGDSRYLAPELLneNYTHLPKADIFSLGVTVYEAATGeplprNGQQWQQLRQGKL-------PLP---PGLVLSQELTR 229
                       250       260
                ....*....|....*....|..
gi 34098881 298 FVKKLLVKDPRARLTAAQALSH 319
Cdd:cd13997 230 LLKVMLDPDPTRRPTADQLLAH 251
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
62-322 7.86e-35

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: 131.27  E-value: 7.86e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFED-DDYVYIVM 140
Cdd:cd14163   2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGPEEFIQRFLPRELQIVERLD-HKNIIHVYEMLESaDGKIYLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCEGGELLDRILskKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLdsplKATDFGLSDFIKPGK 220
Cdd:cd14163  81 ELAEDGDVFDCVL--HGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGFTL----KLTDFGFAKQLPKGG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 221 R--FHDIVGSAYYVAPEVLK--RRSGPESDVWSIGVITYILLCGRRPFwDRTEdgIFKEVLRNKPDFSRKPWATISDSAK 296
Cdd:cd14163 155 RelSQTFCGSTAYAAPEVLQgvPHDSRKGDIWSMGVVLYVMLCAQLPF-DDTD--IPKMLCQQQKGVSLPGHLGVSRTCQ 231
                       250       260
                ....*....|....*....|....*.
gi 34098881 297 DFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14163 232 DLLKRLLEPDMVLRPSIEEVSWHPWL 257
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
62-321 9.56e-35

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: 132.07  E-value: 9.56e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAvEDVKREVQILIALSGHENVVQFHNAFEDDDYVYIVME 141
Cdd:cd07832   2 YKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEGGIP-NQALREIKALQACQGHPYVVKLRDVFPHGTGFVLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGelLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKPG-- 219
Cdd:cd07832  81 YMLSS--LSEVLRDEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISS---TGVLKIADFGLARLFSEEdp 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 220 KRFHDIVGSAYYVAPEVL--KRRSGPESDVWSIGVITYILLCGRrPFWDRTEDG-----IFKEV----------LRNKPD 282
Cdd:cd07832 156 RLYSHQVATRWYRAPELLygSRKYDEGVDLWAVGCIFAELLNGS-PLFPGENDIeqlaiVLRTLgtpnektwpeLTSLPD 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 34098881 283 FS--------RKPWATI----SDSAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd07832 235 YNkitfpeskGIRLEEIfpdcSPEAIDLLKGLLVYNPKKRLSAEEALRHPY 285
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
62-323 1.43e-34

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: 131.21  E-value: 1.43e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIavEDVKREVQILIALSGhENVVQFHNAFEDDDYVYIVME 141
Cdd:cd06609   3 FTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEEAEDEI--EDIQQEIQFLSQCDS-PYITKYYGSFLKGSKLWIIME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELLDRIlskKGNRYSEKDAAVVVRQMLKvaGECHLH--GLVHRDMKPENFLFkSAQLDspLKATDFG----LSDF 215
Cdd:cd06609  80 YCGGGSVLDLL---KPGPLDETYIAFILREVLL--GLEYLHseGKIHRDIKAANILL-SEEGD--VKLADFGvsgqLTST 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 216 IKpgKRfHDIVGSAYYVAPEVLKRRSGPE-SDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDfsRKPWATISDS 294
Cdd:cd06609 152 MS--KR-NTFVGTPFWMAPEVIKQSGYDEkADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPKNNPP--SLEGNKFSKP 226
                       250       260
                ....*....|....*....|....*....
gi 34098881 295 AKDFVKKLLVKDPRARLTAAQALSHAWVR 323
Cdd:cd06609 227 FKDFVELCLNKDPKERPSAKELLKHKFIK 255
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
68-319 1.64e-34

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 130.57  E-value: 1.64e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDR-VAVK-----RLDKSKMVLpiavedvKREVQILIALSgHENVVQFHNAFEDDDYVYIVME 141
Cdd:cd14120   1 IGHGAFAVVFKGRHRKKPDLpVAIKcitkkNLSKSQNLL-------GKEIKILKELS-HENVVALLDCQETSSSVYLVME 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELLDRiLSKKGNrYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLF------KSAQLDSPLKATDFGLSDF 215
Cdd:cd14120  73 YCNGGDLADY-LQAKGT-LSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLshnsgrKPSPNDIRLKIADFGFARF 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 216 IKPGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPwATISDS 294
Cdd:cd14120 151 LQDGMMAATLCGSPMYMAPEVIMSLQyDAKADLWSIGTIVYQCLTGKAPFQAQTPQELKAFYEKNANLRPNIP-SGTSPA 229
                       250       260
                ....*....|....*....|....*
gi 34098881 295 AKDFVKKLLVKDPRARLTAAQALSH 319
Cdd:cd14120 230 LKDLLLGLLKRNPKDRIDFEDFFSH 254
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
56-345 1.81e-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: 132.43  E-value: 1.81e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  56 KDFHdhytIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILiALSGHENVVQFHNAFEDDDY 135
Cdd:cd05601   1 KDFE----VKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVSFFEEERDIM-AKANSPWITKLQYAFQDSEN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 136 VYIVMELCEGGELLDrILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLfksaqLDSP--LKATDFGLS 213
Cdd:cd05601  76 LYLVMEYHPGGDLLS-LLSRYDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENIL-----IDRTghIKLADFGSA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 214 DFIKPGK--RFHDIVGSAYYVAPEVLKRRS-------GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFS 284
Cdd:cd05601 150 AKLSSDKtvTSKMPVGTPDYIAPEVLTSMNggskgtyGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMNFKKFLK 229
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34098881 285 RKPWATISDSAKDFVKKLLVkDPRARLTAAQALSHAWVreggnaTDIPvdisvLNNLRQFV 345
Cdd:cd05601 230 FPEDPKVSESAVDLIKGLLT-DAKERLGYEGLCCHPFF------SGID-----WNNLRQTV 278
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
61-333 3.29e-34

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


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 131.49  E-value: 3.29e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKrldksKMVLPIA-VEDVK---REVQILIALSgHENVVQFHNAFEDDDY- 135
Cdd:cd07834   1 RYELLKPIGSGAYGVVCSAYDKRTGRKVAIK-----KISNVFDdLIDAKrilREIKILRHLK-HENIIGLLDILRPPSPe 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 136 ----VYIVMELCEGGelLDRILsKKGNRYSEKDAAVVVRQMLKvaGECHLH--GLVHRDMKPENFLFKSaqlDSPLKATD 209
Cdd:cd07834  75 efndVYIVTELMETD--LHKVI-KSPQPLTDDHIQYFLYQILR--GLKYLHsaGVIHRDLKPSNILVNS---NCDLKICD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 210 FGLSDFIKPGKRFHDI---VGSAYYVAPEVL--KRRSGPESDVWSIGVITYILLcGRRPFWD-----------------R 267
Cdd:cd07834 147 FGLARGVDPDEDKGFLteyVVTRWYRAPELLlsSKKYTKAIDIWSVGCIFAELL-TRKPLFPgrdyidqlnlivevlgtP 225
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34098881 268 TEDGI-------FKEVLRNKPDFSRKPWATI----SDSAKDFVKKLLVKDPRARLTAAQALSHAWVREGGNATDIPV 333
Cdd:cd07834 226 SEEDLkfissekARNYLKSLPKKPKKPLSEVfpgaSPEAIDLLEKMLVFNPKKRITADEALAHPYLAQLHDPEDEPV 302
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
62-321 3.73e-34

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: 129.72  E-value: 3.73e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVlpiaVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVME 141
Cdd:cd14665   2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKI----DENVQREIINHRSLR-HPNIVRFKEVILTPTHLAIVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELLDRILSkkGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQldSP-LKATDFGLSDFIKPGK 220
Cdd:cd14665  77 YAAGGELFERICN--AGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSP--APrLKICDFGYSKSSVLHS 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 221 RFHDIVGSAYYVAPEVLKRRS--GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRN--KPDFSRKPWATISDSAK 296
Cdd:cd14665 153 QPKSTVGTPAYIAPEVLLKKEydGKIADVWSCGVTLYVMLVGAYPFEDPEEPRNFRKTIQRilSVQYSIPDYVHISPECR 232
                       250       260
                ....*....|....*....|....*
gi 34098881 297 DFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd14665 233 HLISRIFVADPATRITIPEIRNHEW 257
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
61-322 7.15e-34

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: 128.96  E-value: 7.15e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLdksKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVM 140
Cdd:cd06613   1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVI---KLEPGDDFEIIQQEISMLKECR-HPNIVAYFGSYLRRDKLWIVM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCEGGELLDriLSKKGNRYSEKDAAVVVRQMLKvaGECHLH--GLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKP 218
Cdd:cd06613  77 EYCGGGSLQD--IYQVTGPLSELQIAYVCRETLK--GLAYLHstGKIHRDIKGANILLTE---DGDVKLADFGVSAQLTA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 --GKRfHDIVGSAYYVAPEVL--KRRSGPES--DVWSIGvITYILLC-GRRPFWD----RtedgifkeVLRNKPDFSRKP 287
Cdd:cd06613 150 tiAKR-KSFIGTPYWMAPEVAavERKGGYDGkcDIWALG-ITAIELAeLQPPMFDlhpmR--------ALFLIPKSNFDP 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 34098881 288 --------WatiSDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd06613 220 pklkdkekW---SPDFHDFIKKCLTKNPKKRPTATKLLQHPFV 259
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
62-321 1.30e-33

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: 127.96  E-value: 1.30e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVlpiaVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVME 141
Cdd:cd14662   2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKI----DENVQREIINHRSLR-HPNIIRFKEVVLTPTHLAIVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELLDRILSKkgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLfksaqLD-SP---LKATDFGLSDFIK 217
Cdd:cd14662  77 YAAGGELFERICNA--GRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTL-----LDgSPaprLKICDFGYSKSSV 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 218 PGKRFHDIVGSAYYVAPEVLKRRS--GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLR-------NKPDFSRkpw 288
Cdd:cd14662 150 LHSQPKSTVGTPAYIAPEVLSRKEydGKVADVWSCGVTLYVMLVGAYPFEDPDDPKNFRKTIQrimsvqyKIPDYVR--- 226
                       250       260       270
                ....*....|....*....|....*....|...
gi 34098881 289 atISDSAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd14662 227 --VSQDCRHLLSRIFVANPAKRITIPEIKNHPW 257
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
60-322 1.37e-33

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: 127.75  E-value: 1.37e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVK---RLDKSKMVLpiavEDVKREVQILIALSgHENVVQFHNAFEDDDYV 136
Cdd:cd14002   1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALKfipKRGKSEKEL----RNLRQEIEILRKLN-HPNIIEMLDSFETKKEF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 137 YIVMELCEGgELLdRILSKKGNrYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFI 216
Cdd:cd14002  76 VVVTEYAQG-ELF-QILEDDGT-LPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGK---GGVVKLCDFGFARAM 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 217 KPGKRF-HDIVGSAYYVAPEVLKRRsgP---ESDVWSIGVITYILLCGRRPFWdrtEDGIFKEVLRNKPDFSRKPwATIS 292
Cdd:cd14002 150 SCNTLVlTSIKGTPLYMAPELVQEQ--PydhTADLWSLGCILYELFVGQPPFY---TNSIYQLVQMIVKDPVKWP-SNMS 223
                       250       260       270
                ....*....|....*....|....*....|
gi 34098881 293 DSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14002 224 PEFKSFLQGLLNKDPSKRLSWPDLLEHPFV 253
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
66-311 1.47e-33

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: 129.64  E-value: 1.47e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSGHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd05570   1 KVLGKGSFGKVMLAERKKTDELYAIKVLKKEVIIEDDDVECTMTEKRVLALANRHPFLTGLHACFQTEDRLYFVMEYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRILskKGNRYSEKDA---AVVVRQMLKVageCHLHGLVHRDMKPENFLfksaqLDSP--LKATDFGLS-DFIKPG 219
Cdd:cd05570  81 GDLMFHIQ--RARRFTEERArfyAAEICLALQF---LHERGIIYRDLKLDNVL-----LDAEghIKIADFGMCkEGIWGG 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 220 KRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKpwatISDSAKDF 298
Cdd:cd05570 151 NTTSTFCGTPDYIAPEILREQDyGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPRW----LSREAVSI 226
                       250
                ....*....|...
gi 34098881 299 VKKLLVKDPRARL 311
Cdd:cd05570 227 LKGLLTKDPARRL 239
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
62-325 1.69e-33

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: 128.13  E-value: 1.69e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVME 141
Cdd:cd14187   9 YVRGRFLGKGGFAKCYEITDADTKEVFAGKIVPKSLLLKPHQKEKMSMEIAIHRSLA-HQHVVGFHGFFEDNDFVYVVLE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELLDriLSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENfLFKSAQLDspLKATDFGLSDFIK-PGK 220
Cdd:cd14187  88 LCRRRSLLE--LHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGN-LFLNDDME--VKIGDFGLATKVEyDGE 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 221 RFHDIVGSAYYVAPEVL-KRRSGPESDVWSIGVITYILLCGRRPFwdrtEDGIFKEV-LRNKPDFSRKPwATISDSAKDF 298
Cdd:cd14187 163 RKKTLCGTPNYIAPEVLsKKGHSFEVDIWSIGCIMYTLLVGKPPF----ETSCLKETyLRIKKNEYSIP-KHINPVAASL 237
                       250       260
                ....*....|....*....|....*..
gi 34098881 299 VKKLLVKDPRARLTAAQALSHAWVREG 325
Cdd:cd14187 238 IQKMLQTDPTARPTINELLNDEFFTSG 264
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
59-319 1.87e-33

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: 127.38  E-value: 1.87e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  59 HDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKrldkskmVLPI--AVEDVKREVQILiALSGHENVVQFHNAFEDDDYV 136
Cdd:cd06612   2 EEVFDILEKLGEGSYGSVYKAIHKETGQVVAIK-------VVPVeeDLQEIIKEISIL-KQCDSPYIVKYYGSYFKNTDL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 137 YIVMELCEGGELLD--RILSKkgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLS- 213
Cdd:cd06612  74 WIVMEYCGAGSVSDimKITNK---TLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNE---EGQAKLADFGVSg 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 214 DFIKPGKRFHDIVGSAYYVAPEVLKR-RSGPESDVWSIGvITYILLC-GRRPFWDRTEDGIFKEVLRNKPDFSRKP--Wa 289
Cdd:cd06612 148 QLTDTMAKRNTVIGTPFWMAPEVIQEiGYNNKADIWSLG-ITAIEMAeGKPPYSDIHPMRAIFMIPNKPPPTLSDPekW- 225
                       250       260       270
                ....*....|....*....|....*....|
gi 34098881 290 tiSDSAKDFVKKLLVKDPRARLTAAQALSH 319
Cdd:cd06612 226 --SPEFNDFVKKCLVKDPEERPSAIQLLQH 253
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
62-319 2.02e-33

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: 127.72  E-value: 2.02e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIhRPNGDRVAVKRLDKSKmVLPIAVEDVKREVQILIALSGHENVVQF--HNAFEDDDYVYIV 139
Cdd:cd14131   3 YEILKQLGKGGSSKVYKVL-NPKKKIYALKRVDLEG-ADEQTLQSYKNEIELLKKLKGSDRIIQLydYEVTDEDDYLYMV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELcegGEL-LDRILSKK-GNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFksaqLDSPLKATDFGLSDFIK 217
Cdd:cd14131  81 MEC---GEIdLATILKKKrPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLL----VKGRLKLIDFGIAKAIQ 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 218 PGK----RFHdIVGSAYYVAPEVLKRRS-----------GPESDVWSIGVITYILLCGRRPFWDRTeDGIFK-EVLRNK- 280
Cdd:cd14131 154 NDTtsivRDS-QVGTLNYMSPEAIKDTSasgegkpkskiGRPSDVWSLGCILYQMVYGKTPFQHIT-NPIAKlQAIIDPn 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 34098881 281 -----PDFSrkpwatiSDSAKDFVKKLLVKDPRARLTAAQALSH 319
Cdd:cd14131 232 heiefPDIP-------NPDLIDVMKRCLQRDPKKRPSIPELLNH 268
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
64-311 3.05e-33

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 129.17  E-value: 3.05e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881   64 IGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELC 143
Cdd:PTZ00263  22 MGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELS-HPFIVNMMCSFQDENRVYFLLEFV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  144 EGGELLDRIlsKKGNRYSeKDAAVVVRQMLKVAGEcHLH--GLVHRDMKPENFLFKSaqlDSPLKATDFGLSDfiKPGKR 221
Cdd:PTZ00263 101 VGGELFTHL--RKAGRFP-NDVAKFYHAELVLAFE-YLHskDIIYRDLKPENLLLDN---KGHVKVTDFGFAK--KVPDR 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  222 FHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRkpWatISDSAKDFVK 300
Cdd:PTZ00263 172 TFTLCGTPEYLAPEVIQSKGhGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPN--W--FDGRARDLVK 247
                        250
                 ....*....|.
gi 34098881  301 KLLVKDPRARL 311
Cdd:PTZ00263 248 GLLQTDHTKRL 258
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
68-323 3.21e-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: 127.17  E-value: 3.21e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVlpiAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEGGE 147
Cdd:cd06648  15 IGEGSTGIVCIATDKSTGRQVAVKKMDLRKQQ---RRELLFNEVVIMRDYQ-HPNIVEMYSSYLVGDELWVVMEFLEGGA 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 148 LLDrILSKkgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFG----LSDFIkPGKRfh 223
Cdd:cd06648  91 LTD-IVTH--TRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTS---DGRVKLSDFGfcaqVSKEV-PRRK-- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 224 DIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPwATISDSAKDFVKKL 302
Cdd:cd06648 162 SLVGTPYWMAPEVISRLPyGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNEPPKLKNL-HKVSPRLRSFLDRM 240
                       250       260
                ....*....|....*....|.
gi 34098881 303 LVKDPRARLTAAQALSHAWVR 323
Cdd:cd06648 241 LVRDPAQRATAAELLNHPFLA 261
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
66-311 5.90e-33

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: 128.12  E-value: 5.90e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILiALSGHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd05599   7 KVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKEQVAHVRAERDIL-AEADNPWVVKLYYSFQDEENLYLIMEFLPG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDrILSKKgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKPGKRFHDI 225
Cdd:cd05599  86 GDMMT-LLMKK-DTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDA---RGHIKLSDFGLCTGLKKSHLAYST 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 226 VGSAYYVAPEV-LKRRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDSAKDFVKKLLV 304
Cdd:cd05599 161 VGTPDYIAPEVfLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMNWRETLVFPPEVPISPEAKDLIERLLC 240

                ....*..
gi 34098881 305 kDPRARL 311
Cdd:cd05599 241 -DAEHRL 246
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
60-321 7.03e-33

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: 126.17  E-value: 7.03e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLD-KSKmvlpiAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYI 138
Cdd:cd14108   2 DYYDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPvRAK-----KKTSARRELALLAELD-HKSIVRFHDAFEKRRVVII 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 139 VMELCEgGELLDRILSKKGNRYSEKDAavVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSpLKATDFGLSDFIKP 218
Cdd:cd14108  76 VTELCH-EELLERITKRPTVCESEVRS--YMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTDQ-VRICDFGNAQELTP 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 GKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDSAKD 297
Cdd:cd14108 152 NEPQYCKYGTPEFVAPEIVNQSPvSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYNVAFEESMFKDLCREAKG 231
                       250       260
                ....*....|....*....|....
gi 34098881 298 FVKKLLVKDpRARLTAAQALSHAW 321
Cdd:cd14108 232 FIIKVLVSD-RLRPDAEETLEHPW 254
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
68-313 1.36e-32

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: 125.58  E-value: 1.36e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDR---VAVKRLDKSKMVLPIAV-EDVKREVQILIALSGHENVVQFHNAFEDDDYVYIVMELC 143
Cdd:cd05583   2 LGTGAYGKVFLVRKVGGHDAgklYAMKVLKKATIVQKAKTaEHTMTERQVLEAVRQSPFLVTLHYAFQTDAKLHLILDYV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 144 EGGELLDRILSKKgnRYSEKDAAVVVRQMLkVAGEcHLH--GLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKPGK- 220
Cdd:cd05583  82 NGGELFTHLYQRE--HFTESEVRIYIGEIV-LALE-HLHklGIIYRDIKLENILLDS---EGHVVLTDFGLSKEFLPGEn 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 221 -RFHDIVGSAYYVAPEVLKRRSGPES---DVWSIGVITYILLCGRRPFwdrTEDG-------IFKEVLRNKPDFSRkpwa 289
Cdd:cd05583 155 dRAYSFCGTIEYMAPEVVRGGSDGHDkavDWWSLGVLTYELLTGASPF---TVDGernsqseISKRILKSHPPIPK---- 227
                       250       260
                ....*....|....*....|....
gi 34098881 290 TISDSAKDFVKKLLVKDPRARLTA 313
Cdd:cd05583 228 TFSAEAKDFILKLLEKDPKKRLGA 251
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
47-322 1.54e-32

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: 125.89  E-value: 1.54e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  47 GKRTDFGYSKDFHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDkskmvlPI--AVEDVKREVQILIALSGHENVV 124
Cdd:cd06638   5 GKTIIFDSFPDPSDTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILD------PIhdIDEEIEAEYNILKALSDHPNVV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 125 QFHNAF-----EDDDYVYIVMELCEGGELLDRI--LSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFK 197
Cdd:cd06638  79 KFYGMYykkdvKNGDQLWLVLELCNGGSVTDLVkgFLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 198 SaqlDSPLKATDFGLSDFIKPGK-RFHDIVGSAYYVAPEVLKRRSGPES------DVWSIGVITYILLCGRRPFWD-RTE 269
Cdd:cd06638 159 T---EGGVKLVDFGVSAQLTSTRlRRNTSVGTPFWMAPEVIACEQQLDStydarcDVWSLGITAIELGDGDPPLADlHPM 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 34098881 270 DGIFKeVLRNKPDFSRKP--WatiSDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd06638 236 RALFK-IPRNPPPTLHQPelW---SNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
68-321 2.48e-32

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: 125.37  E-value: 2.48e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVK--RLDKSKMVLPIAVedvKREVQILIALSgHENVVQFHN---AFEDDDY---VYIV 139
Cdd:cd07840   7 IGEGTYGQVYKARNKKTGELVALKkiRMENEKEGFPITA---IREIKLLQKLD-HPNVVRLKEivtSKGSAKYkgsIYMV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGelLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKPG 219
Cdd:cd07840  83 FEYMDHD--LTGLLDNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINN---DGVLKLADFGLARPYTKE 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 220 K--RFHDIVGSAYYVAPEVL--KRRSGPESDVWSIGVITYILLCGRRPFWDRTE----DGIFkEVL-----RNKPDFSRK 286
Cdd:cd07840 158 NnaDYTNRVITLWYRPPELLlgATRYGPEVDMWSVGCILAELFTGKPIFQGKTEleqlEKIF-ELCgspteENWPGVSDL 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 34098881 287 PWAT-------------------ISDSAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd07840 237 PWFEnlkpkkpykrrlrevfknvIDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
62-322 2.60e-32

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: 124.90  E-value: 2.60e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPN-----GDRVAVKRLDKSKMVLPIAVEDVKREVQILIALsGHENVVQFHNAFEDDDYV 136
Cdd:cd14076   3 YILGRTLGEGEFGKVKLGWPLPKanhrsGVQVAIKLIRRDTQQENCQTSKIMREINILKGL-THPNIVRLLDVLKTKKYI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 137 YIVMELCEGGELLDRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSD-- 214
Cdd:cd14076  82 GIVLEFVSGGELFDYILARR--RLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDK---NRNLVITDFGFANtf 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 215 FIKPGKRFHDIVGSAYYVAPEVLKRRS---GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLR----------NKP 281
Cdd:cd14076 157 DHFNGDLMSTSCGSPCYAAPELVVSDSmyaGRKADIWSCGVILYAMLAGYLPFDDDPHNPNGDNVPRlyryicntplIFP 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 34098881 282 DFsrkpwatISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14076 237 EY-------VTPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
107-322 2.90e-32

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: 124.16  E-value: 2.90e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 107 VKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEGGELLDRILSKkgNRYSEKDAAVVVRQMLKVAGECHLHGLVH 186
Cdd:cd14111  46 VLQEYEILKSLH-HERIMALHEAYITPRYLVLIAEFCSGKELLHSLIDR--FRYSEDDVVGYLVQILQGLEYLHGRRVLH 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 187 RDMKPENFLFKSaqlDSPLKATDFGLSDFIKP------GKRfhdiVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLC 259
Cdd:cd14111 123 LDIKPDNIMVTN---LNAIKIVDFGSAQSFNPlslrqlGRR----TGTLEYMAPEMVKGEPvGPPADIWSIGVLTYIMLS 195
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34098881 260 GRRPFWDRTEDGIFKEVLRNKPDfSRKPWATISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14111 196 GRSPFEDQDPQETEAKILVAKFD-AFKLYPNVSQSASLFLKKVLSSYPWSRPTTKDCFAHAWL 257
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
62-320 3.05e-32

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: 124.31  E-value: 3.05e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVME 141
Cdd:cd08224   2 YEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIFEMMDAKARQDCLKEIDLLQQLN-HPNIIKYLASFIENNELNIVLE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGEL--LDRILSKKGNRYSEKDaavVVRQMLKVAG---ECHLHGLVHRDMKPENfLFKSAqlDSPLKATDFGLSDFI 216
Cdd:cd08224  81 LADAGDLsrLIKHFKKQKRLIPERT---IWKYFVQLCSaleHMHSKRIMHRDIKPAN-VFITA--NGVVKLGDLGLGRFF 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 217 KPgKRF--HDIVGSAYYVAPEVLkRRSGPE--SDVWSIGVITYILLCGRRPFWDRTED--GIFKEVlrNKPDFSRKPWAT 290
Cdd:cd08224 155 SS-KTTaaHSLVGTPYYMSPERI-REQGYDfkSDIWSLGCLLYEMAALQSPFYGEKMNlySLCKKI--EKCEYPPLPADL 230
                       250       260       270
                ....*....|....*....|....*....|
gi 34098881 291 ISDSAKDFVKKLLVKDPRARLTAAQALSHA 320
Cdd:cd08224 231 YSQELRDLVAACIQPDPEKRPDISYVLDVA 260
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
62-317 3.23e-32

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: 124.06  E-value: 3.23e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVkREVQILIALSgHENVVQFHNAFEDDDYVYIVME 141
Cdd:cd08529   2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRKMREEAI-DEARVLSKLN-SPYVIKYYDSFVDKGKLNIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELLDRILSKKGNRYSEKDAAVVVRQMLkvAGECHLHG--LVHRDMKPENfLFKSAQLDspLKATDFGLSDFIKPG 219
Cdd:cd08529  80 YAENGDLHSLIKSQRGRPLPEDQIWKFFIQTL--LGLSHLHSkkILHRDIKSMN-IFLDKGDN--VKIGDLGVAKILSDT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 220 KRF-HDIVGSAYYVAPEVLKRRSGPE-SDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKpdFSRKPwATISDSAKD 297
Cdd:cd08529 155 TNFaQTIVGTPYYLSPELCEDKPYNEkSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGK--YPPIS-ASYSQDLSQ 231
                       250       260
                ....*....|....*....|
gi 34098881 298 FVKKLLVKDPRARLTAAQAL 317
Cdd:cd08529 232 LIDSCLTKDYRQRPDTTELL 251
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
62-323 4.87e-32

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: 124.12  E-value: 4.87e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVK--RLDKSKMvlpiAVEDVKREVQIL--IALSGHENVVQFHNAFEDDDYVY 137
Cdd:cd06917   3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKvlNLDTDDD----DVSDIQKEVALLsqLKLGQPKNIIKYYGSYLKGPSLW 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 138 IVMELCEGGELldRILSKKGnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAqldSPLKATDFGL-SDFI 216
Cdd:cd06917  79 IIMDYCEGGSI--RTLMRAG-PIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNT---GNVKLCDFGVaASLN 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 217 KPGKRFHDIVGSAYYVAPEVLK--RRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPdfSRKPWATISDS 294
Cdd:cd06917 153 QNSSKRSTFVGTPYWMAPEVITegKYYDTKADIWSLGITTYEMATGNPPYSDVDALRAVMLIPKSKP--PRLEGNGYSPL 230
                       250       260
                ....*....|....*....|....*....
gi 34098881 295 AKDFVKKLLVKDPRARLTAAQALSHAWVR 323
Cdd:cd06917 231 LKEFVAACLDEEPKDRLSADELLKSKWIK 259
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
65-322 1.89e-31

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: 122.26  E-value: 1.89e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  65 GKLLGHGQFGYTYVAIHRPNGDRVAVKRLD-----------KSKMVlpiavEDVKREVQILIALSgHENVVQFHNAFEDD 133
Cdd:cd06628   5 GALIGSGSFGSVYLGMNASSGELMAVKQVElpsvsaenkdrKKSML-----DALQREIALLRELQ-HENIVQYLGSSSDA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 134 DYVYIVMELCEGGELLDRIlskkgNRYSEKDAAVV---VRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDF 210
Cdd:cd06628  79 NHLNIFLEYVPGGSVATLL-----NNYGAFEESLVrnfVRQILKGLNYLHNRGIIHRDIKGANILVDN---KGGIKISDF 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 211 GLSDFI-------KPGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTE-DGIFKEVLRNKP 281
Cdd:cd06628 151 GISKKLeanslstKNNGARPSLQGSVFWMAPEVVKQTSyTRKADIWSLGCLVVEMLTGTHPFPDCTQmQAIFKIGENASP 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 34098881 282 DFSrkpwATISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd06628 231 TIP----SNISSEARDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
68-321 2.69e-31

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: 121.61  E-value: 2.69e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKsKMVlpiAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEGGE 147
Cdd:cd14115   1 IGRGRFSIVKKCLHKATRKDVAVKFVSK-KMK---KKEQAAHEAALLQHLQ-HPQYITLHDTYESPTSYILVLELMDDGR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 148 LLDRILSKkgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENfLFKSAQLDSP-LKATDFGLSDFIKPGKRFHDIV 226
Cdd:cd14115  76 LLDYLMNH--DELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPEN-LLIDLRIPVPrVKLIDLEDAVQISGHRHVHHLL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 227 GSAYYVAPEVLkrRSGPES---DVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDSAKDFVKKLL 303
Cdd:cd14115 153 GNPEFAAPEVI--QGTPVSlatDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDEYFGDVSQAARDFINVIL 230
                       250
                ....*....|....*...
gi 34098881 304 VKDPRARLTAAQALSHAW 321
Cdd:cd14115 231 QEDPRRRPTAATCLQHPW 248
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
68-322 3.07e-31

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: 121.21  E-value: 3.07e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKM-VLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDY--VYIVMELCE 144
Cdd:cd14119   1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKLrRIPNGEANVKREIQILRRLN-HRNVIKLVDVLYNEEKqkLYMVMEYCV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 145 GGeLLDRILSKKGNRYSEKDAAVVVRQMLKvaGECHLH--GLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFI---KPG 219
Cdd:cd14119  80 GG-LQEMLDSAPDKRLPIWQAHGYFVQLID--GLEYLHsqGIIHKDIKPGNLLLTT---DGTLKISDFGVAEALdlfAED 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 220 KRFHDIVGSAYYVAPEV---LKRRSGPESDVWSIGVITYILLCGRRPFWDrteDGIFKeVLRNkpdFSRKPW---ATISD 293
Cdd:cd14119 154 DTCTTSQGSPAFQPPEIangQDSFSGFKVDIWSAGVTLYNMTTGKYPFEG---DNIYK-LFEN---IGKGEYtipDDVDP 226
                       250       260
                ....*....|....*....|....*....
gi 34098881 294 SAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14119 227 DLQDLLRGMLEKDPEKRFTIEQIRQHPWF 255
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
66-317 3.67e-31

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: 121.74  E-value: 3.67e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILialSGHEN--VVQFHNAFEDDDYVYIVMELC 143
Cdd:cd05609   6 KLISNGAYGAVYLVRHRETRQRFAMKKINKQNLILRNQIQQVFVERDIL---TFAENpfVVSMYCSFETKRHLCMVMEYV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 144 EGGELldRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAqldSPLKATDFGLS---------- 213
Cdd:cd05609  83 EGGDC--ATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSM---GHIKLTDFGLSkiglmslttn 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 214 ---DFI-KPGKRFHD--IVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRK 286
Cdd:cd05609 158 lyeGHIeKDTREFLDkqVCGTPEYIAPEVILRQGyGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPEG 237
                       250       260       270
                ....*....|....*....|....*....|.
gi 34098881 287 PWAtISDSAKDFVKKLLVKDPRARLTAAQAL 317
Cdd:cd05609 238 DDA-LPDDAQDLITRLLQQNPLERLGTGGAE 267
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
51-331 3.83e-31

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 122.05  E-value: 3.83e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  51 DFGYSKDFHDHYTigkLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVlpiAVEDVKREVQILIALSgHENVVQFHNAF 130
Cdd:cd06657  14 DPGDPRTYLDNFI---KIGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQ---RRELLFNEVVIMRDYQ-HENVVEMYNSY 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 131 EDDDYVYIVMELCEGGELLDRILSkkgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDF 210
Cdd:cd06657  87 LVGDELWVVMEFLEGGALTDIVTH---TRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTH---DGRVKLSDF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 211 GL-SDFIKPGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDfSRKPW 288
Cdd:cd06657 161 GFcAQVSKEVPRRKSLVGTPYWMAPELISRLPyGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPP-KLKNL 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 34098881 289 ATISDSAKDFVKKLLVKDPRARLTAAQALSHAWVREGGNATDI 331
Cdd:cd06657 240 HKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPSCI 282
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
62-335 6.35e-31

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: 121.75  E-value: 6.35e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDkskmVLPIAVEDVKREVQILIALSGHENVVQFHNAFED------DDY 135
Cdd:cd06637   8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTGDEEEEIKQEINMLKKYSHHRNIATYYGAFIKknppgmDDQ 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 136 VYIVMELCEGGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLS-D 214
Cdd:cd06637  84 LWLVMEFCGAGSVTDLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTE---NAEVKLVDFGVSaQ 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 215 FIKPGKRFHDIVGSAYYVAPEVLKRRSGPE------SDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRN-KPDFSRKP 287
Cdd:cd06637 161 LDRTVGRRNTFIGTPYWMAPEVIACDENPDatydfkSDLWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNpAPRLKSKK 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 34098881 288 WatiSDSAKDFVKKLLVKDPRARLTAAQALSHAWVREGGNATDIPVDI 335
Cdd:cd06637 241 W---SKKFQSFIESCLVKNHSQRPSTEQLMKHPFIRDQPNERQVRIQL 285
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
61-319 8.72e-31

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: 121.07  E-value: 8.72e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRldkskmVLPiaveDVK---REVQILIALSgHENVVQFHNAF------E 131
Cdd:cd14137   5 SYTIEKVIGSGSFGVVYQAKLLETGEVVAIKK------VLQ----DKRyknRELQIMRRLK-HPNIVKLKYFFyssgekK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 132 DDDYVYIVME-----LCEggelLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLF--KSAQldsp 204
Cdd:cd14137  74 DEVYLNLVMEympetLYR----VIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVdpETGV---- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 205 LKATDFGLSDFIKPGKRFHDIVGSAYYVAPEVL--KRRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLR---- 278
Cdd:cd14137 146 LKLCDFGSAKRLVPGEPNVSYICSRYYRAPELIfgATDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKvlgt 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34098881 279 -----------NKPDFS-----RKPWATI-----SDSAKDFVKKLLVKDPRARLTAAQALSH 319
Cdd:cd14137 226 ptreqikamnpNYTEFKfpqikPHPWEKVfpkrtPPDAIDLLSKILVYNPSKRLTALEALAH 287
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
62-318 9.35e-31

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: 120.08  E-value: 9.35e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVK--RLDKSKMvlpiAVEDVKREVqILIALSGHENVVQFHNAFEDDDYVYIV 139
Cdd:cd08219   2 YNVLRVVGEGSFGRALLVQHVNSDQKYAMKeiRLPKSSS----AVEDSRKEA-VLLAKMKHPNIVAFKESFEADGHLYIV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPEN-FLFKSAQldspLKATDFGLSDFI-K 217
Cdd:cd08219  77 MEYCDGGDLMQKIKLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNiFLTQNGK----VKLGDFGSARLLtS 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 218 PGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFwdrtEDGIFKEVLRNKPDFSRKPWAT-ISDSA 295
Cdd:cd08219 153 PGAYACTYVGTPYYVPPEIWENMPyNNKSDIWSLGCILYELCTLKHPF----QANSWKNLILKVCQGSYKPLPShYSYEL 228
                       250       260
                ....*....|....*....|...
gi 34098881 296 KDFVKKLLVKDPRARLTAAQALS 318
Cdd:cd08219 229 RSLIKQMFKRNPRSRPSATTILS 251
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
60-323 2.36e-30

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: 119.85  E-value: 2.36e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIV 139
Cdd:cd05612   1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRLKQEQHVHNEKRVLKEVS-HPFIIRLFWTEHDQRFLYML 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGELLDRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSdfikpg 219
Cdd:cd05612  80 MEYVPGGELFSYLRNSG--RFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDK---EGHIKLTDFGFA------ 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 220 KRFHD----IVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRkpwaTISDS 294
Cdd:cd05612 149 KKLRDrtwtLCGTPEYLAPEVIQSKGhNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFPR----HLDLY 224
                       250       260       270
                ....*....|....*....|....*....|....
gi 34098881 295 AKDFVKKLLVKDPRARL-----TAAQALSHAWVR 323
Cdd:cd05612 225 AKDLIKKLLVVDRTRRLgnmknGADDVKNHRWFK 258
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
62-319 4.30e-30

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: 118.19  E-value: 4.30e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVME 141
Cdd:cd14188   3 YCRGKVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKPHQREKIDKEIELHRILH-HKHVVQFYHYFEDKENIYILLE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELLDRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQldsPLKATDFGLSDFIKP-GK 220
Cdd:cd14188  82 YCSRRSMAHILKARK--VLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENM---ELKVGDFGLAARLEPlEH 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 221 RFHDIVGSAYYVAPEVL-KRRSGPESDVWSIGVITYILLCGRRPFwdrtEDGIFKEVLRNKPDFSRKPWATISDSAKDFV 299
Cdd:cd14188 157 RRRTICGTPNYLSPEVLnKQGHGCESDIWALGCVMYTMLLGRPPF----ETTNLKETYRCIREARYSLPSSLLAPAKHLI 232
                       250       260
                ....*....|....*....|
gi 34098881 300 KKLLVKDPRARLTAAQALSH 319
Cdd:cd14188 233 ASMLSKNPEDRPSLDEIIRH 252
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
66-322 5.30e-30

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: 118.96  E-value: 5.30e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDkskmVLPIAVEDVKREVQILIALSGHENVVQFHNAF------EDDDYVYIV 139
Cdd:cd06636  22 EVVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKLEINMLKKYSHHRNIATYYGAFikksppGHDDQLWLV 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLS-DFIKP 218
Cdd:cd06636  98 MEFCGAGSVTDLVKNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTE---NAEVKLVDFGVSaQLDRT 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 GKRFHDIVGSAYYVAPEVLKRRSGPE------SDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRN-KPDFSRKPWati 291
Cdd:cd06636 175 VGRRNTFIGTPYWMAPEVIACDENPDatydyrSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNpPPKLKSKKW--- 251
                       250       260       270
                ....*....|....*....|....*....|.
gi 34098881 292 SDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd06636 252 SKKFIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
54-322 5.81e-30

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 118.15  E-value: 5.81e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  54 YSKDFHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMvlpiAVEDVKREVQILIALSgHENVVQFHNAFEDD 133
Cdd:cd14113   1 WKDNFDSFYSEVAELGRGRFSVVKKCDQRGTKRAVATKFVNKKLM----KRDQVTHELGVLQSLQ-HPQLVGLLDTFETP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 134 DYVYIVMELCEGGELLDRILSKkGNRYSEKdAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLS 213
Cdd:cd14113  76 TSYILVLEMADQGRLLDYVVRW-GNLTEEK-IRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSKPTIKLADFGDA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 214 DFIKPGKRFHDIVGSAYYVAPE-VLKRRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATIS 292
Cdd:cd14113 154 VQLNTTYYIHQLLGSPEFAAPEiILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPDDYFKGVS 233
                       250       260       270
                ....*....|....*....|....*....|
gi 34098881 293 DSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14113 234 QKAKDFVCFLLQMDPAKRPSAALCLQEQWL 263
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
60-319 5.89e-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: 117.71  E-value: 5.89e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIH-------RPNGDRVAVKRLDKSkmVLPIAVEdvkREVQILIALSGHENVVQFHNAFED 132
Cdd:cd14019   1 NKYRIIEKIGEGTFSSVYKAEDklhdlydRNKGRLVALKHIYPT--SSPSRIL---NELECLERLGGSNNVSGLITAFRN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 133 DDYVYIVMELCEGGELLDRILSkkgnrYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFksaqldSPLKAT---- 208
Cdd:cd14019  76 EDQVVAVLPYIEHDDFRDFYRK-----MSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLY------NRETGKgvlv 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 209 DFGLSDFI--KPGKRfHDIVGSAYYVAPEVLKR--RSGPESDVWSIGVITYILLCGRRPFWDRTED-GIFKEVlrnkpdf 283
Cdd:cd14019 145 DFGLAQREedRPEQR-APRAGTRGFRAPEVLFKcpHQTTAIDIWSAGVILLSILSGRFPFFFSSDDiDALAEI------- 216
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 34098881 284 srkpwATI--SDSAKDFVKKLLVKDPRARLTAAQALSH 319
Cdd:cd14019 217 -----ATIfgSDEAYDLLDKLLELDPSKRITAEEALKH 249
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
68-322 6.04e-30

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 118.23  E-value: 6.04e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIA--------------------VEDVKREVQILIALSgHENVVQFH 127
Cdd:cd14118   2 IGKGSYGIVKLAYNEEDNTLYAMKILSKKKLLKQAGffrrppprrkpgalgkpldpLDRVYREIAILKKLD-HPNVVKLV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 128 NAFED--DDYVYIVMELCEGGELLDRILSkkgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPL 205
Cdd:cd14118  81 EVLDDpnEDNLYMVFELVDKGAVMEVPTD---NPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGD---DGHV 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 206 KATDFGLSDFIKPGKRF-HDIVGSAYYVAPEVL----KRRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVlRNK 280
Cdd:cd14118 155 KIADFGVSNEFEGDDALlSSTAGTPAFMAPEALsesrKKFSGKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKI-KTD 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 34098881 281 P-DFSRKPwaTISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14118 234 PvVFPDDP--VVSEQLKDLILRMLDKNPSERITLPEIKEHPWV 274
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
63-266 6.20e-30

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: 117.65  E-value: 6.20e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881     63 TIGKLLGHGQFGYTYVAIHRPNGD----RVAVKRLDKSKMvlPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYI 138
Cdd:smart00221   2 TLGKKLGEGAFGEVYKGTLKGKGDgkevEVAVKTLKEDAS--EQQIEEFLREARIMRKLD-HPNIVKLLGVCTEEEPLMI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881    139 VMELCEGGELLDRILSKKGNRYSekdaavvVRQMLKVA-----GECHLH--GLVHRDMKPENFLfksaqLDSPL--KATD 209
Cdd:smart00221  79 VMEYMPGGDLLDYLRKNRPKELS-------LSDLLSFAlqiarGMEYLEskNFIHRDLAARNCL-----VGENLvvKISD 146
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881    210 FGLSDFIKPGKrfhdivgsaYYV-----------APEVLKRRS-GPESDVWSIGVITY-ILLCGRRPFWD 266
Cdd:smart00221 147 FGLSRDLYDDD---------YYKvkggklpirwmAPESLKEGKfTSKSDVWSFGVLLWeIFTLGEEPYPG 207
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
62-320 1.05e-29

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: 117.11  E-value: 1.05e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPiAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVME 141
Cdd:cd08530   2 FKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLSQK-EREDSVNEIRLLASVN-HPNIIRYKEAFLDGNRLCIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELLDRIL--SKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLdspLKATDFGLSDFIKPG 219
Cdd:cd08530  80 YAPFGDLSKLISkrKKKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDL---VKIGDLGISKVLKKN 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 220 KRFHDIvGSAYYVAPEVLKRRsgP---ESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKpdFSRKPwATISDSAK 296
Cdd:cd08530 157 LAKTQI-GTPLYAAPEVWKGR--PydyKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRGK--FPPIP-PVYSQDLQ 230
                       250       260
                ....*....|....*....|....
gi 34098881 297 DFVKKLLVKDPRARLTAAQALSHA 320
Cdd:cd08530 231 QIIRSLLQVNPKKRPSCDKLLQSP 254
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
55-311 1.06e-29

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: 119.40  E-value: 1.06e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  55 SKDFHdhytIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVlpiavedvKR-------EVQILIALSGHENVVQFH 127
Cdd:cd05596  25 AEDFD----VIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMI--------KRsdsaffwEERDIMAHANSEWIVQLH 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 128 NAFEDDDYVYIVMELCEGGELLDrILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLfksaqLDSP--L 205
Cdd:cd05596  93 YAFQDDKYLYMVMDYMPGGDLVN-LMSNY--DVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNML-----LDASghL 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 206 KATDFGLSdfIKPGK----RFHDIVGSAYYVAPEVLKRRSGP-----ESDVWSIGVITYILLCGRRPFWDRTEDGIFKEV 276
Cdd:cd05596 165 KLADFGTC--MKMDKdglvRSDTAVGTPDYISPEVLKSQGGDgvygrECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKI 242
                       250       260       270
                ....*....|....*....|....*....|....*
gi 34098881 277 LRNKPDFSRKPWATISDSAKDFVKKLLVkDPRARL 311
Cdd:cd05596 243 MNHKNSLQFPDDVEISKDAKSLICAFLT-DREVRL 276
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
63-266 1.18e-29

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 116.86  E-value: 1.18e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881     63 TIGKLLGHGQFGYTYVAIHRPNGD----RVAVKRLDKSKMvlPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYI 138
Cdd:smart00219   2 TLGKKLGEGAFGEVYKGKLKGKGGkkkvEVAVKTLKEDAS--EQQIEEFLREARIMRKLD-HPNVVKLLGVCTEEEPLYI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881    139 VMELCEGGELLDRILSKKGNrysekdaaVVVRQMLKVA-----GECHLH--GLVHRDMKPENFLfksaqLDSPL--KATD 209
Cdd:smart00219  79 VMEYMEGGDLLSYLRKNRPK--------LSLSDLLSFAlqiarGMEYLEskNFIHRDLAARNCL-----VGENLvvKISD 145
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881    210 FGLSDFIKPGKrfhdivgsaYYV-----------APEVLKRRS-GPESDVWSIGVITY-ILLCGRRPFWD 266
Cdd:smart00219 146 FGLSRDLYDDD---------YYRkrggklpirwmAPESLKEGKfTSKSDVWSFGVLLWeIFTLGEQPYPG 206
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
68-326 2.95e-29

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: 117.01  E-value: 2.95e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVlpiAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEGGE 147
Cdd:cd06659  29 IGEGSTGVVCIAREKHSGRQVAVKMMDLRKQQ---RRELLFNEVVIMRDYQ-HPNVVEMYKSYLVGEELWVLMEYLQGGA 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 148 LLDrILSKkgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKsaqLDSPLKATDFGLSDFIK---PGKRfhD 224
Cdd:cd06659 105 LTD-IVSQ--TRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLT---LDGRVKLSDFGFCAQISkdvPKRK--S 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 225 IVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEvLRNKPDFSRKPWATISDSAKDFVKKLL 303
Cdd:cd06659 177 LVGTPYWMAPEVISRCPyGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKR-LRDSPPPKLKNSHKASPVLRDFLERML 255
                       250       260
                ....*....|....*....|...
gi 34098881 304 VKDPRARLTAAQALSHAWVREGG 326
Cdd:cd06659 256 VRDPQERATAQELLDHPFLLQTG 278
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
60-319 3.02e-29

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: 117.26  E-value: 3.02e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDkskmvlPIAVEDVKREVQILIALSGHENVVQFHNAFEDDD---YV 136
Cdd:cd14132  18 DDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLK------PVKKKKIKREIKILQNLRGGPNIVKLLDVVKDPQsktPS 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 137 yIVMELCEGGELLDRILSkkgnrYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQldSPLKATDFGLSDFI 216
Cdd:cd14132  92 -LIFEYVNNTDFKTLYPT-----LTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEK--RKLRLIDWGLAEFY 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 217 KPGKRFHDIVGSAYYVAPEVL--KRRSGPESDVWSIGVITYILLCGRRPF---WDRTE-----------DGIFK------ 274
Cdd:cd14132 164 HPGQEYNVRVASRYYKGPELLvdYQYYDYSLDMWSLGCMLASMIFRKEPFfhgHDNYDqlvkiakvlgtDDLYAyldkyg 243
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 34098881 275 ----EVLRNK-PDFSRKPWAT---------ISDSAKDFVKKLLVKDPRARLTAAQALSH 319
Cdd:cd14132 244 ielpPRLNDIlGRHSKKPWERfvnsenqhlVTPEALDLLDKLLRYDHQERITAKEAMQH 302
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
60-323 3.43e-29

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: 116.73  E-value: 3.43e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALsGHENVVQFHNAFEDDDYVYIV 139
Cdd:cd14209   1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEHTLNEKRILQAI-NFPFLVKLEYSFKDNSNLYMV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGELLDRiLSKKGnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLfksaqLDSP--LKATDFGLSDFIK 217
Cdd:cd14209  80 MEYVPGGEMFSH-LRRIG-RFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLL-----IDQQgyIKVTDFGFAKRVK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 218 pgKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSrkpwATISDSAK 296
Cdd:cd14209 153 --GRTWTLCGTPEYLAPEIILSKGyNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFP----SHFSSDLK 226
                       250       260       270
                ....*....|....*....|....*....|..
gi 34098881 297 DFVKKLLVKDPRARL-----TAAQALSHAWVR 323
Cdd:cd14209 227 DLLRNLLQVDLTKRFgnlknGVNDIKNHKWFA 258
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
61-315 4.69e-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: 115.89  E-value: 4.69e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVlpiAVEDVKREVQILIALSGHENVVQF-HNAFEDDDY---V 136
Cdd:cd13985   1 RYQVTKQLGEGGFSYVYLAHDVNTGRRYALKRMYFNDEE---QLRVAIKEIEIMKRLCGHPNIVQYyDSAILSSEGrkeV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 137 YIVMELCeGGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGecHLHG----LVHRDMKPENFLFKSaqlDSPLKATDFGL 212
Cdd:cd13985  78 LLLMEYC-PGSLVDILEKSPPSPLSEEEVLRIFYQICQAVG--HLHSqsppIIHRDIKIENILFSN---TGRFKLCDFGS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 213 SDFI-KPGKRFHDIV---------GSAYYVAPEVL----KRRSGPESDVWSIGVITYILLCGRRPFwdrTEDGIFKEVLR 278
Cdd:cd13985 152 ATTEhYPLERAEEVNiieeeiqknTTPMYRAPEMIdlysKKPIGEKADIWALGCLLYKLCFFKLPF---DESSKLAIVAG 228
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 34098881 279 NkpdFSRKPWATISDSAKDFVKKLLVKDPRARLTAAQ 315
Cdd:cd13985 229 K---YSIPEQPRYSPELHDLIRHMLTPDPAERPDIFQ 262
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
66-311 5.47e-29

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: 116.93  E-value: 5.47e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSGHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd05590   1 RVLGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLYCCFQTPDRLFFVMEFVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGL-SDFIKPGKRFHD 224
Cdd:cd05590  81 GDLMFHI--QKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDH---EGHCKLADFGMcKEGIFNGKTTST 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 225 IVGSAYYVAPEVLKRR-SGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSrkPWatISDSAKDFVKKLL 303
Cdd:cd05590 156 FCGTPDYIAPEILQEMlYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYP--TW--LSQDAVDILKAFM 231

                ....*...
gi 34098881 304 VKDPRARL 311
Cdd:cd05590 232 TKNPTMRL 239
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
66-313 5.47e-29

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: 117.03  E-value: 5.47e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSGHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd05575   1 KVIGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRNEVKHIMAERNVLLKNVKHPFLVGLHYSFQTKDKLYFVLDYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGL-SDFIKPGKRFHD 224
Cdd:cd05575  81 GELFFHL--QRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDS---QGHVVLTDFGLcKEGIEPSDTTST 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 225 IVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCGRRPFW--DRTE--DGIFKEVLRNKPdfsrkpwaTISDSAKDFV 299
Cdd:cd05575 156 FCGTPEYLAPEVLRKQPYDRTvDWWCLGAVLYEMLYGLPPFYsrDTAEmyDNILHKPLRLRT--------NVSPSARDLL 227
                       250
                ....*....|....
gi 34098881 300 KKLLVKDPRARLTA 313
Cdd:cd05575 228 EGLLQKDRTKRLGS 241
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
66-311 7.51e-29

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


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 116.30  E-value: 7.51e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILiALSGHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd05571   1 KVLGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEVAHTLTENRVL-QNTRHPFLTSLKYSFQTNDRLCFVMEYVNG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRiLSKKGnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGL-SDFIKPGKRFHD 224
Cdd:cd05571  80 GELFFH-LSRER-VFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDK---DGHIKITDFGLcKEEISYGATTKT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 225 IVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRkpwaTISDSAKDFVKKLL 303
Cdd:cd05571 155 FCGTPEYLAPEVLEDNDyGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPS----TLSPEAKSLLAGLL 230

                ....*...
gi 34098881 304 VKDPRARL 311
Cdd:cd05571 231 KKDPKKRL 238
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
61-319 8.62e-29

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: 114.95  E-value: 8.62e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVlpiavEDVK----REVQILIALSgHENVVQFHNAFEDDD-- 134
Cdd:cd08217   1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKMS-----EKEKqqlvSEVNILRELK-HPNIVRYYDRIVDRAnt 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 135 YVYIVMELCEGGELLDRI-LSKKGNRYSEKDAAV-VVRQMLKVAGECHLHG-----LVHRDMKPEN-FLFKsaqlDSPLK 206
Cdd:cd08217  75 TLYIVMEYCEGGDLAQLIkKCKKENQYIPEEFIWkIFTQLLLALYECHNRSvgggkILHRDLKPANiFLDS----DNNVK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 207 ATDFGLSDFIKPGKRF-HDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKpdFS 284
Cdd:cd08217 151 LGDFGLARVLSHDSSFaKTYVGTPYYMSPELLNEQSyDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEGK--FP 228
                       250       260       270
                ....*....|....*....|....*....|....*
gi 34098881 285 RKPwATISDSAKDFVKKLLVKDPRARLTAAQALSH 319
Cdd:cd08217 229 RIP-SRYSSELNEVIKSMLNVDPDKRPSVEELLQL 262
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
68-322 1.02e-28

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: 114.75  E-value: 1.02e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRldkskMVLPIAVEDVK---REVQILIAlSGHENVVQFHNAFEDDDYVYIVMELCE 144
Cdd:cd06605   9 LGEGNGGVVSKVRHRPSGQIMAVKV-----IRLEIDEALQKqilRELDVLHK-CNSPYIVGFYGAFYSEGDISICMEYMD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 145 GGELlDRILsKKGNRYSEKDAAVVVRQMLKvaGECHL---HGLVHRDMKPENFLFKSAqldSPLKATDFGLSdfikpGKR 221
Cdd:cd06605  83 GGSL-DKIL-KEVGRIPERILGKIAVAVVK--GLIYLhekHKIIHRDVKPSNILVNSR---GQVKLCDFGVS-----GQL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 222 FHDI----VGSAYYVAPEvlkRRSGP----ESDVWSIGVITYILLCGRRPF--WD-RTEDGIF---KEVLRNKPdfSRKP 287
Cdd:cd06605 151 VDSLaktfVGTRSYMAPE---RISGGkytvKSDIWSLGLSLVELATGRFPYppPNaKPSMMIFellSYIVDEPP--PLLP 225
                       250       260       270
                ....*....|....*....|....*....|....*
gi 34098881 288 WATISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd06605 226 SGKFSPDFQDFVSQCLQKDPTERPSYKELMEHPFI 260
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
66-311 1.41e-28

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: 115.10  E-value: 1.41e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTY----VAIHrPNGDRVAVKRLDKSKMVLPI-AVEDVKREVQILIALSGHENVVQFHNAFEDDDYVYIVM 140
Cdd:cd05613   6 KVLGTGAYGKVFlvrkVSGH-DAGKLYAMKVLKKATIVQKAkTAEHTRTERQVLEHIRQSPFLVTLHYAFQTDTKLHLIL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCEGGELLDRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLS-DFI-KP 218
Cdd:cd05613  85 DYINGGELFTHLSQRE--RFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDS---SGHVVLTDFGLSkEFLlDE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 GKRFHDIVGSAYYVAPEVLKrrsGPES------DVWSIGVITYILLCGRRPFwdrTEDG-------IFKEVLRNKPDFSR 285
Cdd:cd05613 160 NERAYSFCGTIEYMAPEIVR---GGDSghdkavDWWSLGVLMYELLTGASPF---TVDGeknsqaeISRRILKSEPPYPQ 233
                       250       260
                ....*....|....*....|....*.
gi 34098881 286 KpwatISDSAKDFVKKLLVKDPRARL 311
Cdd:cd05613 234 E----MSALAKDIIQRLLMKDPKKRL 255
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
67-322 1.81e-28

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: 113.95  E-value: 1.81e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  67 LLGHGQFGYTYVAIHRPNGD-RVAVKRLDKSKMVLPIAVedVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd14202   9 LIGHGAFAVVFKGRHKEKHDlEVAVKCINKKNLAKSQTL--LGKEIKILKELK-HENIVALYDFQEIANSVYLVMEYCNG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLF------KSAQLDSPLKATDFGLSDFIKPG 219
Cdd:cd14202  86 GDLADYLHTMR--TLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLsysggrKSNPNNIRIKIADFGFARYLQNN 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 220 KRFHDIVGSAYYVAPEV-LKRRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATiSDSAKDF 298
Cdd:cd14202 164 MMAATLCGSPMYMAPEViMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDLRLFYEKNKSLSPNIPRET-SSHLRQL 242
                       250       260
                ....*....|....*....|....
gi 34098881 299 VKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14202 243 LLGLLQRNQKDRMDFDEFFHHPFL 266
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
62-321 1.89e-28

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: 114.34  E-value: 1.89e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVK--RLDKS-----KMVLpiaVEDVKREVQILIALSgHENVVQFHNAFE-DD 133
Cdd:cd13990   2 YLLLNLLGKGGFSEVYKAFDLVEQRYVACKihQLNKDwseekKQNY---IKHALREYEIHKSLD-HPRIVKLYDVFEiDT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 134 DYVYIVMELCEGGELlDRILSKKGNrYSEKDAAVVVRQMlkVAGECHLH----GLVHRDMKPENFLFKSAQLDSPLKATD 209
Cdd:cd13990  78 DSFCTVLEYCDGNDL-DFYLKQHKS-IPEREARSIIMQV--VSALKYLNeikpPIIHYDLKPGNILLHSGNVSGEIKITD 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 210 FGLS------DFIKPGKRFHDI-VGSAYYVAPEVLKRRSGPES-----DVWSIGVITYILLCGRRPFWDR-TEDGIFKE- 275
Cdd:cd13990 154 FGLSkimddeSYNSDGMELTSQgAGTYWYLPPECFVVGKTPPKisskvDVWSVGVIFYQMLYGRKPFGHNqSQEAILEEn 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 34098881 276 -VLR-NKPDFSRKPwaTISDSAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd13990 234 tILKaTEVEFPSKP--VVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
62-264 1.96e-28

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: 113.51  E-value: 1.96e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMvlPIAVEDVKREVQILIALSGHENVVQFHNAFEDDDYVYIVME 141
Cdd:cd08225   2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKM--PVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELLDRILSKKGNRYSEKDaavVVRQMLKVA-GECHLHG--LVHRDMKPEN-FLFKSAQLdspLKATDFGLSDFIK 217
Cdd:cd08225  80 YCDGGDLMKRINRQRGVLFSEDQ---ILSWFVQISlGLKHIHDrkILHRDIKSQNiFLSKNGMV---AKLGDFGIARQLN 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 34098881 218 PGKRF-HDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPF 264
Cdd:cd08225 154 DSMELaYTCVGTPYYLSPEICQNRPyNNKTDIWSLGCVLYELCTLKHPF 202
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
88-319 2.04e-28

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: 113.93  E-value: 2.04e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  88 VAVKRLDKSKMvlpiavEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEGGELLDrILSKKGNrYSEKDAAV 167
Cdd:cd14010  28 VAIKCVDKSKR------PEVLNEVRLTHELK-HPNVLKFYEWYETSNHLWLVVEYCTGGDLET-LLRQDGN-LPESSVRK 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 168 VVRQMlkVAGECHLH--GLVHRDMKPENFLfksaqLDSP--LKATDFGLS-----------------DFIKPGKRFHDIV 226
Cdd:cd14010  99 FGRDL--VRGLHYIHskGIIYCDLKPSNIL-----LDGNgtLKLSDFGLArregeilkelfgqfsdeGNVNKVSKKQAKR 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 227 GSAYYVAPEVLkrRSGP---ESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWAT-ISDSAKDFVKKL 302
Cdd:cd14010 172 GTPYYMAPELF--QGGVhsfASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDPPPPPPKVSSkPSPDFKSLLKGL 249
                       250
                ....*....|....*..
gi 34098881 303 LVKDPRARLTAAQALSH 319
Cdd:cd14010 250 LEKDPAKRLSWDELVKH 266
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
63-268 2.53e-28

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: 113.36  E-value: 2.53e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881    63 TIGKLLGHGQFGYTYVAIHRPNGDR----VAVKRLDKSKMvlPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYI 138
Cdd:pfam07714   2 TLGEKLGEGAFGEVYKGTLKGEGENtkikVAVKTLKEGAD--EEEREDFLEEASIMKKLD-HPNIVKLLGVCTQGEPLYI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881   139 VMELCEGGELLDRILSKKGNrysekdaaVVVRQMLKVA-----GECHLH--GLVHRDMKPENFLfksaqLDSPL--KATD 209
Cdd:pfam07714  79 VTEYMPGGDLLDFLRKHKRK--------LTLKDLLSMAlqiakGMEYLEskNFVHRDLAARNCL-----VSENLvvKISD 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34098881   210 FGLSDFIKPgkrfhdivGSAYYV-----------APEVLK-RRSGPESDVWSIGVITY-ILLCGRRPFWDRT 268
Cdd:pfam07714 146 FGLSRDIYD--------DDYYRKrgggklpikwmAPESLKdGKFTSKSDVWSFGVLLWeIFTLGEQPYPGMS 209
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
62-310 3.24e-28

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: 112.98  E-value: 3.24e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVlPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVME 141
Cdd:cd08218   2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMS-PKEREESRKEVAVLSKMK-HPNIVQYQESFEENGNLYIVMD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPEN-FLFKsaqlDSPLKATDFGLSDFIK-PG 219
Cdd:cd08218  80 YCDGGDLYKRINAQRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNiFLTK----DGIIKLGDFGIARVLNsTV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 220 KRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLR-NKPDFSRKpwatISDSAKD 297
Cdd:cd08218 156 ELARTCIGTPYYLSPEICENKPyNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRgSYPPVPSR----YSYDLRS 231
                       250
                ....*....|...
gi 34098881 298 FVKKLLVKDPRAR 310
Cdd:cd08218 232 LVSQLFKRNPRDR 244
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
68-322 4.68e-28

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: 112.79  E-value: 4.68e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHR--PNGDRVAVKRL----DKSKMVLPIAVedVKREVQILIALSgHENVVQFHNAFED--DDYVyIV 139
Cdd:cd13994   1 IGKGATSVVRIVTKKnpRSGVLYAVKEYrrrdDESKRKDYVKR--LTSEYIISSKLH-HPNIVKVLDLCQDlhGKWC-LV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLdspLKATDFGLSDFIK-- 217
Cdd:cd13994  77 MEYCPGGDLFTLI--EKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGV---LKLTDFGTAEVFGmp 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 218 PGKRFHD---IVGSAYYVAPEVL--KRRSGPESDVWSIGVITYILLCGRRPF----WDRTEDGIFKEVLRNKPDFSRKPW 288
Cdd:cd13994 152 AEKESPMsagLCGSEPYMAPEVFtsGSYDGRAVDVWSCGIVLFALFTGRFPWrsakKSDSAYKAYEKSGDFTNGPYEPIE 231
                       250       260       270
                ....*....|....*....|....*....|....
gi 34098881 289 ATISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd13994 232 NLLPSECRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
66-319 5.99e-28

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: 113.95  E-value: 5.99e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILiALSGHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd05595   1 KLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVL-QNTRHPFLTALKYAFQTHDRLCFVMEYANG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRiLSKKgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGL-SDFIKPGKRFHD 224
Cdd:cd05595  80 GELFFH-LSRE-RVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDK---DGHIKITDFGLcKEGITDGATMKT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 225 IVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRkpwaTISDSAKDFVKKLL 303
Cdd:cd05595 155 FCGTPEYLAPEVLEDNDyGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPR----TLSPEAKSLLAGLL 230
                       250       260
                ....*....|....*....|.
gi 34098881 304 VKDPRARL-----TAAQALSH 319
Cdd:cd05595 231 KKDPKQRLgggpsDAKEVMEH 251
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
99-322 8.49e-28

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: 111.93  E-value: 8.49e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  99 VLPIAVED---VKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEGGELLDRILSKkgNRYSEKDAAVVVRQMLKV 175
Cdd:cd14110  35 IIPYKPEDkqlVLREYQVLRRLS-HPRIAQLHSAYLSPRHLVLIEELCSGPELLYNLAER--NSYSEAEVTDYLWQILSA 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 176 AGECHLHGLVHRDMKPENFLFKSAQLdspLKATDFGLSDFIKPGK-----RFHDIVGSayyVAPEVLKRR-SGPESDVWS 249
Cdd:cd14110 112 VDYLHSRRILHLDLRSENMIITEKNL---LKIVDLGNAQPFNQGKvlmtdKKGDYVET---MAPELLEGQgAGPQTDIWA 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34098881 250 IGVITYILLCGRRPF-----WDRTedgifKEVLRNKPDFSRkPWATISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14110 186 IGVTAFIMLSADYPVssdlnWERD-----RNIRKGKVQLSR-CYAGLSGGAVNFLKSTLCAKPWGRPTASECLQNPWL 257
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
51-322 1.05e-27

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: 112.02  E-value: 1.05e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  51 DFGYSKDfhdhytigKLLGHGQFGYTYVAIHRPNGD-RVAVK-----RLDKSKMVLpiavedvKREVQILIALSgHENVV 124
Cdd:cd14201   5 DFEYSRK--------DLVGHGAFAVVFKGRHRKKTDwEVAIKsinkkNLSKSQILL-------GKEIKILKELQ-HENIV 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 125 QFHNAFEDDDYVYIVMELCEGGELLDrILSKKGNrYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSP 204
Cdd:cd14201  69 ALYDVQEMPNSVFLVMEYCNGGDLAD-YLQAKGT-LSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASRKKS 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 205 ------LKATDFGLSDFIKPGKRFHDIVGSAYYVAPEV-LKRRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVL 277
Cdd:cd14201 147 svsgirIKIADFGFARYLQSNMMAATLCGSPMYMAPEViMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLRMFYE 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 34098881 278 RNKPDFSRKPWATiSDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14201 227 KNKNLQPSIPRET-SPYLADLLLGLLQRNQKDRMDFEAFFSHPFL 270
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
60-311 1.32e-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: 113.18  E-value: 1.32e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILiALSGHENVVQFHNAFEDDDYVYIV 139
Cdd:cd05598   1 SMFEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLRKKDVLKRNQVAHVKAERDIL-AEADNEWVVKLYYSFQDKENLYFV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGELLDrILSKKGnrYSEKDAAVVVRQMLKVAGE-CHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDfikp 218
Cdd:cd05598  80 MDYIPGGDLMS-LLIKKG--IFEEDLARFYIAELVCAIEsVHKMGFIHRDIKPDNILIDR---DGHIKLTDFGLCT---- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 GKRF---------HDIVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPW 288
Cdd:cd05598 150 GFRWthdskyylaHSLVGTPNYIAPEVLLRTGYTQLcDWWSVGVILYEMLVGQPPFLAQTPAETQLKVINWRTTLKIPHE 229
                       250       260
                ....*....|....*....|...
gi 34098881 289 ATISDSAKDFVKKLLVkDPRARL 311
Cdd:cd05598 230 ANLSPEAKDLILRLCC-DAEDRL 251
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
62-323 1.77e-27

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: 111.17  E-value: 1.77e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRL---DKSKMVLPIAVEDVKREVQilialsgHENVVQFHNAFEDDDYVYI 138
Cdd:cd06647   9 YTRFEKIGQGASGTVYTAIDVATGQEVAIKQMnlqQQPKKELIINEILVMRENK-------NPNIVNYLDSYLVGDELWV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 139 VMELCEGGELLDRILSkkgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKsaqLDSPLKATDFGLSDFIKP 218
Cdd:cd06647  82 VMEYLAGGSLTDVVTE---TCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLG---MDGSVKLTDFGFCAQITP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 GKRFHD-IVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTE-DGIFKEVLRNKPDFSRKpwATISDSA 295
Cdd:cd06647 156 EQSKRStMVGTPYWMAPEVVTRKAyGPKVDIWSLGIMAIEMVEGEPPYLNENPlRALYLIATNGTPELQNP--EKLSAIF 233
                       250       260
                ....*....|....*....|....*...
gi 34098881 296 KDFVKKLLVKDPRARLTAAQALSHAWVR 323
Cdd:cd06647 234 RDFLNRCLEMDVEKRGSAKELLQHPFLK 261
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
68-323 1.78e-27

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: 112.44  E-value: 1.78e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEG-- 145
Cdd:cd06633  29 IGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKWQDIIKEVKFLQQLK-HPNTIEYKGCYLKDHTAWLVMEYCLGsa 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDriLSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLdspLKATDFGLSDFIKPGKRFhdi 225
Cdd:cd06633 108 SDLLE--VHKK--PLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQ---VKLADFGSASIASPANSF--- 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 226 VGSAYYVAPEVL----KRRSGPESDVWSIGvITYILLCGRRP--FWDRTEDGIFKEVLRNKPDFSRKPWatiSDSAKDFV 299
Cdd:cd06633 178 VGTPYWMAPEVIlamdEGQYDGKVDIWSLG-ITCIELAERKPplFNMNAMSALYHIAQNDSPTLQSNEW---TDSFRGFV 253
                       250       260
                ....*....|....*....|....
gi 34098881 300 KKLLVKDPRARLTAAQALSHAWVR 323
Cdd:cd06633 254 DYCLQKIPQERPSSAELLRHDFVR 277
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
68-323 1.93e-27

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: 111.00  E-value: 1.93e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEG-- 145
Cdd:cd06607   9 IGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTEKWQDIIKEVKFLRQLR-HPNTIEYKGCYLREHTAWLVMEYCLGsa 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDriLSKKGNRysEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKPGKRFhdi 225
Cdd:cd06607  88 SDIVE--VHKKPLQ--EVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTE---PGTVKLADFGSASLVCPANSF--- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 226 VGSAYYVAPEV-LKRRSGP---ESDVWSIGvITYILLCGRRP--FWDRTEDGIFKEVLRNKPDFSRKPWatiSDSAKDFV 299
Cdd:cd06607 158 VGTPYWMAPEViLAMDEGQydgKVDVWSLG-ITCIELAERKPplFNMNAMSALYHIAQNDSPTLSSGEW---SDDFRNFV 233
                       250       260
                ....*....|....*....|....
gi 34098881 300 KKLLVKDPRARLTAAQALSHAWVR 323
Cdd:cd06607 234 DSCLQKIPQDRPSAEDLLKHPFVT 257
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
60-322 2.58e-27

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: 111.27  E-value: 2.58e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLD-KSKMVLpiavEDVKREVQILiALSGHENVVQFHNAFEDDDYVYI 138
Cdd:cd06643   5 DFWEIVGELGDGAFGKVYKAQNKETGILAAAKVIDtKSEEEL----EDYMVEIDIL-ASCDHPNIVKLLDAFYYENNLWI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 139 VMELCEGGELlDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFksaQLDSPLKATDFGLS-DFIK 217
Cdd:cd06643  80 LIEFCAGGAV-DAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILF---TLDGDIKLADFGVSaKNTR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 218 PGKRFHDIVGSAYYVAPEVL------KRRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKP--Wa 289
Cdd:cd06643 156 TLQRRDSFIGTPYWMAPEVVmcetskDRPYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLAQPsrW- 234
                       250       260       270
                ....*....|....*....|....*....|...
gi 34098881 290 tiSDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd06643 235 --SPEFKDFLRKCLEKNVDARWTTSQLLQHPFV 265
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
62-319 3.27e-27

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: 110.09  E-value: 3.27e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRlDKSKMVLPIAVEDVKREVQILIALSGHENVVQFHNAFEDDDYVYIVME 141
Cdd:cd14050   3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKR-SRSRFRGEKDRKRKLEEVERHEKLGEHPNCVRFIKAWEEKGILYIQTE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGelLDRILSKKGnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFksaQLDSPLKATDFGL-SDFikPGK 220
Cdd:cd14050  82 LCDTS--LQQYCEETH-SLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFL---SKDGVCKLGDFGLvVEL--DKE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 221 RFHDIV-GSAYYVAPEVLKRRSGPESDVWSIG-----VITYILLCGRRPFWDRTEDGIFKEVLRNKpdfsrkpwatISDS 294
Cdd:cd14050 154 DIHDAQeGDPRYMAPELLQGSFTKAADIFSLGitileLACNLELPSGGDGWHQLRQGYLPEEFTAG----------LSPE 223
                       250       260
                ....*....|....*....|....*
gi 34098881 295 AKDFVKKLLVKDPRARLTAAQALSH 319
Cdd:cd14050 224 LRSIIKLMMDPDPERRPTAEDLLAL 248
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
68-326 3.39e-27

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: 111.28  E-value: 3.39e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVlpiAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEGGE 147
Cdd:cd06658  30 IGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQ---RRELLFNEVVIMRDYH-HENVVDMYNSYLVGDELWVVMEFLEGGA 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 148 LLDRILSkkgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGL-SDFIKPGKRFHDIV 226
Cdd:cd06658 106 LTDIVTH---TRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTS---DGRIKLSDFGFcAQVSKEVPKRKSLV 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 227 GSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDfSRKPWATISDSAKDFVKKLLVK 305
Cdd:cd06658 180 GTPYWMAPEVISRLPyGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDNLPP-RVKDSHKVSSVLRGFLDLMLVR 258
                       250       260
                ....*....|....*....|.
gi 34098881 306 DPRARLTAAQALSHAWVREGG 326
Cdd:cd06658 259 EPSQRATAQELLQHPFLKLAG 279
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
66-323 6.00e-27

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: 110.96  E-value: 6.00e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVA--IHRPNGDRV-AVKRLDKSKMVLpiAVEDV---KREVQILIALSgHENVVQFHNAFEDDDYVYIV 139
Cdd:cd05584   2 KVLGKGGYGKVFQVrkTTGSDKGKIfAMKVLKKASIVR--NQKDTahtKAERNILEAVK-HPFIVDLHYAFQTGGKLYLI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGELLDRiLSKKGnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLS-DFIKP 218
Cdd:cd05584  79 LEYLSGGELFMH-LEREG-IFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDA---QGHVKLTDFGLCkESIHD 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 GKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKpdFSRKPWatISDSAKD 297
Cdd:cd05584 154 GTVTHTFCGTIEYMAPEILTRSGhGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGK--LNLPPY--LTNEARD 229
                       250       260       270
                ....*....|....*....|....*....|.
gi 34098881 298 FVKKLLVKDPRARL-----TAAQALSHAWVR 323
Cdd:cd05584 230 LLKKLLKRNVSSRLgsgpgDAEEIKAHPFFR 260
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
59-311 6.52e-27

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: 112.43  E-value: 6.52e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  59 HDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILiALSGHENVVQFHNAFEDDDYVYI 138
Cdd:cd05600  10 LSDFQILTQVGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLNEVNHVLTERDIL-TTTNSPWLVKLLYAFQDPENVYL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 139 VMELCEGGELldRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLfksaqLDSP--LKATDFGLS--- 213
Cdd:cd05600  89 AMEYVPGGDF--RTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFL-----IDSSghIKLTDFGLAsgt 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 214 -----------------------------------DFIKPGKRFHDIVGSAYYVAPEVLKRRSGPES-DVWSIGVITYIL 257
Cdd:cd05600 162 lspkkiesmkirleevkntafleltakerrniyraMRKEDQNYANSVVGSPDYMAPEVLRGEGYDLTvDYWSLGCILFEC 241
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 258 LCGRRPFWDRTEDGIFKEVLRNKPDFSRKPW------ATISDSAKDFVKKLLVkDPRARL 311
Cdd:cd05600 242 LVGFPPFSGSTPNETWANLYHWKKTLQRPVYtdpdleFNLSDEAWDLITKLIT-DPQDRL 300
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
66-311 6.54e-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: 110.94  E-value: 6.54e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSGHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd05592   1 KVLGKGSFGKVMLAELKGTNQYFAIKALKKDVVLEDDDVECTMIERRVLALASQHPFLTHLFCTFQTESHLFFVMEYLNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRILSKKgnRYSEKDAAVVVRQMlkVAGECHLH--GLVHRDMKPENFLFKSaqlDSPLKATDFGL-SDFIKPGKRF 222
Cdd:cd05592  81 GDLMFHIQQSG--RFDEDRARFYGAEI--ICGLQFLHsrGIIYRDLKLDNVLLDR---EGHIKIADFGMcKENIYGENKA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 223 HDIVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRkpwaTISDSAKDFVKK 301
Cdd:cd05592 154 STFCGTPDYIAPEILKGQKYNQSvDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPHYPR----WLTKEAASCLSL 229
                       250
                ....*....|
gi 34098881 302 LLVKDPRARL 311
Cdd:cd05592 230 LLERNPEKRL 239
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
68-324 6.68e-27

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: 110.12  E-value: 6.68e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLD-KSKMVLpiavEDVKREVQILiALSGHENVVQFHNAFEDDDYVYIVMELCEGG 146
Cdd:cd06644  20 LGDGAFGKVYKAKNKETGALAAAKVIEtKSEEEL----EDYMVEIEIL-ATCNHPYIVKLLGAFYWDGKLWIMIEFCPGG 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 147 ELlDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKsaqLDSPLKATDFGLS-DFIKPGKRFHDI 225
Cdd:cd06644  95 AV-DAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLT---LDGDIKLADFGVSaKNVKTLQRRDSF 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 226 VGSAYYVAPEVL---KRRSGP---ESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKP--WatiSDSAKD 297
Cdd:cd06644 171 IGTPYWMAPEVVmceTMKDTPydyKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEPPTLSQPskW---SMEFRD 247
                       250       260
                ....*....|....*....|....*..
gi 34098881 298 FVKKLLVKDPRARLTAAQALSHAWVRE 324
Cdd:cd06644 248 FLKTALDKHPETRPSAAQLLEHPFVSS 274
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
62-322 1.15e-26

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: 109.01  E-value: 1.15e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRL---------DKSKMVLpiAVEDVKREVQILIALSgHENVVQFHNAFED 132
Cdd:cd06629   3 WVKGELIGKGTYGRVYLAMNATTGEMLAVKQVelpktssdrADSRQKT--VVDALKSEIDTLKDLD-HPNIVQYLGFEET 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 133 DDYVYIVMELCEGGElLDRILSKKGnRYSEKDAAVVVRQMLKvaGECHLH--GLVHRDMKPENFLfksAQLDSPLKATDF 210
Cdd:cd06629  80 EDYFSIFLEYVPGGS-IGSCLRKYG-KFEEDLVRFFTRQILD--GLAYLHskGILHRDLKADNIL---VDLEGICKISDF 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 211 GLSdfikpgKRFHDIV---------GSAYYVAPEVL---KRRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEV-- 276
Cdd:cd06629 153 GIS------KKSDDIYgnngatsmqGSVFWMAPEVIhsqGQGYSAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLgn 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 34098881 277 LRNKPDFsrKPWATISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd06629 227 KRSAPPV--PEDVNLSPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
68-321 1.30e-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: 1.30e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVK--RLD-KSKMVLPIAVedvkREVQILIALSgHENVVQFHNAFEDDDYVYIVMELce 144
Cdd:cd07835   7 IGEGTYGVVYKARDKLTGEIVALKkiRLEtEDEGVPSTAI----REISLLKELN-HPNIVRLLDVVHSENKLYLVFEF-- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 145 ggelLDRILSKKGNRYSE--KDAAVVVR---QMLKVAGECHLHGLVHRDMKPENFLFKSAQLdspLKATDFGLSD-FIKP 218
Cdd:cd07835  80 ----LDLDLKKYMDSSPLtgLDPPLIKSylyQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGA---LKLADFGLARaFGVP 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 GKRF-HDIVgSAYYVAPEVL---KRRSGPeSDVWSIGVItYILLCGRRPFW--DRTEDGIFK--EVL-----------RN 279
Cdd:cd07835 153 VRTYtHEVV-TLWYRAPEILlgsKHYSTP-VDIWSVGCI-FAEMVTRRPLFpgDSEIDQLFRifRTLgtpdedvwpgvTS 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 34098881 280 KPDF-------SRKPWATI----SDSAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd07835 230 LPDYkptfpkwARQDLSKVvpslDEDGLDLLSQMLVYDPAKRISAKAALQHPY 282
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
68-319 1.41e-26

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: 108.57  E-value: 1.41e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLpiavEDVKREVQILIALSGHENVVQ-FHNAFEDDDYVYIVMELCEGG 146
Cdd:cd13987   1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKL----KDFLREYNISLELSVHPHIIKtYDVAFETEDYYVFAQEYAPYG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 147 ELLDRILSKKGnrYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLdSPLKATDFGLSDfiKPGKRFHDIV 226
Cdd:cd13987  77 DLFSIIPPQVG--LPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDC-RRVKLCDFGLTR--RVGSTVKRVS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 227 GSAYYVAPEV--LKRRSG----PESDVWSIGVITYILLCGRRPfWDRT--EDGIFKEVLR---NKPDFSRKPWATISDSA 295
Cdd:cd13987 152 GTIPYTAPEVceAKKNEGfvvdPSIDVWAFGVLLFCCLTGNFP-WEKAdsDDQFYEEFVRwqkRKNTAVPSQWRRFTPKA 230
                       250       260
                ....*....|....*....|....
gi 34098881 296 KDFVKKLLVKDPRARLTAAQALSH 319
Cdd:cd13987 231 LRMFKKLLAPEPERRCSIKEVFKY 254
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
66-314 1.62e-26

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: 110.01  E-value: 1.62e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVA--IHRPNGDRV-AVKRLDKSKMVLPI-AVEDVKREVQILIALSGHENVVQFHNAFEDDDYVYIVME 141
Cdd:cd05614   6 KVLGTGAYGKVFLVrkVSGHDANKLyAMKVLRKAALVQKAkTVEHTRTERNVLEHVRQSPFLVTLHYAFQTDAKLHLILD 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELLDRILSKkgNRYSEKDAAVVVRQMLkVAGEcHLH--GLVHRDMKPENFLFKSaqlDSPLKATDFGLS-DFIKP 218
Cdd:cd05614  86 YVSGGELFTHLYQR--DHFSEDEVRFYSGEII-LALE-HLHklGIVYRDIKLENILLDS---EGHVVLTDFGLSkEFLTE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 GK-RFHDIVGSAYYVAPEVLKRRSG--PESDVWSIGVITYILLCGRRPFW----DRTEDGIFKEVLRNKPDFSrkpwATI 291
Cdd:cd05614 159 EKeRTYSFCGTIEYMAPEIIRGKSGhgKAVDWWSLGILMFELLTGASPFTlegeKNTQSEVSRRILKCDPPFP----SFI 234
                       250       260
                ....*....|....*....|...
gi 34098881 292 SDSAKDFVKKLLVKDPRARLTAA 314
Cdd:cd05614 235 GPVARDLLQKLLCKDPKKRLGAG 257
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
60-322 1.87e-26

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


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 108.90  E-value: 1.87e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIA-----------------------VEDVKREVQILIA 116
Cdd:cd14199   2 NQYKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLMRQAGfprrppprgaraapegctqprgpIERVYQEIAILKK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 117 LSgHENVVQFHNAFED--DDYVYIVMELCEGGELLDRILSKKgnrYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENF 194
Cdd:cd14199  82 LD-HPNVVKLVEVLDDpsEDHLYMVFELVKQGPVMEVPTLKP---LSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 195 LFKSaqlDSPLKATDFGLSDFIKPGKRF-HDIVGSAYYVAPEVL----KRRSGPESDVWSIGVITYILLCGRRPFWDRTE 269
Cdd:cd14199 158 LVGE---DGHIKIADFGVSNEFEGSDALlTNTVGTPAFMAPETLsetrKIFSGKALDVWAMGVTLYCFVFGQCPFMDERI 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 34098881 270 DGIFKEVLRNKPDFSRKPwaTISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14199 235 LSLHSKIKTQPLEFPDQP--DISDDLKDLLFRMLDKNPESRISVPEIKLHPWV 285
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
62-322 1.99e-26

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: 107.89  E-value: 1.99e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRP---NGDRVAVKRLDKSKMVlPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYI 138
Cdd:cd08222   2 YRVVRKLGSGNFGTVYLVSDLKataDEELKVLKEISVGELQ-PDETVDANREAKLLSKLD-HPAIVKFHDSFVEKESFCI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 139 VMELCEGGELLDRILS--KKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKsaqlDSPLKATDFGLSDFI 216
Cdd:cd08222  80 VTEYCEGGDLDDKISEykKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLK----NNVIKVGDFGISRIL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 217 KPGKRFHD-IVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNK----PDFSRKPwat 290
Cdd:cd08222 156 MGTSDLATtFTGTPYYMSPEVLKHEGyNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGEtpslPDKYSKE--- 232
                       250       260       270
                ....*....|....*....|....*....|..
gi 34098881 291 isdsAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd08222 233 ----LNAIYSRMLNKDPALRPSAAEILKIPFI 260
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
57-323 2.19e-26

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: 108.93  E-value: 2.19e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  57 DFHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDkskmvlPIAV--EDVKREVQILIALSGHENVVQFHNAF-EDD 133
Cdd:cd06639  19 DPSDTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILD------PISDvdEEIEAEYNILRSLPNHPNVVKFYGMFyKAD 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 134 DYV----YIVMELCEGGELLDRI--LSKKGNRYSEKDAAVVVRQMLkvAGECHLHG--LVHRDMKPENFLFKSaqlDSPL 205
Cdd:cd06639  93 QYVggqlWLVLELCNGGSVTELVkgLLKCGQRLDEAMISYILYGAL--LGLQHLHNnrIIHRDVKGNNILLTT---EGGV 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 206 KATDFGLSDFIKPGK-RFHDIVGSAYYVAPEVLKRRSGPES------DVWSIGVITYILLCGRRPFWDRTEDGIFKEVLR 278
Cdd:cd06639 168 KLVDFGVSAQLTSARlRRNTSVGTPFWMAPEVIACEQQYDYsydarcDVWSLGITAIELADGDPPLFDMHPVKALFKIPR 247
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 34098881 279 NKPDFSRKP--WAtisDSAKDFVKKLLVKDPRARLTAAQALSHAWVR 323
Cdd:cd06639 248 NPPPTLLNPekWC---RGFSHFISQCLIKDFEKRPSVTHLLEHPFIK 291
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
68-322 2.76e-26

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: 107.88  E-value: 2.76e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDkskmvlpiavEDVKREVQIL---IALSG---HENVVQFHNAFEDDDYVYIVME 141
Cdd:cd06624  16 LGKGTFGVVYAARDLSTQVRIAIKEIP----------ERDSREVQPLheeIALHSrlsHKNIVQYLGSVSEDGFFKIFME 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELLDRILSKKGN-RYSEKDAAVVVRQMLKvaGECHLHG--LVHRDMKPENFLFKSaqLDSPLKATDFGLSdfikp 218
Cdd:cd06624  86 QVPGGSLSALLRSKWGPlKDNENTIGYYTKQILE--GLKYLHDnkIVHRDIKGDNVLVNT--YSGVVKISDFGTS----- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 gKRFHDI-------VGSAYYVAPEVL---KRRSGPESDVWSIGVITYILLCGRRPFWDRTED-------GIFKEvlrnKP 281
Cdd:cd06624 157 -KRLAGInpctetfTGTLQYMAPEVIdkgQRGYGPPADIWSLGCTIIEMATGKPPFIELGEPqaamfkvGMFKI----HP 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 34098881 282 DFSrkpwATISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd06624 232 EIP----ESLSEEAKSFILRCFEPDPDKRATASDLLQDPFL 268
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
66-319 3.16e-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: 107.74  E-value: 3.16e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGyTYVAIHRPNGDRVAVKRLdkskmvLPIAVEDVKREVQILIALSGHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd13982   7 KVLGYGSEG-TIVFRGTFDGRPVAVKRL------LPEFFDFADREVQLLRESDEHPNVIRYFCTEKDRQFLYIALELCAA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 G--ELLDRILSKKGNRYSEKDAAVVVRQMlkVAGECHLH--GLVHRDMKPENFLFKSAQLDSPLKA--TDFGLSDFIKPG 219
Cdd:cd13982  80 SlqDLVESPRESKLFLRPGLEPVRLLRQI--ASGLAHLHslNIVHRDLKPQNILISTPNAHGNVRAmiSDFGLCKKLDVG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 220 K----RFHDIVGSAYYVAPEVL----KRRSGPESDVWSIG-VITYILLCGRRPFWDRTEDGifKEVLRNKPDFSR-KPWA 289
Cdd:cd13982 158 RssfsRRSGVAGTSGWIAPEMLsgstKRRQTRAVDIFSLGcVFYYVLSGGSHPFGDKLERE--ANILKGKYSLDKlLSLG 235
                       250       260       270
                ....*....|....*....|....*....|
gi 34098881 290 TISDSAKDFVKKLLVKDPRARLTAAQALSH 319
Cdd:cd13982 236 EHGPEAQDLIERMIDFDPEKRPSAEEVLNH 265
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
60-308 3.64e-26

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


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 110.48  E-value: 3.64e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVaIHRPNGDRV-AVKRLDKSKMVLPIAVEDVKREVQILIalSGH-ENVVQFHNAFEDDDYVY 137
Cdd:cd05624  72 DDFEIIKVIGRGAFGEVAV-VKMKNTERIyAMKILNKWEMLKRAETACFREERNVLV--NGDcQWITTLHYAFQDENYLY 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 138 IVMELCEGGELLDrILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFksaQLDSPLKATDFGLS-DFI 216
Cdd:cd05624 149 LVMDYYVGGDLLT-LLSKFEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLL---DMNGHIRLADFGSClKMN 224
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 217 KPGKRFHDI-VGSAYYVAPEVLKR------RSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWA 289
Cdd:cd05624 225 DDGTVQSSVaVGTPDYISPEILQAmedgmgKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEERFQFPSHV 304
                       250       260
                ....*....|....*....|
gi 34098881 290 T-ISDSAKDFVKKLLVKDPR 308
Cdd:cd05624 305 TdVSEEAKDLIQRLICSRER 324
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
60-333 4.43e-26

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 108.93  E-value: 4.43e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLdkSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDY---- 135
Cdd:cd07849   5 PRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKI--SPFEHQTYCLRTLREIKILLRFK-HENIIGILDIQRPPTFesfk 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 136 -VYIVMELCEGGelLDRILskKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAqldSPLKATDFGLSD 214
Cdd:cd07849  82 dVYIVQELMETD--LYKLI--KTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTN---CDLKICDFGLAR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 215 FIKPGkrfHD-------IVGSAYYVAPEVLKRRSGPES--DVWSIGVITYILLCGRRPFWDR----------------TE 269
Cdd:cd07849 155 IADPE---HDhtgflteYVATRWYRAPEIMLNSKGYTKaiDIWSVGCILAEMLSNRPLFPGKdylhqlnlilgilgtpSQ 231
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34098881 270 DGIF-------KEVLRNKPDFSRKPWATI----SDSAKDFVKKLLVKDPRARLTAAQALSHAWVREGGNATDIPV 333
Cdd:cd07849 232 EDLNciislkaRNYIKSLPFKPKVPWNKLfpnaDPKALDLLDKMLTFNPHKRITVEEALAHPYLEQYHDPSDEPV 306
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
62-322 6.54e-26

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: 106.59  E-value: 6.54e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMV----LPIAVEdVKREVQILIAL-SGHENVVQFHNAFEDDDYV 136
Cdd:cd14100   2 YQVGPLLGSGGFGSVYSGIRVADGAPVAIKHVEKDRVSewgeLPNGTR-VPMEIVLLKKVgSGFRGVIRLLDWFERPDSF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 137 YIVMELCEGGELLDRILSKKGnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDspLKATDFGLSDFI 216
Cdd:cd14100  81 VLVLERPEPVQDLFDFITERG-ALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDLNTGE--LKLIDFGSGALL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 217 KpGKRFHDIVGSAYYVAPEVLK--RRSGPESDVWSIGVITYILLCGRRPFwdrTEDgifKEVLRNKPDFSRKpwatISDS 294
Cdd:cd14100 158 K-DTVYTDFDGTRVYSPPEWIRfhRYHGRSAAVWSLGILLYDMVCGDIPF---EHD---EEIIRGQVFFRQR----VSSE 226
                       250       260
                ....*....|....*....|....*...
gi 34098881 295 AKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14100 227 CQHLIKWCLALRPSDRPSFEDIQNHPWM 254
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
45-313 6.76e-26

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: 108.57  E-value: 6.76e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  45 PCGKRTDFGYSKdfhdhytigkLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSGHENVV 124
Cdd:cd05602   2 PHAKPSDFHFLK----------VIGKGSFGKVLLARHKSDEKFYAVKVLQKKAILKKKEEKHIMSERNVLLKNVKHPFLV 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 125 QFHNAFEDDDYVYIVMELCEGGELLDRILSKKGnrYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSP 204
Cdd:cd05602  72 GLHFSFQTTDKLYFVLDYINGGELFYHLQRERC--FLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDS---QGH 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 205 LKATDFGL-SDFIKPGKRFHDIVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCGRRPFWDRTEDGIFKEVLrNKPd 282
Cdd:cd05602 147 IVLTDFGLcKENIEPNGTTSTFCGTPEYLAPEVLHKQPYDRTvDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNIL-NKP- 224
                       250       260       270
                ....*....|....*....|....*....|.
gi 34098881 283 FSRKPwaTISDSAKDFVKKLLVKDPRARLTA 313
Cdd:cd05602 225 LQLKP--NITNSARHLLEGLLQKDRTKRLGA 253
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
68-321 6.93e-26

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: 107.18  E-value: 6.93e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVK--RLDKSKMVLPIAVedvkREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd07836   8 LGEGTYATVYKGRNRTTGEIVALKeiHLDAEEGTPSTAI----REISLMKELK-HENIVRLHDVIHTENKLMLVFEYMDK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GelLDRILSKKGNRYSEKDAAV--VVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLS-DFIKPGKRF 222
Cdd:cd07836  83 D--LKKYMDTHGVRGALDPNTVksFTYQLLKGIAFCHENRVLHRDLKPQNLLINK---RGELKLADFGLArAFGIPVNTF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 223 HDIVGSAYYVAPEVL--KRRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDSAK---- 296
Cdd:cd07836 158 SNEVVTLWYRAPDVLlgSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRIMGTPTESTWPGISQLPEykpt 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 34098881 297 ---------------------DFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd07836 238 fpryppqdlqqlfphadplgiDLLHRLLQLNPELRISAHDALQHPW 283
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
61-317 8.10e-26

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: 106.36  E-value: 8.10e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTyvAIHRPNGD-------RVAVKRLDKSKMvlpiavEDVKREVQILiALSGHENVVQFHNAFEDD 133
Cdd:cd08221   1 HYIPVRVLGRGAFGEA--VLYRKTEDnslvvwkEVNLSRLSEKER------RDALNEIDIL-SLLNHDNIITYYNHFLDG 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 134 DYVYIVMELCEGGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLdspLKATDFGLS 213
Cdd:cd08221  72 ESLFIEMEYCNGGNLHDKIAQQKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADL---VKLGDFGIS 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 214 DFIKPGKRFHD-IVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFwDRTEDgifkevLRNKPDFSRKPWATI 291
Cdd:cd08221 149 KVLDSESSMAEsIVGTPYYMSPELVQGVKyNFKSDIWAVGCVLYELLTLKRTF-DATNP------LRLAVKIVQGEYEDI 221
                       250       260       270
                ....*....|....*....|....*....|
gi 34098881 292 ----SDSAKDFVKKLLVKDPRARLTAAQAL 317
Cdd:cd08221 222 deqySEEIIQLVHDCLHQDPEDRPTAEELL 251
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
51-321 1.32e-25

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 107.07  E-value: 1.32e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  51 DFGYSKDFHDHYTIGKLlGHGQFGYTYVAIHRPNGDRVAVKR--LDKSKMVLPIAVedvKREVQILIALSgHENVVQF-- 126
Cdd:cd07865   4 EFPFCDEVSKYEKLAKI-GQGTFGEVFKARHRKTGQIVALKKvlMENEKEGFPITA---LREIKILQLLK-HENVVNLie 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 127 --------HNAFEDDdyVYIVMELCEGGelLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKS 198
Cdd:cd07865  79 icrtkatpYNRYKGS--IYLVFEFCEHD--LAGLLSNKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 199 aqlDSPLKATDFGLS-DFIKP----GKRFHDIVGSAYYVAPEVL--KRRSGPESDVWSIGVI------------------ 253
Cdd:cd07865 155 ---DGVLKLADFGLArAFSLAknsqPNRYTNRVVTLWYRPPELLlgERDYGPPIDMWGAGCImaemwtrspimqgnteqh 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 254 --TYIL-LCG-----------RRPFWDRTE---DGIFKEVLRNKPDFSrkpwatiSDSAKDFVKKLLVKDPRARLTAAQA 316
Cdd:cd07865 232 qlTLISqLCGsitpevwpgvdKLELFKKMElpqGQKRKVKERLKPYVK-------DPYALDLIDKLLVLDPAKRIDADTA 304

                ....*
gi 34098881 317 LSHAW 321
Cdd:cd07865 305 LNHDF 309
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
66-311 1.40e-25

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: 107.81  E-value: 1.40e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILiALSGHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd05594  31 KLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVL-QNSRHPFLTALKYSFQTHDRLCFVMEYANG 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELL-----DRILSKKGNRYSekdAAVVVRQMLKVAGEchlHGLVHRDMKPENFLFKSaqlDSPLKATDFGL-SDFIKPG 219
Cdd:cd05594 110 GELFfhlsrERVFSEDRARFY---GAEIVSALDYLHSE---KNVVYRDLKLENLMLDK---DGHIKITDFGLcKEGIKDG 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 220 KRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRkpwaTISDSAKDF 298
Cdd:cd05594 181 ATMKTFCGTPEYLAPEVLEDNDyGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPR----TLSPEAKSL 256
                       250
                ....*....|...
gi 34098881 299 VKKLLVKDPRARL 311
Cdd:cd05594 257 LSGLLKKDPKQRL 269
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
71-321 1.54e-25

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


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 106.54  E-value: 1.54e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  71 GQFGYTYVAIHRPNGDRVAVKRL--DKSKMVLPIAVedvKREVQILIALSgHENVVQFHNAF--EDDDYVYIVMELCEGg 146
Cdd:cd07843  16 GTYGVVYRARDKKTGEIVALKKLkmEKEKEGFPITS---LREINILLKLQ-HPNIVTVKEVVvgSNLDKIYMVMEYVEH- 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 147 ELLDrILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLF-KSAQldspLKATDFGLS-DFIKPGKRFHD 224
Cdd:cd07843  91 DLKS-LMETMKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLnNRGI----LKICDFGLArEYGSPLKPYTQ 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 225 IVGSAYYVAPEVL--KRRSGPESDVWSIGVITYILLCGRRPFWDRTE----DGIFKEV----LRNKPDFSRKPWA----- 289
Cdd:cd07843 166 LVVTLWYRAPELLlgAKEYSTAIDMWSVGCIFAELLTKKPLFPGKSEidqlNKIFKLLgtptEKIWPGFSELPGAkkktf 245
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 34098881 290 ---------------TISDSAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd07843 246 tkypynqlrkkfpalSLSDNGFDLLNRLLTYDPAKRISAEDALKHPY 292
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
57-334 1.71e-25

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: 107.38  E-value: 1.71e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  57 DFHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKskmvlPI-AVEDVK---REVQILiALSGHENVVQFHNAF-- 130
Cdd:cd07851  12 EVPDRYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSR-----PFqSAIHAKrtyRELRLL-KHMKHENVIGLLDVFtp 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 131 ----EDDDYVYIVMELCegGELLDRILskKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLK 206
Cdd:cd07851  86 asslEDFQDVYLVTHLM--GADLNNIV--KCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNE---DCELK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 207 ATDFGLSDfiKPGKRFHDIVGSAYYVAPEVL--KRRSGPESDVWSIGVITYILLCGRRPFwdRTEDGI------------ 272
Cdd:cd07851 159 ILDFGLAR--HTDDEMTGYVATRWYRAPEIMlnWMHYNQTVDIWSVGCIMAELLTGKTLF--PGSDHIdqlkrimnlvgt 234
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34098881 273 -------------FKEVLRNKPDFSRKPWATI----SDSAKDFVKKLLVKDPRARLTAAQALSHAWVREGGNATDIPVD 334
Cdd:cd07851 235 pdeellkkissesARNYIQSLPQMPKKDFKEVfsgaNPLAIDLLEKMLVLDPDKRITAAEALAHPYLAEYHDPEDEPVA 313
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
64-321 1.76e-25

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: 105.92  E-value: 1.76e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  64 IGKLlGHGQFGYTYVAIHRPNGDRVAVKRLDKSK---MVLPIAVedvkREVQILIALSgHENVVQFHNAFEDDDYVYIVM 140
Cdd:cd07847   6 LSKI-GEGSYGVVFKCRNRETGQIVAIKKFVESEddpVIKKIAL----REIRMLKQLK-HPNLVNLIEVFRRKRKLHLVF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCEGgELLDRiLSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLF-KSAQldspLKATDFGLSDFIK-P 218
Cdd:cd07847  80 EYCDH-TVLNE-LEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILItKQGQ----IKLCDFGFARILTgP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 GKRFHDIVGSAYYVAPEVL--KRRSGPESDVWSIGVITYILLCGrRPFWDRTED-------------------------G 271
Cdd:cd07847 154 GDDYTDYVATRWYRAPELLvgDTQYGPPVDVWAIGCVFAELLTG-QPLWPGKSDvdqlylirktlgdliprhqqifstnQ 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 34098881 272 IFKEVLRNKPDfSRKP----WATISDSAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd07847 233 FFKGLSIPEPE-TREPleskFPNISSPALSFLKGCLQMDPTERLSCEELLEHPY 285
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
60-303 1.92e-25

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


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 108.56  E-value: 1.92e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVaIHRPNGDRV-AVKRLDKSKMVLPIAVEDVKREVQILIAlSGHENVVQFHNAFEDDDYVYI 138
Cdd:cd05623  72 EDFEILKVIGRGAFGEVAV-VKLKNADKVfAMKILNKWEMLKRAETACFREERDVLVN-GDSQWITTLHYAFQDDNNLYL 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 139 VMELCEGGELLDrILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFksaQLDSPLKATDFGLS-DFIK 217
Cdd:cd05623 150 VMDYYVGGDLLT-LLSKFEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILM---DMNGHIRLADFGSClKLME 225
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 218 PGKRFHDI-VGSAYYVAPEVL------KRRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWAT 290
Cdd:cd05623 226 DGTVQSSVaVGTPDYISPEILqamedgKGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKERFQFPTQVT 305
                       250
                ....*....|....
gi 34098881 291 -ISDSAKDFVKKLL 303
Cdd:cd05623 306 dVSENAKDLIRRLI 319
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
61-322 2.53e-25

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: 105.13  E-value: 2.53e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRL--DKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFED--DDYV 136
Cdd:cd06652   3 NWRLGKLLGQGAFGRVYLCYDADTGRELAVKQVqfDPESPETSKEVNALECEIQLLKNLL-HERIVQYYGCLRDpqERTL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 137 YIVMELCEGGELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAqldSPLKATDFGLSDFI 216
Cdd:cd06652  82 SIFMEYMPGGSIKDQL--KSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSV---GNVKLGDFGASKRL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 217 K----PGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGViTYILLCGRRPFWDRTE--DGIFKevLRNKPDFSRKPwA 289
Cdd:cd06652 157 QticlSGTGMKSVTGTPYWMSPEVISGEGyGRKADIWSVGC-TVVEMLTEKPPWAEFEamAAIFK--IATQPTNPQLP-A 232
                       250       260       270
                ....*....|....*....|....*....|...
gi 34098881 290 TISDSAKDFVKKLLVkDPRARLTAAQALSHAWV 322
Cdd:cd06652 233 HVSDHCRDFLKRIFV-EAKLRPSADELLRHTFV 264
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
66-276 2.61e-25

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: 104.93  E-value: 2.61e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGD---RVAVKRLDKSKMvlPIAVEDVKREVQILIALsGHENVVQFHNAFEDDDYVYIVMEL 142
Cdd:cd00192   1 KKLGEGAFGEVYKGKLKGGDGktvDVAVKTLKEDAS--ESERKDFLKEARVMKKL-GHPNVVRLLGVCTEEEPLYLVMEY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 143 CEGGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGEC-----HLH--GLVHRDMKPENFLFKSaqlDSPLKATDFGLSDF 215
Cdd:cd00192  78 MEGGDLLDFLRKSRPVFPSPEPSTLSLKDLLSFAIQIakgmeYLAskKFVHRDLAARNCLVGE---DLVVKISDFGLSRD 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34098881 216 IKPGKrfhdivgsaYYV------------APEVLK-RRSGPESDVWSIGVITY-ILLCGRRPFWDRTEDGIFKEV 276
Cdd:cd00192 155 IYDDD---------YYRkktggklpirwmAPESLKdGIFTSKSDVWSFGVLLWeIFTLGATPYPGLSNEEVLEYL 220
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
66-314 2.80e-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: 106.33  E-value: 2.80e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVA--IHRPN-GDRVAVKRLDKSKMvlpiAVED---VKREVQILIALSgHENVVQFHNAFEDDDYVYIV 139
Cdd:cd05582   1 KVLGQGSFGKVFLVrkITGPDaGTLYAMKVLKKATL----KVRDrvrTKMERDILADVN-HPFIVKLHYAFQTEGKLYLI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGELLDRiLSKKgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLS-DFIKP 218
Cdd:cd05582  76 LDFLRGGDLFTR-LSKE-VMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDE---DGHIKLTDFGLSkESIDH 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 GKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNK---PDFsrkpwatISDS 294
Cdd:cd05582 151 EKKAYSFCGTVEYMAPEVVNRRGhTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKlgmPQF-------LSPE 223
                       250       260
                ....*....|....*....|
gi 34098881 295 AKDFVKKLLVKDPRARLTAA 314
Cdd:cd05582 224 AQSLLRALFKRNPANRLGAG 243
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
62-322 2.88e-25

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: 104.65  E-value: 2.88e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILI---ALSGHENVVQFHNAFEDDDYVYI 138
Cdd:cd14102   2 YQVGSVLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEWGTLNGVMVPLEIVLlkkVGSGFRGVIKLLDWYERPDGFLI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 139 VMELCEGGELLDRILSKKGnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAqlDSPLKATDFGLSDFIKp 218
Cdd:cd14102  82 VMERPEPVKDLFDFITEKG-ALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLR--TGELKLIDFGSGALLK- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 GKRFHDIVGSAYYVAPEVLK--RRSGPESDVWSIGVITYILLCGRRPFwdrTEDgifKEVLRNKPDFSRKpwatISDSAK 296
Cdd:cd14102 158 DTVYTDFDGTRVYSPPEWIRyhRYHGRSATVWSLGVLLYDMVCGDIPF---EQD---EEILRGRLYFRRR----VSPECQ 227
                       250       260
                ....*....|....*....|....*.
gi 34098881 297 DFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14102 228 QLIKWCLSLRPSDRPTLEQIFDHPWM 253
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
62-322 3.29e-25

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: 104.66  E-value: 3.29e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEdvkrEVQILIALSGH-----ENVVQFHNAFEDDDYV 136
Cdd:cd14133   1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDYLDQSLD----EIRLLELLNKKdkadkYHIVRLKDVFYFKNHL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 137 YIVMELCeGGELLDRILSKKGNRYSEKDAAVVVRQMLKvaGECHLH--GLVHRDMKPENFLFKSaQLDSPLKATDFGLSD 214
Cdd:cd14133  77 CIVFELL-SQNLYEFLKQNKFQYLSLPRIRKIAQQILE--ALVFLHslGLIHCDLKPENILLAS-YSRCQIKIIDFGSSC 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 215 FIkpGKRFHDIVGSAYYVAPEV-LKRRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEV--LRNKPDFsRKPWATI 291
Cdd:cd14133 153 FL--TQRLYSYIQSRYYRAPEViLGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIigTIGIPPA-HMLDQGK 229
                       250       260       270
                ....*....|....*....|....*....|...
gi 34098881 292 SDSAK--DFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14133 230 ADDELfvDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
61-322 3.56e-25

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: 104.72  E-value: 3.56e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRL--DKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDD--YV 136
Cdd:cd06653   3 NWRLGKLLGRGAFGEVYLCYDADTGRELAVKQVpfDPDSQETSKEVNALECEIQLLKNLR-HDRIVQYYGCLRDPEekKL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 137 YIVMELCEGGELLDRIlsKKGNRYSEKDAAVVVRQMLKvaGECHLHG--LVHRDMKPENFLFKSAqldSPLKATDFGLSD 214
Cdd:cd06653  82 SIFVEYMPGGSVKDQL--KAYGALTENVTRRYTRQILQ--GVSYLHSnmIVHRDIKGANILRDSA---GNVKLGDFGASK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 215 FIK----PGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGViTYILLCGRRPFWDRTE--DGIFKevLRNKPDFSRKP 287
Cdd:cd06653 155 RIQticmSGTGIKSVTGTPYWMSPEVISGEGyGRKADVWSVAC-TVVEMLTEKPPWAEYEamAAIFK--IATQPTKPQLP 231
                       250       260       270
                ....*....|....*....|....*....|....*
gi 34098881 288 wATISDSAKDFVKKLLVKDPRaRLTAAQALSHAWV 322
Cdd:cd06653 232 -DGVSDACRDFLRQIFVEEKR-RPTAEFLLRHPFV 264
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
68-322 3.87e-25

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 105.20  E-value: 3.87e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLdkSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAF--EDDDYVYIVMELCEG 145
Cdd:cd06621   9 LGEGAGGSVTKCRLRNTKTIFALKTI--TTDPNPDVQKQILRELEINKSCA-SPYIVKYYGAFldEQDSSIGIAMEYCEG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELlDRI---LSKKGNRYSEKdaavvvrQMLKVAgECHLHGL--------VHRDMKPENFLFKSaqlDSPLKATDFGLS- 213
Cdd:cd06621  86 GSL-DSIykkVKKKGGRIGEK-------VLGKIA-ESVLKGLsylhsrkiIHRDIKPSNILLTR---KGQVKLCDFGVSg 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 214 DFIKPG-KRFhdiVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDG------------IFKEVLRN 279
Cdd:cd06621 154 ELVNSLaGTF---TGTSYYMAPERIQGGPySITSDVWSLGLTLLEVAQNRFPFPPEGEPPlgpiellsyivnMPNPELKD 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 34098881 280 KPDFSRKpWatiSDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd06621 231 EPENGIK-W---SESFKDFIEKCLEKDGTRRPGPWQMLAHPWI 269
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
66-324 3.95e-25

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 106.04  E-value: 3.95e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAiHRPNGDRV-AVKRLDKSKMVLPIAVEDVKREVQILIALSGHENVVQFHNAFEDDDYVYIVMELCE 144
Cdd:cd05591   1 KVLGKGSFGKVMLA-ERKGTDEVyAIKVLKKDVILQDDDVDCTMTEKRILALAAKHPFLTALHSCFQTKDRLFFVMEYVN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 145 GGELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGL-SDFIKPGKRFH 223
Cdd:cd05591  80 GGDLMFQI--QRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDA---EGHCKLADFGMcKEGILNGKTTT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 224 DIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNkpDFSRKPWatISDSAKDFVKKL 302
Cdd:cd05591 155 TFCGTPDYIAPEILQELEyGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHD--DVLYPVW--LSKEAVSILKAF 230
                       250       260
                ....*....|....*....|....*....
gi 34098881 303 LVKDPRARL--TAAQA-----LSHAWVRE 324
Cdd:cd05591 231 MTKNPAKRLgcVASQGgedaiRQHPFFRE 259
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
61-231 6.10e-25

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: 104.08  E-value: 6.10e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKrLDKSKMVLPIavedVKREVQILIALSGHENVVQFHNAFEDDDYVYIVM 140
Cdd:cd14016   1 RYKLVKKIGSGSFGEVYLGIDLKTGEEVAIK-IEKKDSKHPQ----LEYEAKVYKLLQGGPGIPRLYWFGQEGDYNVMVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCegGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLSD-FIKPG 219
Cdd:cd14016  76 DLL--GPSLEDLFNKCGRKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNKVYLIDFGLAKkYRDPR 153
                       170
                ....*....|....*....
gi 34098881 220 KRFH-------DIVGSAYY 231
Cdd:cd14016 154 TGKHipyregkSLTGTARY 172
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
62-322 9.67e-25

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: 103.02  E-value: 9.67e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFE-DDDYVYIVM 140
Cdd:cd14164   2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPDFVQKFLPRELSILRRVN-HPNIVQMFECIEvANGRLYIVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCEGgELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAqlDSPLKATDFGLSDFIK-PG 219
Cdd:cd14164  81 EAAAT-DLLQKI--QEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSAD--DRKIKIADFGFARFVEdYP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 220 KRFHDIVGSAYYVAPEVLKR--RSGPESDVWSIGVITYILLCGRRPFwdrteDGIFKEVLRNKPDFSRKPWA-TISDSAK 296
Cdd:cd14164 156 ELSTTFCGSRAYTPPEVILGtpYDPKKYDVWSLGVVLYVMVTGTMPF-----DETNVRRLRLQQRGVLYPSGvALEEPCR 230
                       250       260
                ....*....|....*....|....*.
gi 34098881 297 DFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14164 231 ALIRTLLQFNPSTRPSIQQVAGNSWL 256
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
68-311 1.28e-24

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: 103.38  E-value: 1.28e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILiALSGHENVVQFHNAFEDDDYVYIVMELCEGGE 147
Cdd:cd05577   1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMALNEKIIL-EKVSSPFIVSLAYAFETKDKLCLVLTLMNGGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 148 LLDRILSKKGNRYSEKDAAVVVRQMlkVAGECHLH--GLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKPGKRFHDI 225
Cdd:cd05577  80 LKYHIYNVGTRGFSEARAIFYAAEI--ICGLEHLHnrFIVYRDLKPENILLDD---HGHVRISDLGLAVEFKGGKKIKGR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 226 VGSAYYVAPEVLKRRSGPES--DVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDSAKDFVKKLL 303
Cdd:cd05577 155 VGTHGYMAPEVLQKEVAYDFsvDWFALGCMLYEMIAGRSPFRQRKEKVDKEELKRRTLEMAVEYPDSFSPEARSLCEGLL 234

                ....*...
gi 34098881 304 VKDPRARL 311
Cdd:cd05577 235 QKDPERRL 242
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
66-311 1.29e-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: 104.78  E-value: 1.29e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILiALSGHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd05593  21 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVL-KNTRHPFLTSLKYSFQTKDRLCFVMEYVNG 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELL-----DRILSKKGNRYSEKDAAVVVRQMlkvagecHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGL-SDFIKPG 219
Cdd:cd05593 100 GELFfhlsrERVFSEDRTRFYGAEIVSALDYL-------HSGKIVYRDLKLENLMLDK---DGHIKITDFGLcKEGITDA 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 220 KRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRkpwaTISDSAKDF 298
Cdd:cd05593 170 ATMKTFCGTPEYLAPEVLEDNDyGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPR----TLSADAKSL 245
                       250
                ....*....|...
gi 34098881 299 VKKLLVKDPRARL 311
Cdd:cd05593 246 LSGLLIKDPNKRL 258
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
68-328 1.49e-24

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: 103.39  E-value: 1.49e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKR----LDKSKMvlpiavEDVKREVQILialsgHENV----VQFHNAFEDDDYVYIV 139
Cdd:cd06622   9 LGKGNYGSVYKVLHRPTGVTMAMKEirleLDESKF------NQIIMELDIL-----HKAVspyiVDFYGAFFIEGAVYMC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGELlDRiLSKKGNRYSEKDAAVVVR------QMLKVAGEchLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLS 213
Cdd:cd06622  78 MEYMDAGSL-DK-LYAGGVATEGIPEDVLRRityavvKGLKFLKE--EHNIIHRDVKPTNVLVNG---NGQVKLCDFGVS 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 214 DFIKPGKRFHDIvGSAYYVAPEVLKRrSGP--------ESDVWSIGVITYILLCGRRPFWDRTEDGIFKE---VLRNKPd 282
Cdd:cd06622 151 GNLVASLAKTNI-GCQSYMAPERIKS-GGPnqnptytvQSDVWSLGLSILEMALGRYPYPPETYANIFAQlsaIVDGDP- 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 34098881 283 fSRKPwATISDSAKDFVKKLLVKDPRARLTAAQALSHAWVREGGNA 328
Cdd:cd06622 228 -PTLP-SGYSDDAQDFVAKCLNKIPNRRPTYAQLLEHPWLVKYKNA 271
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
62-319 2.10e-24

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: 103.12  E-value: 2.10e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKR----LDKSKMvlPIAVedvKREVQILIAL--SGHENVVQFHNAFEDDDY 135
Cdd:cd07838   1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKvrvpLSEEGI--PLST---IREIALLKQLesFEHPNVVRLLDVCHGPRT 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 136 -----VYIVMELCEggELLDRILSK---KGnrYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKA 207
Cdd:cd07838  76 drelkLTLVFEHVD--QDLATYLDKcpkPG--LPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTS---DGQVKL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 208 TDFGLSDFIKPGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLcGRRP-FWDRTE----DGIFK------- 274
Cdd:cd07838 149 ADFGLARIYSFEMALTSVVVTLWYRAPEVLLQSSyATPVDMWSVGCIFAELF-NRRPlFRGSSEadqlGKIFDviglpse 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 34098881 275 -----EVLRNKPDFSR-------KPWATISDSAKDFVKKLLVKDPRARLTAAQALSH 319
Cdd:cd07838 228 eewprNSALPRSSFPSytprpfkSFVPEIDEEGLDLLKKMLTFNPHKRISAFEALQH 284
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
52-322 2.66e-24

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


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 102.72  E-value: 2.66e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  52 FGYSKDFHDHYTIgKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIavEDVKREVQILIALSgHENVVQFHNAFE 131
Cdd:cd14200  18 LAYNESDDKYYAM-KVLSKKKLLKQYGFPRRPPPRGSKAAQGEQAKPLAPL--ERVYQEIAILKKLD-HVNIVKLIEVLD 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 132 D--DDYVYIVMELCEGGELLDrILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATD 209
Cdd:cd14200  94 DpaEDNLYMVFDLLRKGPVME-VPSDK--PFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGD---DGHVKIAD 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 210 FGLSD-FIKPGKRFHDIVGSAYYVAPEVL----KRRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVlRNKP-DF 283
Cdd:cd14200 168 FGVSNqFEGNDALLSSTAGTPAFMAPETLsdsgQSFSGKALDVWAMGVTLYCFVYGKCPFIDEFILALHNKI-KNKPvEF 246
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 34098881 284 SRKPwaTISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14200 247 PEEP--EISEELKDLILKMLDKNPETRITVPEIKVHPWV 283
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
66-323 3.04e-24

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 103.13  E-value: 3.04e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSGhENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd05632   8 RVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMALNEKQILEKVNS-QFVVNLAYAYETKDALCLVLTIMNG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKPGKRFHDI 225
Cdd:cd05632  87 GDLKFHIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDD---YGHIRISDLGLAVKIPEGESIRGR 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 226 VGSAYYVAPEVLK-RRSGPESDVWSIGVITYILLCGRRPFWDRTE----DGIFKEVLRNKPDFSRKpwatISDSAKDFVK 300
Cdd:cd05632 164 VGTVGYMAPEVLNnQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEkvkrEEVDRRVLETEEVYSAK----FSEEAKSICK 239
                       250       260
                ....*....|....*....|....*...
gi 34098881 301 KLLVKDPRARL-----TAAQALSHAWVR 323
Cdd:cd05632 240 MLLTKDPKQRLgcqeeGAGEVKRHPFFR 267
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
56-319 3.51e-24

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: 101.80  E-value: 3.51e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  56 KDFHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDkskmvlpIAVEDVKREVQILIALSgHENVVQFHNAFEDDD- 134
Cdd:cd14047   2 ERFRQDFKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVK-------LNNEKAEREVKALAKLD-HPNIVRYNGCWDGFDy 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 135 ---------------YVYIVMELCEGGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSa 199
Cdd:cd14047  74 dpetsssnssrsktkCLFIQMEFCEKGTLESWIEKRNGEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVD- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 200 qlDSPLKATDFGLSDFIK-PGKRFHDiVGSAYYVAPEVL-KRRSGPESDVWSIGVITYILLC------GRRPFWDRTEDG 271
Cdd:cd14047 153 --TGKVKIGDFGLVTSLKnDGKRTKS-KGTLSYMSPEQIsSQDYGKEVDIYALGLILFELLHvcdsafEKSKFWTDLRNG 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 34098881 272 IFkevlrnKPDFSRKPWATisdsaKDFVKKLLVKDPRARLTAAQALSH 319
Cdd:cd14047 230 IL------PDIFDKRYKIE-----KTIIKKMLSKKPEDRPNASEILRT 266
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
59-310 3.75e-24

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 103.52  E-value: 3.75e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881   59 HDHYTIGKLLGHGQFGYTYVAIHRpNGD--RVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYV 136
Cdd:PTZ00426  29 YEDFNFIRTLGTGSFGRVILATYK-NEDfpPVAIKRFEKSKIIKQKQVDHVFSERKILNYIN-HPFCVNLYGSFKDESYL 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  137 YIVMELCEGGELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFI 216
Cdd:PTZ00426 107 YLVLEFVIGGEFFTFL--RRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDK---DGFIKMTDFGFAKVV 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  217 KpgKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRkpwaTISDSA 295
Cdd:PTZ00426 182 D--TRTYTLCGTPEYIAPEILLNVGhGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGIIYFPK----FLDNNC 255
                        250
                 ....*....|....*
gi 34098881  296 KDFVKKLLVKDPRAR 310
Cdd:PTZ00426 256 KHLMKKLLSHDLTKR 270
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
66-311 4.79e-24

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 102.71  E-value: 4.79e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSGHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd05620   1 KVLGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDDVECTMVEKRVLALAWENPFLTHLYCTFQTKEHLFFVMEFLNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRILSKkgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGL-SDFIKPGKRFHD 224
Cdd:cd05620  81 GDLMFHIQDK--GRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDR---DGHIKIADFGMcKENVFGDNRAST 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 225 IVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRkpWatISDSAKDFVKKLL 303
Cdd:cd05620 156 FCGTPDYIAPEILQGLKYTFSvDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPR--W--ITKESKDILEKLF 231

                ....*...
gi 34098881 304 VKDPRARL 311
Cdd:cd05620 232 ERDPTRRL 239
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
60-311 1.33e-23

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: 102.78  E-value: 1.33e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVlpiavedvKR-------EVQILIALSGHENVVQFHNAFED 132
Cdd:cd05622  73 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMI--------KRsdsaffwEERDIMAFANSPWVVQLFYAFQD 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 133 DDYVYIVMELCEGGELLDRIlskKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAqldSPLKATDFGL 212
Cdd:cd05622 145 DRYLYMVMEYMPGGDLVNLM---SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKS---GHLKLADFGT 218
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 213 SdfIKPGK----RFHDIVGSAYYVAPEVLKRRSGP-----ESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDF 283
Cdd:cd05622 219 C--MKMNKegmvRCDTAVGTPDYISPEVLKSQGGDgyygrECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSL 296
                       250       260
                ....*....|....*....|....*...
gi 34098881 284 SRKPWATISDSAKDFVKKLLVkDPRARL 311
Cdd:cd05622 297 TFPDDNDISKEAKNLICAFLT-DREVRL 323
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
68-313 1.46e-23

Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 101.49  E-value: 1.46e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSGHEN--VVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd05586   1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVAHTIGERNILVRTALDESpfIVGLKFSFQTPTDLYLVTDYMSG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRiLSKKGnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDF-IKPGKRFHD 224
Cdd:cd05586  81 GELFWH-LQKEG-RFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDA---NGHIALCDFGLSKAdLTDNKTTNT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 225 IVGSAYYVAPEVLKRRSG--PESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFsrkPWATISDSAKDFVKKL 302
Cdd:cd05586 156 FCGTTEYLAPEVLLDEKGytKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRF---PKDVLSDEGRSFVKGL 232
                       250
                ....*....|.
gi 34098881 303 LVKDPRARLTA 313
Cdd:cd05586 233 LNRNPKHRLGA 243
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
57-323 1.49e-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: 100.95  E-value: 1.49e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  57 DFHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLD---KSKMVLPIAVEDVKREvqilialSGHENVVQFHNAFEDD 133
Cdd:cd06656  16 DPKKKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNlqqQPKKELIINEILVMRE-------NKNPNIVNYLDSYLVG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 134 DYVYIVMELCEGGELLDRILSkkgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKsaqLDSPLKATDFGLS 213
Cdd:cd06656  89 DELWVVMEYLAGGSLTDVVTE---TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLG---MDGSVKLTDFGFC 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 214 DFIKPGK-RFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPwATI 291
Cdd:cd06656 163 AQITPEQsKRSTMVGTPYWMAPEVVTRKAyGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNP-ERL 241
                       250       260       270
                ....*....|....*....|....*....|..
gi 34098881 292 SDSAKDFVKKLLVKDPRARLTAAQALSHAWVR 323
Cdd:cd06656 242 SAVFRDFLNRCLEMDVDRRGSAKELLQHPFLK 273
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
62-264 1.56e-23

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 104.11  E-value: 1.56e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881   62 YTIGKLLGHGQFGYTYVA----IHRPngdrVAVKRL------DkskmvlPIAVEDVKREVQILIALSgHENVVQFHNAFE 131
Cdd:NF033483   9 YEIGERIGRGGMAEVYLAkdtrLDRD----VAVKVLrpdlarD------PEFVARFRREAQSAASLS-HPNIVSVYDVGE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  132 DDDYVYIVMELCEGGELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFG 211
Cdd:NF033483  78 DGGIPYIVMEYVDGRTLKDYI--REHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITK---DGRVKVTDFG 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34098881  212 LSdfikpgkRF---------HDIVGSAYYVAPE------VLKRrsgpeSDVWSIGVITYILLCGRRPF 264
Cdd:NF033483 153 IA-------RAlssttmtqtNSVLGTVHYLSPEqarggtVDAR-----SDIYSLGIVLYEMLTGRPPF 208
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
60-324 1.56e-23

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: 101.54  E-value: 1.56e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSGHENVVQFHNAFEDDDYVYIV 139
Cdd:cd05619   5 EDFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSLAWEHPFLTHLFCTFQTKENLFFV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGELLDRILSkkGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGL-SDFIKP 218
Cdd:cd05619  85 MEYLNGGDLMFHIQS--CHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDK---DGHIKIADFGMcKENMLG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 GKRFHDIVGSAYYVAPEV-LKRRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRkpWatISDSAKD 297
Cdd:cd05619 160 DAKTSTFCGTPDYIAPEIlLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRMDNPFYPR--W--LEKEAKD 235
                       250       260
                ....*....|....*....|....*...
gi 34098881 298 FVKKLLVKDPRARLTAAQAL-SHAWVRE 324
Cdd:cd05619 236 ILVKLFVREPERRLGVRGDIrQHPFFRE 263
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
57-323 1.83e-23

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: 100.57  E-value: 1.83e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  57 DFHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLD---KSKMVLPIAVEDVKREvqilialSGHENVVQFHNAFEDD 133
Cdd:cd06654  17 DPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNlqqQPKKELIINEILVMRE-------NKNPNIVNYLDSYLVG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 134 DYVYIVMELCEGGELLDRILSkkgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKsaqLDSPLKATDFGLS 213
Cdd:cd06654  90 DELWVVMEYLAGGSLTDVVTE---TCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLG---MDGSVKLTDFGFC 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 214 DFIKPGK-RFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPwATI 291
Cdd:cd06654 164 AQITPEQsKRSTMVGTPYWMAPEVVTRKAyGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNP-EKL 242
                       250       260       270
                ....*....|....*....|....*....|..
gi 34098881 292 SDSAKDFVKKLLVKDPRARLTAAQALSHAWVR 323
Cdd:cd06654 243 SAIFRDFLNRCLEMDVEKRGSAKELLQHQFLK 274
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
66-311 2.25e-23

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: 100.93  E-value: 2.25e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILiALSGHEN-VVQFHNAFEDDDYVYIVMELCE 144
Cdd:cd05587   2 MVLGKGSFGKVMLAERKGTDELYAIKILKKDVIIQDDDVECTMVEKRVL-ALSGKPPfLTQLHSCFQTMDRLYFVMEYVN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 145 GGELLDRIlsKKGNRYSEKDAAVVVRQMlkVAGECHLH--GLVHRDMKPENFLFKSaqlDSPLKATDFGL-SDFIKPGKR 221
Cdd:cd05587  81 GGDLMYHI--QQVGKFKEPVAVFYAAEI--AVGLFFLHskGIIYRDLKLDNVMLDA---EGHIKIADFGMcKEGIFGGKT 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 222 FHDIVGSAYYVAPE-VLKRRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRkpwaTISDSAKDFVK 300
Cdd:cd05587 154 TRTFCGTPDYIAPEiIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPK----SLSKEAVSICK 229
                       250
                ....*....|.
gi 34098881 301 KLLVKDPRARL 311
Cdd:cd05587 230 GLLTKHPAKRL 240
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
74-322 2.65e-23

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: 98.80  E-value: 2.65e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  74 GYTYVAIHRPNGDRVAVKrldkskmVLPIavedvkREVQILIA----LSGHENVVQFHNAFEDDDYVYIVMELcEGGELL 149
Cdd:cd14024   7 QELYRAEHYQTEKEYTCK-------VLSL------RSYQECLApydrLGPHEGVCSVLEVVIGQDRAYAFFSR-HYGDMH 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 150 DRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDsplKATDFGLSD---FIKPGKRFHDIV 226
Cdd:cd14024  73 SHVRRRR--RLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRT---KLVLVNLEDscpLNGDDDSLTDKH 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 227 GSAYYVAPEVLKRR---SGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKpdFSRKPWatISDSAKDFVKKLL 303
Cdd:cd14024 148 GCPAYVGPEILSSRrsySGKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIRRGA--FSLPAW--LSPGARCLVSCML 223
                       250
                ....*....|....*....
gi 34098881 304 VKDPRARLTAAQALSHAWV 322
Cdd:cd14024 224 RRSPAERLKASEILLHPWL 242
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
62-333 2.74e-23

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 100.71  E-value: 2.74e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRL--------DKSKMVlpiavedvkREVQILIALSGHENVVQFHNAF--E 131
Cdd:cd07852   9 YEILKKLGKGAYGIVWKAIDKKTGEVVALKKIfdafrnatDAQRTF---------REIMFLQELNDHPNIIKLLNVIraE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 132 DDDYVYIVMElceggelldrilskkgnrYSEKDAAVVVR--------------QMLKVAGECHLHGLVHRDMKPENFLFK 197
Cdd:cd07852  80 NDKDIYLVFE------------------YMETDLHAVIRaniledihkqyimyQLLKALKYLHSGGVIHRDLKPSNILLN 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 198 SaqlDSPLKATDFGLSDFIKPGKRFH------DIVGSAYYVAPEVL--KRRSGPESDVWSIGVITYILLCGR-------- 261
Cdd:cd07852 142 S---DCRVKLADFGLARSLSQLEEDDenpvltDYVATRWYRAPEILlgSTRYTKGVDMWSVGCILGEMLLGKplfpgtst 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 262 ------------RPfwdRTED------GIFKEVLRNKPDFSRKPWATI----SDSAKDFVKKLLVKDPRARLTAAQALSH 319
Cdd:cd07852 219 lnqlekiievigRP---SAEDiesiqsPFAATMLESLPPSRPKSLDELfpkaSPDALDLLKKLLVFNPNKRLTAEEALRH 295
                       330
                ....*....|....
gi 34098881 320 AWVREGGNATDIPV 333
Cdd:cd07852 296 PYVAQFHNPADEPS 309
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
57-323 2.88e-23

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: 99.80  E-value: 2.88e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  57 DFHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVlpiAVEDVKREVQILIALSgHENVVQFHNAFEDDDYV 136
Cdd:cd06655  16 DPKKKYTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQP---KKELIINEILVMKELK-NPNIVNFLDSFLVGDEL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 137 YIVMELCEGGELLDRILSkkgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKsaqLDSPLKATDFGLSDFI 216
Cdd:cd06655  92 FVVMEYLAGGSLTDVVTE---TCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLG---MDGSVKLTDFGFCAQI 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 217 KPGK-RFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPwATISDS 294
Cdd:cd06655 166 TPEQsKRSTMVGTPYWMAPEVVTRKAyGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNP-EKLSPI 244
                       250       260
                ....*....|....*....|....*....
gi 34098881 295 AKDFVKKLLVKDPRARLTAAQALSHAWVR 323
Cdd:cd06655 245 FRDFLNRCLEMDVEKRGSAKELLQHPFLK 273
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
75-321 2.89e-23

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: 98.57  E-value: 2.89e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  75 YTYVAIHRPNGDRVAVKRLDKSKMvlpiavedvKREVQILIALSGHENVVQFHNAFEDDDYVYIVMELCEGGElldRILS 154
Cdd:cd14022   8 HVFRAVHLHSGEELVCKVFDIGCY---------QESLAPCFCLPAHSNINQITEIILGETKAYVFFERSYGDM---HSFV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 155 KKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKS-----AQLDS-----PLKATDFGLSDFikpgkrfHd 224
Cdd:cd14022  76 RTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDeertrVKLESledayILRGHDDSLSDK-------H- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 225 ivGSAYYVAPEVLKRR---SGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLR---NKPDfsrkpwaTISDSAKDF 298
Cdd:cd14022 148 --GCPAYVSPEILNTSgsySGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRgqfNIPE-------TLSPKAKCL 218
                       250       260
                ....*....|....*....|...
gi 34098881 299 VKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd14022 219 IRSILRREPSERLTSQEILDHPW 241
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
66-311 3.34e-23

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: 99.71  E-value: 3.34e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSGhENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd05630   6 RVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNS-RFVVSLAYAYETKDALCLVLTLMNG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKPGKRFHDI 225
Cdd:cd05630  85 GDLKFHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDD---HGHIRISDLGLAVHVPEGQTIKGR 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 226 VGSAYYVAPEVLK-RRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDSAKDFVKKLLV 304
Cdd:cd05630 162 VGTVGYMAPEVVKnERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLVKEVPEEYSEKFSPQARSLCSMLLC 241

                ....*..
gi 34098881 305 KDPRARL 311
Cdd:cd05630 242 KDPAERL 248
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
117-321 3.56e-23

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: 98.27  E-value: 3.56e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 117 LSGHENVVQFHNAFEDDDYVYIVMELcEGGELLDRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLF 196
Cdd:cd13976  41 LPSHPNISGVHEVIAGETKAYVFFER-DHGDLHSYVRSRK--RLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVF 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 197 KSA-----QLDS-----PLKATDFGLSDfikpgKRfhdivGSAYYVAPEVLKRR---SGPESDVWSIGVITYILLCGRRP 263
Cdd:cd13976 118 ADEertklRLESledavILEGEDDSLSD-----KH-----GCPAYVSPEILNSGatySGKAADVWSLGVILYTMLVGRYP 187
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34098881 264 FWDRTEDGIFKEVLR---NKPdfsrkpwATISDSAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd13976 188 FHDSEPASLFAKIRRgqfAIP-------ETLSPRARCLIRSLLRREPSERLTAEDILLHPW 241
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
68-264 4.26e-23

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: 99.87  E-value: 4.26e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEdvKREVQILIALSgHENVVQFHNAFEDDD--YVYIVMELCEG 145
Cdd:cd13988   1 LGQGATANVFRGRHKKTGDLYAVKVFNNLSFMRPLDVQ--MREFEVLKKLN-HKNIVKLFAIEEELTtrHKVLVMELCPC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDrILSKKGNRY--SEKDAAVVVRQMlkVAGECHLH--GLVHRDMKPENFL-FKSAQLDSPLKATDFGLSDFIKPGK 220
Cdd:cd13988  78 GSLYT-VLEEPSNAYglPESEFLIVLRDV--VAGMNHLRenGIVHRDIKPGNIMrVIGEDGQSVYKLTDFGAARELEDDE 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 34098881 221 RFHDIVGSAYYVAPEVLKR---------RSGPESDVWSIGVITYILLCGRRPF 264
Cdd:cd13988 155 QFVSLYGTEEYLHPDMYERavlrkdhqkKYGATVDLWSIGVTFYHAATGSLPF 207
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
66-313 4.33e-23

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: 100.04  E-value: 4.33e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSGHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd05604   2 KVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVNG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAqldSPLKATDFGLSdfiKPGKRFHDI 225
Cdd:cd05604  82 GELFFHL--QRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQ---GHIVLTDFGLC---KEGISNSDT 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 226 V----GSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCGRRPFWDRTE----DGIFKEVLRNKPDFSRKPWATIsdsak 296
Cdd:cd05604 154 TttfcGTPEYLAPEVIRKQPYDNTvDWWCLGSVLYEMLYGLPPFYCRDTaemyENILHKPLVLRPGISLTAWSIL----- 228
                       250
                ....*....|....*..
gi 34098881 297 dfvKKLLVKDPRARLTA 313
Cdd:cd05604 229 ---EELLEKDRQLRLGA 242
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
60-311 4.58e-23

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 100.84  E-value: 4.58e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVlpiavedvKR-------EVQILIALSGHENVVQFHNAFED 132
Cdd:cd05621  52 EDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMI--------KRsdsaffwEERDIMAFANSPWVVQLFCAFQD 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 133 DDYVYIVMELCEGGELLDRILSKKgnrYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAqldSPLKATDFGL 212
Cdd:cd05621 124 DKYLYMVMEYMPGGDLVNLMSNYD---VPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKY---GHLKLADFGT 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 213 SDFIKPGKRFH--DIVGSAYYVAPEVLKRRSGP-----ESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSR 285
Cdd:cd05621 198 CMKMDETGMVHcdTAVGTPDYISPEVLKSQGGDgyygrECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDHKNSLNF 277
                       250       260
                ....*....|....*....|....*.
gi 34098881 286 KPWATISDSAKDFVKKLLVkDPRARL 311
Cdd:cd05621 278 PDDVEISKHAKNLICAFLT-DREVRL 302
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
61-320 4.99e-23

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: 98.89  E-value: 4.99e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRL---DKSkmvlpiAVEDVKREVQILIALSGHENVVQF----HNAFEDD 133
Cdd:cd14037   4 HVTIEKYLAEGGFAHVYLVKTSNGGNRAALKRVyvnDEH------DLNVCKREIEIMKRLSGHKNIVGYidssANRSGNG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 134 DY-VYIVMELCEGGELLDRILSKKGNRYSEK-------DAAVVVRQM--LKVAgechlhgLVHRDMKPENFLfksaqLDS 203
Cdd:cd14037  78 VYeVLLLMEYCKGGGVIDLMNQRLQTGLTESeilkifcDVCEAVAAMhyLKPP-------LIHRDLKVENVL-----ISD 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 204 PL--KATDFGLSDFIKPGKRFHDIVG----------SAYYVAPEVLKRRSGPE----SDVWSIGVITYILLCGRRPFWDR 267
Cdd:cd14037 146 SGnyKLCDFGSATTKILPPQTKQGVTyveedikkytTLQYRAPEMIDLYRGKPitekSDIWALGCLLYKLCFYTTPFEES 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 34098881 268 TEDGIfkevLRNK---PDFSRkpwatISDSAKDFVKKLLVKDPRARLTAAQALSHA 320
Cdd:cd14037 226 GQLAI----LNGNftfPDNSR-----YSKRLHKLIRYMLEEDPEKRPNIYQVSYEA 272
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
108-321 5.81e-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: 97.81  E-value: 5.81e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 108 KREVQILIALSGHENVVQFHNAFEDDDYVYIVMELcEGGELLDRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHR 187
Cdd:cd14023  32 QDKIRPYIQLPSHRNITGIVEVILGDTKAYVFFEK-DFGDMHSYVRSCK--RLREEEAARLFKQIVSAVAHCHQSAIVLG 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 188 DMKPENFLFKSAQ-----LDS-----PLKATDFGLSDFikpgkrfHdivGSAYYVAPEVLKRR---SGPESDVWSIGVIT 254
Cdd:cd14023 109 DLKLRKFVFSDEErtqlrLESledthIMKGEDDALSDK-------H---GCPAYVSPEILNTTgtySGKSADVWSLGVML 178
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 255 YILLCGRRPFWDRTEDGIFKEVLRNK---PDFsrkpwatISDSAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd14023 179 YTLLVGRYPFHDSDPSALFSKIRRGQfciPDH-------VSPKARCLIRSLLRREPSERLTAPEILLHPW 241
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
108-317 6.29e-23

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 101.63  E-value: 6.29e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  108 KREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEGGELLDRILSKKGNR--YSEKDAAVVVRQMLKVAGECHLHGLV 185
Cdd:PTZ00267 113 RSELHCLAACD-HFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQIKQRLKEHlpFQEYEVGLLFYQIVLALDEVHSRKMM 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  186 HRDMKPENFLFKSAQLdspLKATDFGLSdfikpgKRFHDIV---------GSAYYVAPEVLKR-RSGPESDVWSIGVITY 255
Cdd:PTZ00267 192 HRDLKSANIFLMPTGI---IKLGDFGFS------KQYSDSVsldvassfcGTPYYLAPELWERkRYSKKADMWSLGVILY 262
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34098881  256 ILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPwatISDSAKDFVKKLLVKDPRARLTAAQAL 317
Cdd:PTZ00267 263 ELLTLHRPFKGPSQREIMQQVLYGKYDPFPCP---VSSGMKALLDPLLSKNPALRPTTQQLL 321
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
57-321 8.21e-23

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: 99.18  E-value: 8.21e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  57 DFHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVK---RLDKSKmvlpiavEDVKREVQIL--IALSGHEN---VVQFHN 128
Cdd:cd14134   9 LLTNRYKILRLLGEGTFGKVLECWDRKRKRYVAVKiirNVEKYR-------EAAKIEIDVLetLAEKDPNGkshCVQLRD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 129 AFEDDDYVYIVMELCeGGELLDRIlskKGNRY---SEKDAAVVVRQMLK-VAgecHLH--GLVHRDMKPENFLFKSAQLD 202
Cdd:cd14134  82 WFDYRGHMCIVFELL-GPSLYDFL---KKNNYgpfPLEHVQHIAKQLLEaVA---FLHdlKLTHTDLKPENILLVDSDYV 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 203 S-----------PLKATDFGLSDFikpG-----KRFH-DIVGSAYYVAPEV---LKrRSGPeSDVWSIGVITYILLCGRR 262
Cdd:cd14134 155 KvynpkkkrqirVPKSTDIKLIDF---GsatfdDEYHsSIVSTRHYRAPEVilgLG-WSYP-CDVWSIGCILVELYTGEL 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 263 PFwdRTEDG-----------------IFKEVLRNKPDFSR------------------------KPWATISDSAK----D 297
Cdd:cd14134 230 LF--QTHDNlehlammerilgplpkrMIRRAKKGAKYFYFyhgrldwpegsssgrsikrvckplKRLMLLVDPEHrllfD 307
                       330       340
                ....*....|....*....|....
gi 34098881 298 FVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd14134 308 LIRKMLEYDPSKRITAKEALKHPF 331
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
66-311 9.31e-23

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: 98.92  E-value: 9.31e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILiALSGHEN-VVQFHNAFEDDDYVYIVMELCE 144
Cdd:cd05616   6 MVLGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVL-ALSGKPPfLTQLHSCFQTMDRLYFVMEYVN 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 145 GGELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGL-SDFIKPGKRFH 223
Cdd:cd05616  85 GGDLMYHI--QQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDS---EGHIKIADFGMcKENIWDGVTTK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 224 DIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRkpwaTISDSAKDFVKKL 302
Cdd:cd05616 160 TFCGTPDYIAPEIIAYQPyGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPK----SMSKEAVAICKGL 235

                ....*....
gi 34098881 303 LVKDPRARL 311
Cdd:cd05616 236 MTKHPGKRL 244
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
60-311 9.67e-23

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: 98.96  E-value: 9.67e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIalSGHEN-VVQFHNAFEDDDYVYI 138
Cdd:cd05597   1 DDFEILKVIGRGAFGEVAVVKLKSTEKVYAMKILNKWEMLKRAETACFREERDVLV--NGDRRwITKLHYAFQDENYLYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 139 VMELCEGGELLDrILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFksaQLDSPLKATDFG----LSD 214
Cdd:cd05597  79 VMDYYCGGDLLT-LLSKFEDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLL---DRNGHIRLADFGsclkLRE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 215 fikPGKRFHDI-VGSAYYVAPEVL------KRRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKP 287
Cdd:cd05597 155 ---DGTVQSSVaVGTPDYISPEILqamedgKGRYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKEHFSFPD 231
                       250       260
                ....*....|....*....|....*
gi 34098881 288 WAT-ISDSAKDFVKKLLVkDPRARL 311
Cdd:cd05597 232 DEDdVSEEAKDLIRRLIC-SRERRL 255
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
52-333 1.02e-22

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: 99.18  E-value: 1.02e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  52 FGYSKDFHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSkMVLPIAVEDVKREVQILIALSgHENVVQ----FH 127
Cdd:cd07856   2 FGTVFEITTRYSDLQPVGMGAFGLVCSARDQLTGQNVAVKKIMKP-FSTPVLAKRTYRELKLLKHLR-HENIISlsdiFI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 128 NAFEDddyVYIVMELCegGELLDRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKA 207
Cdd:cd07856  80 SPLED---IYFVTELL--GTDLHRLLTSR--PLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNE---NCDLKI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 208 TDFGLSDFIKPgkRFHDIVGSAYYVAPEVLK--RRSGPESDVWSIGVITYILLCGRRPFWDR---TEDGIFKEVLRNKPD 282
Cdd:cd07856 150 CDFGLARIQDP--QMTGYVSTRYYRAPEIMLtwQKYDVEVDIWSAGCIFAEMLEGKPLFPGKdhvNQFSIITELLGTPPD 227
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34098881 283 -------------------------FSRKpWATISDSAKDFVKKLLVKDPRARLTAAQALSHAWVREGGNATDIPV 333
Cdd:cd07856 228 dvinticsentlrfvqslpkrervpFSEK-FKNADPDAIDLLEKMLVFDPKKRISAAEALAHPYLAPYHDPTDEPV 302
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
66-313 1.39e-22

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: 98.50  E-value: 1.39e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSGHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd05603   1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNHIMAERNVLLKNLKHPFLVGLHYSFQTSEKLYFVLDYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGL-SDFIKPGKRFHD 224
Cdd:cd05603  81 GELFFHL--QRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDC---QGHVVLTDFGLcKEGMEPEETTST 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 225 IVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCGRRPFWDRTEDGIFKEVLrNKPdFSRKPWATIsdSAKDFVKKLL 303
Cdd:cd05603 156 FCGTPEYLAPEVLRKEPYDRTvDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNIL-HKP-LHLPGGKTV--AACDLLQGLL 231
                       250
                ....*....|
gi 34098881 304 VKDPRARLTA 313
Cdd:cd05603 232 HKDQRRRLGA 241
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
62-319 1.54e-22

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


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 98.80  E-value: 1.54e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILiALSGHENVVQFHNAFEDDDYVYIVME 141
Cdd:cd05610   6 FVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMVHQVQAERDAL-ALSKSPFIVHLYYSLQSANNVYLVME 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELlDRILSKKGnrYSEKDAAV-VVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLS------- 213
Cdd:cd05610  85 YLIGGDV-KSLLHIYG--YFDEEMAVkYISEVALALDYLHRHGIIHRDLKPDNMLISN---EGHIKLTDFGLSkvtlnre 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 214 ----DFI------KPGKRF-------------------------------------HDIVGSAYYVAPEVLKRRS-GPES 245
Cdd:cd05610 159 lnmmDILttpsmaKPKNDYsrtpgqvlslisslgfntptpyrtpksvrrgaarvegERILGTPDYLAPELLLGKPhGPAV 238
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34098881 246 DVWSIGVITYILLCGRRPFWDRTEDGIFKEVLrnKPDFsrkPWA----TISDSAKDFVKKLLVKDPRARLTAAQALSH 319
Cdd:cd05610 239 DWWALGVCLFEFLTGIPPFNDETPQQVFQNIL--NRDI---PWPegeeELSVNAQNAIEILLTMDPTKRAGLKELKQH 311
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
62-323 1.54e-22

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: 96.84  E-value: 1.54e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYvAIHR-PNGDRVAVKRLDKSKM--------VLPIAVEDVKreVQILIALSGHENVVQFHNAFED 132
Cdd:cd14101   2 YTMGNLLGKGGFGTVY-AGHRiSDGLQVAIKQISRNRVqqwsklpgVNPVPNEVAL--LQSVGGGPGHRGVIRLLDWFEI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 133 DDYVYIVMELCEGGELLDRILSKKGNrYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDspLKATDFGL 212
Cdd:cd14101  79 PEGFLLVLERPQHCQDLFDYITERGA-LDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLRTGD--IKLIDFGS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 213 SDFIKpGKRFHDIVGSAYYVAPEVLKRRS--GPESDVWSIGVITYILLCGRRPFwDRTEDgifkeVLRNKPDFsRKPwat 290
Cdd:cd14101 156 GATLK-DSMYTDFDGTRVYSPPEWILYHQyhALPATVWSLGILLYDMVCGDIPF-ERDTD-----ILKAKPSF-NKR--- 224
                       250       260       270
                ....*....|....*....|....*....|...
gi 34098881 291 ISDSAKDFVKKLLVKDPRARLTAAQALSHAWVR 323
Cdd:cd14101 225 VSNDCRSLIRSCLAYNPSDRPSLEQILLHPWMM 257
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
61-311 1.71e-22

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: 97.37  E-value: 1.71e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYtigKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSGhENVVQFHNAFEDDDYVYIVM 140
Cdd:cd05631   4 HY---RVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKRILEKVNS-RFVVSLAYAYETKDALCLVL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCEGGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAqldSPLKATDFGLSDFIKPGK 220
Cdd:cd05631  80 TIMNGGDLKFHIYNMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDR---GHIRISDLGLAVQIPEGE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 221 RFHDIVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCGRRPFWDRTE----DGIFKEVLRNKPDFSRKpwatISDSA 295
Cdd:cd05631 157 TVRGRVGTVGYMAPEVINNEKYTFSpDWWGLGCLIYEMIQGQSPFRKRKErvkrEEVDRRVKEDQEEYSEK----FSEDA 232
                       250
                ....*....|....*.
gi 34098881 296 KDFVKKLLVKDPRARL 311
Cdd:cd05631 233 KSICRMLLTKNPKERL 248
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
68-324 2.79e-22

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: 97.44  E-value: 2.79e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVK--RLDKSKMVLPIAVedvKREVQILIALSgHENVVQFHNAFEDD--DYVYIVMELC 143
Cdd:cd07845  15 IGEGTYGIVYRARDTTSGEIVALKkvRMDNERDGIPISS---LREITLLLNLR-HPNIVELKEVVVGKhlDSIFLVMEYC 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 144 EggELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLdspLKATDFGLS-DFIKPGKRF 222
Cdd:cd07845  91 E--QDLASLLDNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGC---LKIADFGLArTYGLPAKPM 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 223 HDIVGSAYYVAPEVL--KRRSGPESDVWSIGVITYILLCGRRPFWDRTE---------------DGIF----------KE 275
Cdd:cd07845 166 TPKVVTLWYRAPELLlgCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEieqldliiqllgtpnESIWpgfsdlplvgKF 245
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 34098881 276 VLRNKP-DFSRKPWATISDSAKDFVKKLLVKDPRARLTAAQALSHAWVRE 324
Cdd:cd07845 246 TLPKQPyNNLKHKFPWLSEAGLRLLNFLLMYDPKKRATAEEALESSYFKE 295
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
66-323 3.54e-22

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: 96.66  E-value: 3.54e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSK--------MVLpiavedvkREVQILIALSGhENVVQFHNAFEDDDYVY 137
Cdd:cd05605   6 RVLGKGGFGEVCACQVRATGKMYACKKLEKKRikkrkgeaMAL--------NEKQILEKVNS-RFVVSLAYAYETKDALC 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 138 IVMELCEGGELLDRILSKKGNRYSEKDAAVVVRQMLkvAGECHLH--GLVHRDMKPENFLfksaqLDSP--LKATDFGLS 213
Cdd:cd05605  77 LVLTIMNGGDLKFHIYNMGNPGFEEERAVFYAAEIT--CGLEHLHseRIVYRDLKPENIL-----LDDHghVRISDLGLA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 214 DFIKPGKRFHDIVGSAYYVAPEVLK-RRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLR----NKPDFSRKpw 288
Cdd:cd05605 150 VEIPEGETIRGRVGTVGYMAPEVVKnERYTFSPDWWGLGCLIYEMIEGQAPFRARKEKVKREEVDRrvkeDQEEYSEK-- 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 34098881 289 atISDSAKDFVKKLLVKDPRARL-----TAAQALSHAWVR 323
Cdd:cd05605 228 --FSEEAKSICSQLLQKDPKTRLgcrgeGAEDVKSHPFFK 265
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
40-322 3.67e-22

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: 97.04  E-value: 3.67e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  40 RTGSIPCGKRTDFGYSKDFHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSg 119
Cdd:cd06635   5 RAGSLKDPDIAELFFKEDPEKLFSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQRIK- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 120 HENVVQFHNAFEDDDYVYIVMELCEGGEllDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSA 199
Cdd:cd06635  84 HPNSIEYKGCYLREHTAWLVMEYCLGSA--SDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 200 qldSPLKATDFGLSDFIKPGKRFhdiVGSAYYVAPEVL----KRRSGPESDVWSIGvITYILLCGRRP--FWDRTEDGIF 273
Cdd:cd06635 162 ---GQVKLADFGSASIASPANSF---VGTPYWMAPEVIlamdEGQYDGKVDVWSLG-ITCIELAERKPplFNMNAMSALY 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 34098881 274 KEVLRNKPDFSRKPWatiSDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd06635 235 HIAQNESPTLQSNEW---SDYFRNFVDSCLQKIPQDRPTSEELLKHMFV 280
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
62-310 6.52e-22

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: 95.26  E-value: 6.52e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTY----------------VAIHRPNGDRVAVKRlDKSkmvlpiaVEDVKREVQILIALSGHENVVQ 125
Cdd:cd08528   2 YAVLELLGSGAFGCVYkvrkksngqtllalkeINMTNPAFGRTEQER-DKS-------VGDIISEVNIIKEQLRHPNIVR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 126 FHNAFEDDDYVYIVMELCEGGELLDRI--LSKKGNRYSEKDAAVVVRQMlkVAGECHLH---GLVHRDMKPENFLFKSaq 200
Cdd:cd08528  74 YYKTFLENDRLYIVMELIEGAPLGEHFssLKEKNEHFTEDRIWNIFVQM--VLALRYLHkekQIVHRDLKPNNIMLGE-- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 201 lDSPLKATDFGLSDFIKP-GKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLR 278
Cdd:cd08528 150 -DDKVTITDFGLAKQKGPeSSKMTSVVGTILYSCPEIVQNEPyGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVE 228
                       250       260       270
                ....*....|....*....|....*....|..
gi 34098881 279 NKpdFSRKPWATISDSAKDFVKKLLVKDPRAR 310
Cdd:cd08528 229 AE--YEPLPEGMYSDDITFVIRSCLTPDPEAR 258
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
68-322 6.56e-22

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: 96.25  E-value: 6.56e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEGGE 147
Cdd:cd06634  23 IGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQKLR-HPNTIEYRGCYLREHTAWLVMEYCLGSA 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 148 llDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLdspLKATDFGLSDFIKPGKRFhdiVG 227
Cdd:cd06634 102 --SDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGL---VKLGDFGSASIMAPANSF---VG 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 228 SAYYVAPEVL----KRRSGPESDVWSIGvITYILLCGRRP--FWDRTEDGIFKEVLRNKPDFSRKPWatiSDSAKDFVKK 301
Cdd:cd06634 174 TPYWMAPEVIlamdEGQYDGKVDVWSLG-ITCIELAERKPplFNMNAMSALYHIAQNESPALQSGHW---SEYFRNFVDS 249
                       250       260
                ....*....|....*....|.
gi 34098881 302 LLVKDPRARLTAAQALSHAWV 322
Cdd:cd06634 250 CLQKIPQDRPTSDVLLKHRFL 270
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
59-322 6.79e-22

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: 96.07  E-value: 6.79e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  59 HDH----YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRL-DKSKMVLPIAVEdvkreVQILIAL-----SGHENVVQFHN 128
Cdd:cd14210   8 GDHiayrYEVLSVLGKGSFGQVVKCLDHKTGQLVAIKIIrNKKRFHQQALVE-----VKILKHLndndpDDKHNIVRYKD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 129 AFEDDDYVYIVMELceggelldriLSK------KGNRYSEKDAAVV---VRQMLKVAGECHLHGLVHRDMKPENFLFKSa 199
Cdd:cd14210  83 SFIFRGHLCIVFEL----------LSInlyellKSNNFQGLSLSLIrkfAKQILQALQFLHKLNIIHCDLKPENILLKQ- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 200 QLDSPLKATDFGLSDFIkpGKRFHDIVGSAYYVAPEV-LKRRSGPESDVWSIGVI------------------------- 253
Cdd:cd14210 152 PSKSSIKVIDFGSSCFE--GEKVYTYIQSRFYRAPEViLGLPYDTAIDMWSLGCIlaelytgyplfpgeneeeqlacime 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 254 -------TYILLCGRRP-FWDrtEDGIFKEVLRNK----PDFSRKpWATISDSAK----DFVKKLLVKDPRARLTAAQAL 317
Cdd:cd14210 230 vlgvppkSLIDKASRRKkFFD--SNGKPRPTTNSKgkkrRPGSKS-LAQVLKCDDpsflDFLKKCLRWDPSERMTPEEAL 306

                ....*
gi 34098881 318 SHAWV 322
Cdd:cd14210 307 QHPWI 311
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
68-313 6.92e-22

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: 96.60  E-value: 6.92e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALS--GHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd05589   7 LGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARDEVESLMCEKRIFETVNsaRHPFLVNLFACFQTPEHVCFVMEYAAG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRILSkkgNRYSEKD----AAVVVR--QMLkvagecHLHGLVHRDMKPENFLfksaqLDSP--LKATDFGL-SDFI 216
Cdd:cd05589  87 GDLMMHIHE---DVFSEPRavfyAACVVLglQFL------HEHKIVYRDLKLDNLL-----LDTEgyVKIADFGLcKEGM 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 217 KPGKRFHDIVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRkpwaTISDSA 295
Cdd:cd05589 153 GFGDRTSTFCGTPEFLAPEVLTDTSYTRAvDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPR----FLSTEA 228
                       250
                ....*....|....*...
gi 34098881 296 KDFVKKLLVKDPRARLTA 313
Cdd:cd05589 229 ISIMRRLLRKNPERRLGA 246
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
66-319 8.88e-22

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: 95.18  E-value: 8.88e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHR-PNGDRVAVKRLdKSKMVLPIAVEDVKREVQILIALS--GHENVVQFHNAFEDDDYVYIVMEL 142
Cdd:cd14052   6 ELIGSGEFSQVYKVSERvPTGKVYAVKKL-KPNYAGAKDRLRRLEEVSILRELTldGHDNIVQLIDSWEYHGHLYIQTEL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 143 CEGGElLDRILSKKGnRYSEKDAAVVVRQMLKVA---GECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIkPG 219
Cdd:cd14052  85 CENGS-LDVFLSELG-LLGRLDEFRVWKILVELSlglRFIHDHHFVHLDLKPANVLITF---EGTLKIGDFGMATVW-PL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 220 KRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVI-----TYILLCGRRPFWDRTEDGIFKEVLRNK--------PDFSR 285
Cdd:cd14052 159 IRGIEREGDREYIAPEILSEHMyDKPADIFSLGLIlleaaANVVLPDNGDAWQKLRSGDLSDAPRLSstdlhsasSPSSN 238
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 34098881 286 KPWATI-----SDSAKDFVKKLLVKDPRARLTAAQALSH 319
Cdd:cd14052 239 PPPDPPnmpilSGSLDRVVRWMLSPEPDRRPTADDVLAT 277
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
67-315 1.42e-21

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: 95.83  E-value: 1.42e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  67 LLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSGHENVVQFHNAFEDDDYVYIVMELCEGG 146
Cdd:cd05615  17 VLGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVECTMVEKRVLALQDKPPFLTQLHSCFQTVDRLYFVMEYVNGG 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 147 ELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGL-SDFIKPGKRFHDI 225
Cdd:cd05615  97 DLMYHI--QQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDS---EGHIKIADFGMcKEHMVEGVTTRTF 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 226 VGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRkpwaTISDSAKDFVKKLLV 304
Cdd:cd05615 172 CGTPDYIAPEIIAYQPyGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPK----SLSKEAVSICKGLMT 247
                       250
                ....*....|.
gi 34098881 305 KDPRARLTAAQ 315
Cdd:cd05615 248 KHPAKRLGCGP 258
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
60-319 1.45e-21

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: 94.81  E-value: 1.45e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLlGHGQFGYTYVAIHRPNGDRVAvkrldksKMVLPIaveDVKREV--QILIALS-----GHENVVQFHNAF-E 131
Cdd:cd06620   6 DLETLKDL-GAGNGGSVSKVLHIPTGTIMA-------KKVIHI---DAKSSVrkQILRELQilhecHSPYIVSFYGAFlN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 132 DDDYVYIVMELCEGGELlDRILSKKGnRYSEKDAAVVVRQMLKvaGECHL---HGLVHRDMKPENFLFKSAqldSPLKAT 208
Cdd:cd06620  75 ENNNIIICMEYMDCGSL-DKILKKKG-PFPEEVLGKIAVAVLE--GLTYLynvHRIIHRDIKPSNILVNSK---GQIKLC 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 209 DFGLSdfikpGKRFHDI----VGSAYYVAPEVLK-RRSGPESDVWSIGVITYILLCGRRPFWDRTED--------GIFKE 275
Cdd:cd06620 148 DFGVS-----GELINSIadtfVGTSTYMSPERIQgGKYSVKSDVWSLGLSIIELALGEFPFAGSNDDddgyngpmGILDL 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 34098881 276 VLR--NKPDfSRKPWATI-SDSAKDFVKKLLVKDPRARLTAAQALSH 319
Cdd:cd06620 223 LQRivNEPP-PRLPKDRIfPKDLRDFVDRCLLKDPRERPSPQLLLDH 268
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
68-319 1.77e-21

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: 94.49  E-value: 1.77e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVK--RLD-KSKMVLPIAVedvkREVQILIALSgHENVVQFHNAFEDDDYVYIVMELce 144
Cdd:cd07860   8 IGEGTYGVVYKARNKLTGEVVALKkiRLDtETEGVPSTAI----REISLLKELN-HPNIVKLLDVIHTENKLYLVFEF-- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 145 ggelLDRILSK--KGNRYSEKDAAVV---VRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSD-FIKP 218
Cdd:cd07860  81 ----LHQDLKKfmDASALTGIPLPLIksyLFQLLQGLAFCHSHRVLHRDLKPQNLLINT---EGAIKLADFGLARaFGVP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 GKRF-HDIVgSAYYVAPEVL---KRRSGPeSDVWSIGVItYILLCGRRPFW--DRTEDGIFKeVLRN------------- 279
Cdd:cd07860 154 VRTYtHEVV-TLWYRAPEILlgcKYYSTA-VDIWSLGCI-FAEMVTRRALFpgDSEIDQLFR-IFRTlgtpdevvwpgvt 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 34098881 280 -----KPDF---SRKPWATI----SDSAKDFVKKLLVKDPRARLTAAQALSH 319
Cdd:cd07860 230 smpdyKPSFpkwARQDFSKVvpplDEDGRDLLSQMLHYDPNKRISAKAALAH 281
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
64-319 2.25e-21

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: 94.26  E-value: 2.25e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  64 IGKLlGHGQFGYTYVAIHRPNGDRVAVKRLdKSKMVlpiAVEDVK--REVQILIALSGHENVVQFHNAFEDDDY--VYIV 139
Cdd:cd07831   4 LGKI-GEGTFSEVLKAQSRKTGKYYAIKCM-KKHFK---SLEQVNnlREIQALRRLSPHPNILRLIEVLFDRKTgrLALV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGgELLDRIlskKGNRY--SEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKsaqlDSPLKATDFGLSDFIK 217
Cdd:cd07831  79 FELMDM-NLYELI---KGRKRplPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIK----DDILKLADFGSCRGIY 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 218 PGKRFHDIVGSAYYVAPEVL--KRRSGPESDVWSIGVITYILLCGRRPFWDRTE-DGIFK--EVL---RNKPDFSRKPWA 289
Cdd:cd07831 151 SKPPYTEYISTRWYRAPECLltDGYYGPKMDIWAVGCVFFEILSLFPLFPGTNElDQIAKihDVLgtpDAEVLKKFRKSR 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 34098881 290 TI-------------------SDSAKDFVKKLLVKDPRARLTAAQALSH 319
Cdd:cd07831 231 HMnynfpskkgtglrkllpnaSAEGLDLLKKLLAYDPDERITAKQALRH 279
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
66-320 2.28e-21

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: 93.97  E-value: 2.28e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRL---DKSKmvlpiAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMEL 142
Cdd:cd14046  12 QVLGKGAFGQVVKVRNKLDGRYYAIKKIklrSESK-----NNSRILREVMLLSRLN-HQHVVRYYQAWIERANLYIQMEY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 143 CEGGELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIK----- 217
Cdd:cd14046  86 CEKSTLRDLI--DSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDS---NGNVKIGDFGLATSNKlnvel 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 218 --------------PGKRFHDIVGSAYYVAPEVLKRRSG---PESDVWSIGVItYILLCgrRPFWDRTEDGIFKEVLRNK 280
Cdd:cd14046 161 atqdinkstsaalgSSGDLTGNVGTALYVAPEVQSGTKStynEKVDMYSLGII-FFEMC--YPFSTGMERVQILTALRSV 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 34098881 281 -----PDFSRKPWATisdsAKDFVKKLLVKDPRARLTAAQALSHA 320
Cdd:cd14046 238 siefpPDFDDNKHSK----QAKLIRWLLNHDPAKRPSAQELLKSE 278
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
60-322 3.20e-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: 94.10  E-value: 3.20e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVK--RLDKSKMVLPI-AVedvkREVQILIALSgHENVVQFHNAFEDD--- 133
Cdd:cd07864   7 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKkvRLDNEKEGFPItAI----REIKILRQLN-HRSVVNLKEIVTDKqda 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 134 -DY------VYIVMELCEGGelLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAqldSPLK 206
Cdd:cd07864  82 lDFkkdkgaFYLVFEYMDHD--LMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNK---GQIK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 207 ATDFGLSDFIKPGKR--FHDIVGSAYYVAPEVL--KRRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLR---- 278
Cdd:cd07864 157 LADFGLARLYNSEESrpYTNKVITLWYRPPELLlgEERYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRlcgs 236
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34098881 279 ----NKPDFSRKP-WAT-----------------ISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd07864 237 pcpaVWPDVIKLPyFNTmkpkkqyrrrlreefsfIPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
61-322 3.84e-21

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: 93.27  E-value: 3.84e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRpNGDRVAVKR--LDKSKMVlpIA---VEDVKREVQILIALSgHENVVQFHNAFEDDDY 135
Cdd:cd06631   2 QWKKGNVLGKGAYGTVYCGLTS-TGQLIAVKQveLDTSDKE--KAekeYEKLQEEVDLLKTLK-HVNIVGYLGTCLEDNV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 136 VYIVMELCEGGELlDRILskkgNRYSEKDAAVVVR---QMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFG- 211
Cdd:cd06631  78 VSIFMEFVPGGSI-ASIL----ARFGALEEPVFCRytkQILEGVAYLHNNNVIHRDIKGNNIMLMP---NGVIKLIDFGc 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 212 ---LSDFIKPG------KRFHdivGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTE-DGIFKEVLRNK 280
Cdd:cd06631 150 akrLCINLSSGsqsqllKSMR---GTPYWMAPEVINETGhGRKSDIWSIGCTVFEMATGKPPWADMNPmAAIFAIGSGRK 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 34098881 281 PdFSRKPwATISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd06631 227 P-VPRLP-DKFSPEARDFVHACLTRDQDERPSAEQLLKHPFI 266
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
68-264 4.91e-21

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: 93.28  E-value: 4.91e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKR-------LDKSKmvlpiavEDVKREVQILIALSgHENVVQFH------NAFEDDD 134
Cdd:cd13989   1 LGSGGFGYVTLWKHQDTGEYVAIKKcrqelspSDKNR-------ERWCLEVQIMKKLN-HPNVVSARdvppelEKLSPND 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 135 YVYIVMELCEGGELlDRILSKKGNRYSEKDAAVvvRQMLKVAGEC--HLHGL--VHRDMKPENFLFKSAQLDSPLKATDF 210
Cdd:cd13989  73 LPLLAMEYCSGGDL-RKVLNQPENCCGLKESEV--RTLLSDISSAisYLHENriIHRDLKPENIVLQQGGGRVIYKLIDL 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 34098881 211 GLSDFIKPGKRFHDIVGSAYYVAPEVLK-RRSGPESDVWSIGVITYILLCGRRPF 264
Cdd:cd13989 150 GYAKELDQGSLCTSFVGTLQYLAPELFEsKKYTCTVDYWSFGTLAFECITGYRPF 204
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
67-319 6.89e-21

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: 92.87  E-value: 6.89e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  67 LLGHGQFGYTYVAIHRPNGDRVAVKRL---DKSKMVLPIAVedvkREVQILIALSgHENVVQFHNAFEDDDYVYIVMELC 143
Cdd:cd07846   8 LVGEGSYGMVMKCRHKETGQIVAIKKFlesEDDKMVKKIAM----REIKMLKQLR-HENLVNLIEVFRRKKRWYLVFEFV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 144 EGGELLDriLSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLdspLKATDFGLSDFIK-PGKRF 222
Cdd:cd07846  83 DHTVLDD--LEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGV---VKLCDFGFARTLAaPGEVY 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 223 HDIVGSAYYVAPEVL--KRRSGPESDVWSIGVITYILLCGRRPF-WDRTEDGIFKEVL-------RNKPDFSRKP----- 287
Cdd:cd07846 158 TDYVATRWYRAPELLvgDTKYGKAVDVWAVGCLVTEMLTGEPLFpGDSDIDQLYHIIKclgnlipRHQELFQKNPlfagv 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 34098881 288 --------------WATISDSAKDFVKKLLVKDPRARLTAAQALSH 319
Cdd:cd07846 238 rlpevkeveplerrYPKLSGVVIDLAKKCLHIDPDKRPSCSELLHH 283
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
65-323 7.35e-21

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: 92.45  E-value: 7.35e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  65 GKLLGHGQFGYTYVAIHRPNGDRVAVKRL--DKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFED--DDYVYIVM 140
Cdd:cd06651  12 GKLLGQGAFGRVYLCYDVDTGRELAAKQVqfDPESPETSKEVSALECEIQLLKNLQ-HERIVQYYGCLRDraEKTLTIFM 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCEGGELLDRIlsKKGNRYSEKDAAVVVRQMLKvaGECHLHG--LVHRDMKPENFLFKSAqldSPLKATDFGLSDFIK- 217
Cdd:cd06651  91 EYMPGGSVKDQL--KAYGALTESVTRKYTRQILE--GMSYLHSnmIVHRDIKGANILRDSA---GNVKLGDFGASKRLQt 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 218 ---PGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGViTYILLCGRRPFWDRTE--DGIFKevLRNKPDFSRKPwATI 291
Cdd:cd06651 164 icmSGTGIRSVTGTPYWMSPEVISGEGyGRKADVWSLGC-TVVEMLTEKPPWAEYEamAAIFK--IATQPTNPQLP-SHI 239
                       250       260       270
                ....*....|....*....|....*....|..
gi 34098881 292 SDSAKDFVKKLLVkDPRARLTAAQALSHAWVR 323
Cdd:cd06651 240 SEHARDFLGCIFV-EARHRPSAEELLRHPFAQ 270
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
68-264 7.74e-21

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: 91.73  E-value: 7.74e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRpnGDRVAVKRLDKSKmvlpiAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEGGE 147
Cdd:cd14058   1 VGRGSFGVVCKARWR--NQIVAVKIIESES-----EKKAFEVEVRQLSRVD-HPNIIKLYGACSNQKPVCLVMEYAEGGS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 148 LLDRILSKKGN-RYSekdAAVVVRQMLKVA-GECHLHG-----LVHRDMKPENFLFKSAQLDspLKATDFGLSDFIKPGK 220
Cdd:cd14058  73 LYNVLHGKEPKpIYT---AAHAMSWALQCAkGVAYLHSmkpkaLIHRDLKPPNLLLTNGGTV--LKICDFGTACDISTHM 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 34098881 221 RfhDIVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCGRRPF 264
Cdd:cd14058 148 T--NNKGSAAWMAPEVFEGSKYSEKcDVFSWGIILWEVITRRKPF 190
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
60-321 7.89e-21

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: 7.89e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRL--DKSKMVLPIAVEdvkREVQILIALSgHENVVQFHN-AFEDDD-- 134
Cdd:cd07866   8 RDYEILGKLGEGTFGEVYKARQIKTGRVVALKKIlmHNEKDGFPITAL---REIKILKKLK-HPNVVPLIDmAVERPDks 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 135 -----YVYIVMELCEGGelLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLfksaqLDSP--LKA 207
Cdd:cd07866  84 krkrgSVYMVTPYMDHD--LSGLLENPSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANIL-----IDNQgiLKI 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 208 TDFGLSDFI-----KPGK-------RFHDIVGSAYYVAPEVL--KRRSGPESDVWSIGVITYILLCGRRPFWDRTE---- 269
Cdd:cd07866 157 ADFGLARPYdgpppNPKGgggggtrKYTNLVVTRWYRPPELLlgERRYTTAVDIWGIGCVFAEMFTRRPILQGKSDidql 236
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34098881 270 DGIFK-------------EVLRNKPD---FSRKP------WATISDSAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd07866 237 HLIFKlcgtpteetwpgwRSLPGCEGvhsFTNYPrtleerFGKLGPEGLDLLSKLLSLDPYKRLTASDALEHPY 310
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
62-320 8.93e-21

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: 91.72  E-value: 8.93e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAihrpngdrvavKRLDKSKMVL--PIAVEDVKR--------EVQILIALSgHENVVQFHNAFE 131
Cdd:cd08220   2 YEKIRVVGRGAYGTVYLC-----------RRKDDNKLVIikQIPVEQMTKeerqaalnEVKVLSMLH-HPNIIEYYESFL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 132 DDDYVYIVMELCEGGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQldSPLKATDFG 211
Cdd:cd08220  70 EDKALMIVMEYAPGGTLFEYIQQRKGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKR--TVVKIGDFG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 212 LSDFIKPGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKpdfsrkpWAT 290
Cdd:cd08220 148 ISKILSSKSKAYTVVGTPCYISPELCEGKPyNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGT-------FAP 220
                       250       260       270
                ....*....|....*....|....*....|....
gi 34098881 291 ISDS----AKDFVKKLLVKDPRARLTAAQALSHA 320
Cdd:cd08220 221 ISDRyseeLRHLILSMLHLDPNKRPTLSEIMAQP 254
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
60-344 1.16e-20

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: 93.58  E-value: 1.16e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSGHENVVQFHnAFEDDDYVYIV 139
Cdd:cd05627   2 DDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHIRAERDILVEADGAWVVKMFY-SFQDKRNLYLI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGELLDRILSKkgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAqldSPLKATDFGLSDFIKPG 219
Cdd:cd05627  81 MEFLPGGDMMTLLMKK--DTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAK---GHVKLSDFGLCTGLKKA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 220 KR----------------FHDI--------------------VGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRR 262
Cdd:cd05627 156 HRtefyrnlthnppsdfsFQNMnskrkaetwkknrrqlaystVGTPDYIAPEVFMQTGyNKLCDWWSLGVIMYEMLIGYP 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 263 PFWDRTEDGIFKEVLRNKPDFSRKPWATISDSAKDFVKKLLVkDPRARLTAA---QALSHAW--------VREGGNAtdI 331
Cdd:cd05627 236 PFCSETPQETYRKVMNWKETLVFPPEVPISEKAKDLILRFCT-DAENRIGSNgveEIKSHPFfegvdwehIRERPAA--I 312
                       330
                ....*....|...
gi 34098881 332 PVDISVLNNLRQF 344
Cdd:cd05627 313 PIEIKSIDDTSNF 325
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
68-322 1.16e-20

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: 92.04  E-value: 1.16e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMvlPIAVEDVKREVQILiALSGHENVVQFHNAFEDDDYVYIVMELCEGGE 147
Cdd:cd06642  12 IGKGSFGEVYKGIDNRTKEVVAIKIIDLEEA--EDEIEDIQQEITVL-SQCDSPYITRYYGSYLKGTKLWIIMEYLGGGS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 148 LLDRIlskKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFkSAQLDspLKATDFGLSDFIKPGK-RFHDIV 226
Cdd:cd06642  89 ALDLL---KPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLL-SEQGD--VKLADFGVAGQLTDTQiKRNTFV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 227 GSAYYVAPEVLKRRSGP-ESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWatiSDSAKDFVKKLLVK 305
Cdd:cd06642 163 GTPFWMAPEVIKQSAYDfKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKNSPPTLEGQH---SKPFKEFVEACLNK 239
                       250
                ....*....|....*..
gi 34098881 306 DPRARLTAAQALSHAWV 322
Cdd:cd06642 240 DPRFRPTAKELLKHKFI 256
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
66-331 1.51e-20

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: 93.54  E-value: 1.51e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILiALSGHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd05626   7 KTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQVAHVKAERDIL-AEADNEWVVKLYYSFQDKDNLYFVMDYIPG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRILskKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFksaQLDSPLKATDFGL------------- 212
Cdd:cd05626  86 GDMMSLLI--RMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILI---DLDGHIKLTDFGLctgfrwthnskyy 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 213 -------SDFIKP------------GKRF----------------HDIVGSAYYVAPEVLKRRSGPE-SDVWSIGVITYI 256
Cdd:cd05626 161 qkgshirQDSMEPsdlwddvsncrcGDRLktleqratkqhqrclaHSLVGTPNYIAPEVLLRKGYTQlCDWWSVGVILFE 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34098881 257 LLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDSAKDFVKKLL--VKDPRARLTAAQALSHAWVREGGNATDI 331
Cdd:cd05626 241 MLVGQPPFLAPTPTETQLKVINWENTLHIPPQVKLSPEAVDLITKLCcsAEERLGRNGADDIKAHPFFSEVDFSSDI 317
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
60-326 1.62e-20

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 95.57  E-value: 1.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881    60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRV--------AVKRLDKSKMVLPIaveDVKREVQilialsgHENVVQFHNAF- 130
Cdd:PTZ00266   13 NEYEVIKKIGNGRFGEVFLVKHKRTQEFFcwkaisyrGLKEREKSQLVIEV---NVMRELK-------HKNIVRYIDRFl 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881   131 -EDDDYVYIVMELCEGGELLDRILS--KKGNRYSEKDAAVVVRQMLKVAGECHL-------HGLVHRDMKPENFLFKS-- 198
Cdd:PTZ00266   83 nKANQKLYILMEFCDAGDLSRNIQKcyKMFGKIEEHAIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFLSTgi 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881   199 -------AQLDS----PL-KATDFGLSDFIKPGKRFHDIVGSAYYVAPEVLKRRSGP---ESDVWSIGVITYILLCGRRP 263
Cdd:PTZ00266  163 rhigkitAQANNlngrPIaKIGDFGLSKNIGIESMAHSCVGTPYYWSPELLLHETKSyddKSDMWALGCIIYELCSGKTP 242
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34098881   264 FWDRTEDGIFKEVLRNKPDFsrkPWATISDSAKDFVKKLLVKDPRARLTAAQALSHAWVREGG 326
Cdd:PTZ00266  243 FHKANNFSQLISELKRGPDL---PIKGKSKELNILIKNLLNLSAKERPSALQCLGYQIIKNVG 302
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
62-310 1.69e-20

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: 91.24  E-value: 1.69e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVME 141
Cdd:cd08228   4 FQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIFEMMDAKARQDCVKEIDLLKQLN-HPNVIKYLDSFIEDNELNIVLE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELLDRI--LSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLdspLKATDFGLSDFIKPG 219
Cdd:cd08228  83 LADAGDLSQMIkyFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGV---VKLGDLGLGRFFSSK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 220 KRF-HDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDgIFKEVLR-NKPDFSRKPWATISDSAK 296
Cdd:cd08228 160 TTAaHSLVGTPYYMSPERIHENGyNFKSDIWSLGCLLYEMAALQSPFYGDKMN-LFSLCQKiEQCDYPPLPTEHYSEKLR 238
                       250
                ....*....|....
gi 34098881 297 DFVKKLLVKDPRAR 310
Cdd:cd08228 239 ELVSMCIYPDPDQR 252
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
61-333 2.01e-20

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


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 92.47  E-value: 2.01e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVA--IHRPNGDRVAVKRLDK--SKMVLpiaVEDVKREVQILIALSGHENVVQFH---NAFEDD 133
Cdd:cd07857   1 RYELIKELGQGAYGIVCSArnAETSEEETVAIKKITNvfSKKIL---AKRALRELKLLRHFRGHKNITCLYdmdIVFPGN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 134 -DYVYIVMELCEGGelLDRILsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGL 212
Cdd:cd07857  78 fNELYLYEELMEAD--LHQII-RSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNA---DCELKICDFGL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 213 SDFIKPGKRFHD-----IVGSAYYVAPEVL--KRRSGPESDVWSIGVITYILLcGRRPFWD-----------------RT 268
Cdd:cd07857 152 ARGFSENPGENAgfmteYVATRWYRAPEIMlsFQSYTKAIDVWSVGCILAELL-GRKPVFKgkdyvdqlnqilqvlgtPD 230
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34098881 269 EDGIFK-------EVLRNKPDFSRKPWATI----SDSAKDFVKKLLVKDPRARLTAAQALSHAWVREGGNATDIPV 333
Cdd:cd07857 231 EETLSRigspkaqNYIRSLPNIPKKPFESIfpnaNPLALDLLEKLLAFDPTKRISVEEALEHPYLAIWHDPDDEPV 306
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
62-322 2.28e-20

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: 90.57  E-value: 2.28e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLD---KSKMVLPIAvedvKREVQILIALSgHENVVQFHNAFEDDD-YVY 137
Cdd:cd08223   2 YQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNlknASKRERKAA----EQEAKLLSKLK-HPNIVSYKESFEGEDgFLY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 138 IVMELCEGGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPEN-FLFKSaqldSPLKATDFGLSDFI 216
Cdd:cd08223  77 IVMGFCEGGDLYTRLKEQKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNiFLTKS----NIIKVGDLGIARVL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 217 KPGKRFHD-IVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNK-PDFSRKpwatISD 293
Cdd:cd08223 153 ESSSDMATtLIGTPYYMSPELFSNKPyNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKlPPMPKQ----YSP 228
                       250       260
                ....*....|....*....|....*....
gi 34098881 294 SAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd08223 229 ELGELIKAMLHQDPEKRPSVKRILRQPYI 257
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
68-321 4.51e-20

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: 90.57  E-value: 4.51e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKR--LDKSKMVLPiavEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCeg 145
Cdd:cd07839   8 IGEGTYGTVFKAKNRETHEIVALKRvrLDDDDEGVP---SSALREICLLKELK-HKNIVRLYDVLHSDKKLTLVFEYC-- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 gellDRILSKK-GNRYSEKDAAVV---VRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLS-DFIKPGK 220
Cdd:cd07839  82 ----DQDLKKYfDSCNGDIDPEIVksfMFQLLKGLAFCHSHNVLHRDLKPQNLLINK---NGELKLADFGLArAFGIPVR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 221 RFHDIVGSAYYVAPEVLKRRSGPES--DVWSIGVITYILLCGRRPFWDRTE-----DGIFKEV----------LRNKPDF 283
Cdd:cd07839 155 CYSAEVVTLWYRPPDVLFGAKLYSTsiDMWSAGCIFAELANAGRPLFPGNDvddqlKRIFRLLgtpteeswpgVSKLPDY 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 34098881 284 SRKP-------WATI----SDSAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd07839 235 KPYPmypattsLVNVvpklNSTGRDLLQNLLVCNPVQRISAEEALQHPY 283
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
57-333 5.36e-20

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: 91.27  E-value: 5.36e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  57 DFHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVkREVQILIALSgHENVVQFHNAF------ 130
Cdd:cd07855   2 DVGDRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVVTTAKRTL-RELKILRHFK-HDNIIAIRDILrpkvpy 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 131 EDDDYVYIVMELCEGGelLDRILsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDF 210
Cdd:cd07855  80 ADFKDVYVVLDLMESD--LHHII-HSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNE---NCELKIGDF 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 211 G----LSDFIKPGKRFH-DIVGSAYYVAPEVLkrRSGPES----DVWSIGVITYILLcGRRP------------------ 263
Cdd:cd07855 154 GmargLCTSPEEHKYFMtEYVATRWYRAPELM--LSLPEYtqaiDMWSVGCIFAEML-GRRQlfpgknyvhqlqliltvl 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 264 ------FWDRTEDGIFKEVLRNKPDFSRKPWATISDSAK----DFVKKLLVKDPRARLTAAQALSHAWVREGGNATDIPV 333
Cdd:cd07855 231 gtpsqaVINAIGADRVRRYIQNLPNKQPVPWETLYPKADqqalDLLSQMLRFDPSERITVAEALQHPFLAKYHDPDDEPD 310
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
68-322 6.19e-20

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 91.42  E-value: 6.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881   68 LGHGQFGYTYVAIHRPNGDRVAVKrldkskmVLPIAVED-----VKREVQILIALSgHENVVQFHNAFEDDDYVYIVMEL 142
Cdd:PLN00034  82 IGSGAGGTVYKVIHRPTGRLYALK-------VIYGNHEDtvrrqICREIEILRDVN-HPNVVKCHDMFDHNGEIQVLLEF 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  143 CEGGELldrilskKGNR-YSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQldsPLKATDFGLSDFI-KPGK 220
Cdd:PLN00034 154 MDGGSL-------EGTHiADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAK---NVKIADFGVSRILaQTMD 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  221 RFHDIVGSAYYVAPEVLK------RRSGPESDVWSIGVITYILLCGRRPFwdrtedGIFKE----VLRNKPDFSRKPWA- 289
Cdd:PLN00034 224 PCNSSVGTIAYMSPERINtdlnhgAYDGYAGDIWSLGVSILEFYLGRFPF------GVGRQgdwaSLMCAICMSQPPEAp 297
                        250       260       270
                 ....*....|....*....|....*....|....
gi 34098881  290 -TISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:PLN00034 298 aTASREFRHFISCCLQREPAKRWSAMQLLQHPFI 331
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
64-308 6.58e-20

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: 89.72  E-value: 6.58e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  64 IGKLLGHGQFGYTYVAihRPNGDrVAVK-----RLDKSKMVLpiavedVKREVQILIAlSGHENVVQFHNAFEDDDYVYI 138
Cdd:cd14063   4 IKEVIGKGRFGRVHRG--RWHGD-VAIKllnidYLNEEQLEA------FKEEVAAYKN-TRHDNLVLFMGACMDPPHLAI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 139 VMELCEGGELLDRILSKKgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQldspLKATDFGL---SDF 215
Cdd:cd14063  74 VTSLCKGRTLYSLIHERK-EKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLENGR----VVITDFGLfslSGL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 216 IKPGKRFHDIV---GSAYYVAPEVLKRRS-----------GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRN-K 280
Cdd:cd14063 149 LQPGRREDTLVipnGWLCYLAPEIIRALSpdldfeeslpfTKASDVYAFGTVWYELLAGRWPFKEQPAESIIWQVGCGkK 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 34098881 281 PDFSR------------KPWATISDSAKDF--VKKLLVKDPR 308
Cdd:cd14063 229 QSLSQldigrevkdilmQCWAYDPEKRPTFsdLLRMLERLPK 270
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
60-322 6.98e-20

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: 89.13  E-value: 6.98e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHR--PNGDRVAVKRLDKSKmvlpiAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVY 137
Cdd:cd14112   3 GRFSFGSEIFRGRFSVIVKAVDSttETDAHCAVKIFEVSD-----EASEAVREFESLRTLQ-HENVQRLIAAFKPSNFAY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 138 IVMELCEGgELLDRILSKkgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQlDSPLKATDFGLSDFIK 217
Cdd:cd14112  77 LVMEKLQE-DVFTRFSSN--DYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVR-SWQVKLVDFGRAQKVS 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 218 P-GKRFHDivGSAYYVAPEVLKRRSG--PESDVWSIGVITYILLCGRRPFW--DRTEDGIFKEVLRNKPDFSRKPwATIS 292
Cdd:cd14112 153 KlGKVPVD--GDTDWASPEFHNPETPitVQSDIWGLGVLTFCLLSGFHPFTseYDDEEETKENVIFVKCRPNLIF-VEAT 229
                       250       260       270
                ....*....|....*....|....*....|
gi 34098881 293 DSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14112 230 QEALRFATWALKKSPTRRMRTDEALEHRWL 259
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
68-323 8.30e-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: 90.19  E-value: 8.30e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSkmVLPIAVEDVKREVQILialsgHE----NVVQFHNAFEDDDYVYIVMELC 143
Cdd:cd06615   9 LGAGNGGVVTKVLHRPSGLIMARKLIHLE--IKPAIRNQIIRELKVL-----HEcnspYIVGFYGAFYSDGEISICMEHM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 144 EGGELlDRILsKKGNRYSEKDAAVVVRQMLKvaGECHL---HGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDfikpgk 220
Cdd:cd06615  82 DGGSL-DQVL-KKAGRIPENILGKISIAVLR--GLTYLrekHKIMHRDVKPSNILVNS---RGEIKLCDFGVSG------ 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 221 RFHD-----IVGSAYYVAPEVLK-RRSGPESDVWSIGVITYILLCGRRP------------FWDRTEDGIFKEVLRNK-- 280
Cdd:cd06615 149 QLIDsmansFVGTRSYMSPERLQgTHYTVQSDIWSLGLSLVEMAIGRYPipppdakeleamFGRPVSEGEAKESHRPVsg 228
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34098881 281 -PDFSRKPWA-------------------TISDSAKDFVKKLLVKDPRARLTAAQALSHAWVR 323
Cdd:cd06615 229 hPPDSPRPMAifelldyivnepppklpsgAFSDEFQDFVDKCLKKNPKERADLKELTKHPFIK 291
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
68-333 8.32e-20

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 90.87  E-value: 8.32e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLpIAVEDVKREVQILIALSgHENVVQFHNAF------EDDDYVYIVME 141
Cdd:cd07877  25 VGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSI-IHAKRTYRELRLLKHMK-HENVIGLLDVFtparslEEFNDVYLVTH 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCegGELLDRILskKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFlfkSAQLDSPLKATDFGLSDfiKPGKR 221
Cdd:cd07877 103 LM--GADLNNIV--KCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNL---AVNEDCELKILDFGLAR--HTDDE 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 222 FHDIVGSAYYVAPEVLKR--RSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLR--------------------- 278
Cdd:cd07877 174 MTGYVATRWYRAPEIMLNwmHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRlvgtpgaellkkissesarny 253
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34098881 279 --NKPDFSRKPWATI----SDSAKDFVKKLLVKDPRARLTAAQALSHAWVREGGNATDIPV 333
Cdd:cd07877 254 iqSLTQMPKMNFANVfigaNPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPDDEPV 314
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
62-332 9.07e-20

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: 90.73  E-value: 9.07e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSkMVLPIAVEDVKREVQILIALSgHENVVQFHNAFED----DDY-- 135
Cdd:cd07879  17 YTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKLSRP-FQSEIFAKRAYRELTLLKHMQ-HENVIGLLDVFTSavsgDEFqd 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 136 VYIVMELCEGGelLDRILskkGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFlfkSAQLDSPLKATDFGLSdf 215
Cdd:cd07879  95 FYLVMPYMQTD--LQKIM---GHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNL---AVNEDCELKILDFGLA-- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 216 ikpgkRFHDI-----VGSAYYVAPEVLKR--RSGPESDVWSIGVITYILLCGRR-----------------------PFW 265
Cdd:cd07879 165 -----RHADAemtgyVVTRWYRAPEVILNwmHYNQTVDIWSVGCIMAEMLTGKTlfkgkdyldqltqilkvtgvpgpEFV 239
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34098881 266 DRTEDGIFKEVLRNKPDFSRKPWATI----SDSAKDFVKKLLVKDPRARLTAAQALSHAWVREGGNATDIP 332
Cdd:cd07879 240 QKLEDKAAKSYIKSLPKYPRKDFSTLfpkaSPQAVDLLEKMLELDVDKRLTATEALEHPYFDSFRDADEET 310
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
66-323 1.15e-19

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: 90.17  E-value: 1.15e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKskmvlPIA-VEDVKREVQ--ILIALSGHENVVQFHNAF------EDDDYV 136
Cdd:cd07850   6 KPIGSGAQGIVCAAYDTVTGQNVAIKKLSR-----PFQnVTHAKRAYRelVLMKLVNHKNIIGLLNVFtpqkslEEFQDV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 137 YIVMELCEGG--ELLDRILSKKGNRYsekdaavVVRQMLkvAGECHLH--GLVHRDMKPENFLFKSaqlDSPLKATDFGL 212
Cdd:cd07850  81 YLVMELMDANlcQVIQMDLDHERMSY-------LLYQML--CGIKHLHsaGIIHRDLKPSNIVVKS---DCTLKILDFGL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 213 SDFIKPGKRFHDIVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCGRRPF--------WDR------TEDGIFKEVL 277
Cdd:cd07850 149 ARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENvDIWSVGCIMGEMIRGTVLFpgtdhidqWNKiieqlgTPSDEFMSRL 228
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34098881 278 --------RNKPDFSRKPWATI-------SDS----------AKDFVKKLLVKDPRARLTAAQALSHAWVR 323
Cdd:cd07850 229 qptvrnyvENRPKYAGYSFEELfpdvlfpPDSeehnklkasqARDLLSKMLVIDPEKRISVDDALQHPYIN 299
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
60-328 1.50e-19

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 89.11  E-value: 1.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881   60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVK--RLDKSKMVLPiavEDVKREVQILIALSgHENVVQFHNAFEDDDYVY 137
Cdd:PLN00009   2 DQYEKVEKIGEGTYGVVYKARDRVTNETIALKkiRLEQEDEGVP---STAIREISLLKEMQ-HGNIVRLQDVVHSEKRLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  138 IVMELceggelLDRILSKKGNRYSE--KDAAVV---VRQMLKVAGECHLHGLVHRDMKPENFLFKSAQldSPLKATDFGL 212
Cdd:PLN00009  78 LVFEY------LDLDLKKHMDSSPDfaKNPRLIktyLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRT--NALKLADFGL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  213 SD-FIKPGKRFHDIVGSAYYVAPEVL---KRRSGPeSDVWSIGVItYILLCGRRPFW--DRTEDGIFKeVLR-------- 278
Cdd:PLN00009 150 ARaFGIPVRTFTHEVVTLWYRAPEILlgsRHYSTP-VDIWSVGCI-FAEMVNQKPLFpgDSEIDELFK-IFRilgtpnee 226
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34098881  279 ------NKPDF-SRKP-W---------ATISDSAKDFVKKLLVKDPRARLTAAQALSHAWVREGGNA 328
Cdd:PLN00009 227 twpgvtSLPDYkSAFPkWppkdlatvvPTLEPAGVDLLSKMLRLDPSKRITARAALEHEYFKDLGDA 293
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
66-311 1.56e-19

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: 90.49  E-value: 1.56e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILiALSGHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd05625   7 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDIL-AEADNEWVVRLYYSFQDKDNLYFVMDYIPG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRILskKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGL------------- 212
Cdd:cd05625  86 GDMMSLLI--RMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDR---DGHIKLTDFGLctgfrwthdskyy 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 213 -------------------------SDFIKPGKR----------FHDIVGSAYYVAPEVLKRRSGPE-SDVWSIGVITYI 256
Cdd:cd05625 161 qsgdhlrqdsmdfsnewgdpencrcGDRLKPLERraarqhqrclAHSLVGTPNYIAPEVLLRTGYTQlCDWWSVGVILFE 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 34098881 257 LLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDSAKDFVKKlLVKDPRARL 311
Cdd:cd05625 241 MLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIK-LCRGPEDRL 294
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
66-299 1.72e-19

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: 90.10  E-value: 1.72e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSGHENVVQFHnAFEDDDYVYIVMELCEG 145
Cdd:cd05628   7 KVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRAERDILVEADSLWVVKMFY-SFQDKLNLYLIMEFLPG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRILSKkgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAqldSPLKATDFGLSDFIKPGKR---- 221
Cdd:cd05628  86 GDMMTLLMKK--DTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSK---GHVKLSDFGLCTGLKKAHRtefy 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 222 ------------FHDI--------------------VGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRT 268
Cdd:cd05628 161 rnlnhslpsdftFQNMnskrkaetwkrnrrqlafstVGTPDYIAPEVFMQTGyNKLCDWWSLGVIMYEMLIGYPPFCSET 240
                       250       260       270
                ....*....|....*....|....*....|.
gi 34098881 269 EDGIFKEVLRNKPDFSRKPWATISDSAKDFV 299
Cdd:cd05628 241 PQETYKKVMNWKETLIFPPEVPISEKAKDLI 271
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
60-324 1.84e-19

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: 89.63  E-value: 1.84e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKskmvlPIAVE----DVKREVQILIALSgHENVVQFHNAFEDDDY 135
Cdd:cd07880  15 DRYRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYR-----PFQSElfakRAYRELRLLKHMK-HENVIGLLDVFTPDLS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 136 V------YIVMELCegGELLDRILskKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFlfkSAQLDSPLKATD 209
Cdd:cd07880  89 LdrfhdfYLVMPFM--GTDLGKLM--KHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNL---AVNEDCELKILD 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 210 FGLSDfiKPGKRFHDIVGSAYYVAPEVLKR--RSGPESDVWSIGVITYILLCGR-----------------------RPF 264
Cdd:cd07880 162 FGLAR--QTDSEMTGYVVTRWYRAPEVILNwmHYTQTVDIWSVGCIMAEMLTGKplfkghdhldqlmeimkvtgtpsKEF 239
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34098881 265 WDRTEDGIFKEVLRNKPDFSRKPWATI----SDSAKDFVKKLLVKDPRARLTAAQALSHAWVRE 324
Cdd:cd07880 240 VQKLQSEDAKNYVKKLPRFRKKDFRSLlpnaNPLAVNVLEKMLVLDAESRITAAEALAHPYFEE 303
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
68-329 3.51e-19

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: 87.82  E-value: 3.51e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMvlPIAVEDVKREVQILiALSGHENVVQFHNAFEDDDYVYIVMELCEGGE 147
Cdd:cd06641  12 IGKGSFGEVFKGIDNRTQKVVAIKIIDLEEA--EDEIEDIQQEITVL-SQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 148 LLDRIlskKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKPGK-RFHDIV 226
Cdd:cd06641  89 ALDLL---EPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSE---HGEVKLADFGVAGQLTDTQiKRN*FV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 227 GSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRkpwATISDSAKDFVKKLLVK 305
Cdd:cd06641 163 GTPFWMAPEVIKQSAyDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLE---GNYSKPLKEFVEACLNK 239
                       250       260
                ....*....|....*....|....
gi 34098881 306 DPRARLTAAQALSHAWVREGGNAT 329
Cdd:cd06641 240 EPSFRPTAKELLKHKFILRNAKKT 263
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
54-323 3.89e-19

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: 87.81  E-value: 3.89e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  54 YSKDFHDHYTIGkLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKmvlpiAVEDVKREVQIL-IALSGHE--NVVQFHNAF 130
Cdd:cd06618  10 YKADLNDLENLG-EIGSGTCGQVYKMRHKKTGHVMAVKQMRRSG-----NKEENKRILMDLdVVLKSHDcpYIVKCYGYF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 131 EDDDYVYIVMELCegGELLDRILSKKGNRYSE----KDAAVVVRQM--LKVAgechlHGLVHRDMKPENFLFKSaqlDSP 204
Cdd:cd06618  84 ITDSDVFICMELM--STCLDKLLKRIQGPIPEdilgKMTVSIVKALhyLKEK-----HGVIHRDVKPSNILLDE---SGN 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 205 LKATDFGLSDFIKPGKRFHDIVGSAYYVAPEVLKRRSGPE----SDVWSIGVITYILLCGRRPFWD-RTEDGIFKEVLRN 279
Cdd:cd06618 154 VKLCDFGISGRLVDSKAKTRSAGCAAYMAPERIDPPDNPKydirADVWSLGISLVELATGQFPYRNcKTEFEVLTKILNE 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 34098881 280 KPDfSRKPWATISDSAKDFVKKLLVKDPRARLTAAQALSHAWVR 323
Cdd:cd06618 234 EPP-SLPPNEGFSPDFCSFVDLCLTKDHRYRPKYRELLQHPFIR 276
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
57-323 4.10e-19

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


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 89.14  E-value: 4.10e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  57 DFHdhyTIgKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILiALSGHENVVQFHNAFEDDDYV 136
Cdd:cd05629   2 DFH---TV-KVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQLAHVKAERDVL-AESDSPWVVSLYYSFQDAQYL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 137 YIVMELCEGGELLDRILskKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLS--- 213
Cdd:cd05629  77 YLIMEFLPGGDLMTMLI--KYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDR---GGHIKLSDFGLStgf 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 214 ------------------------------DFI-------------KPGKRF--HDIVGSAYYVAPEV-LKRRSGPESDV 247
Cdd:cd05629 152 hkqhdsayyqkllqgksnknridnrnsvavDSInltmsskdqiatwKKNRRLmaYSTVGTPDYIAPEIfLQQGYGQECDW 231
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34098881 248 WSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDSAKDFVKKLLVkDPRARL---TAAQALSHAWVR 323
Cdd:cd05629 232 WSLGAIMFECLIGWPPFCSENSHETYRKIINWRETLYFPDDIHLSVEAEDLIRRLIT-NAENRLgrgGAHEIKSHPFFR 309
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
60-264 4.75e-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: 87.44  E-value: 4.75e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGD----RVAVKRLDKSKMvlPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDY 135
Cdd:cd05038   4 RHLKFIKQLGEGHFGSVELCRYDPLGDntgeQVAVKSLQPSGE--EQHMSDFKREIEILRTLD-HEYIVKYKGVCESPGR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 136 --VYIVMELCEGGELLD-------RILSKKGNRYSEkdaavvvrQMLKvaGECHLH--GLVHRDMKPENFLFKSaqlDSP 204
Cdd:cd05038  81 rsLRLIMEYLPSGSLRDylqrhrdQIDLKRLLLFAS--------QICK--GMEYLGsqRYIHRDLAARNILVES---EDL 147
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34098881 205 LKATDFGLSDFIKPGKRFhdivgsaYYV-----------APEVLK-RRSGPESDVWSIGVITYILLCGRRPF 264
Cdd:cd05038 148 VKISDFGLAKVLPEDKEY-------YYVkepgespifwyAPECLReSRFSSASDVWSFGVTLYELFTYGDPS 212
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
66-320 5.05e-19

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: 87.24  E-value: 5.05e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLpiAVEDVKREVQILIALSgHENVVQFHNAF-----------EDDD 134
Cdd:cd14048  12 QCLGRGGFGVVFEAKNKVDDCNYAVKRIRLPNNEL--AREKVLREVRALAKLD-HPGIVRYFNAWlerppegwqekMDEV 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 135 YVYIVMELCEGGELLDRILSKKgnRYSEKDAAVVVRQMLKVA-GECHLH--GLVHRDMKPENFLFksaQLDSPLKATDFG 211
Cdd:cd14048  89 YLYIQMQLCRKENLKDWMNRRC--TMESRELFVCLNIFKQIAsAVEYLHskGLIHRDLKPSNVFF---SLDDVVKVGDFG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 212 LSDFIKPGKRFHDI-------------VGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLcgrRPFwdrtedGIFKEVL 277
Cdd:cd14048 164 LVTAMDQGEPEQTVltpmpayakhtgqVGTRLYMSPEQIHGNQYSEKvDIFALGLILFELI---YSF------STQMERI 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 34098881 278 RNKPDFSRKPWATISDS----AKDFVKKLLVKDPRARLTAAQALSHA 320
Cdd:cd14048 235 RTLTDVRKLKFPALFTNkypeERDMVQQMLSPSPSERPEAHEVIEHA 281
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
57-312 5.33e-19

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 86.83  E-value: 5.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881   57 DFHDHYTIGKLLG--HGQFGYTYVAIHRPNgDRVAVKRLDKSKMVLPIavedvkrEVQILIALSGHENVVQFHNAFEDDD 134
Cdd:PHA03390  11 QFLKNCEIVKKLKliDGKFGKVSVLKHKPT-QKLFVQKIIKAKNFNAI-------EPMVHQLMKDNPNFIKLYYSVTTLK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  135 YVYIVMELCEGGELLDriLSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLF--KSAQLdsplKATDFGL 212
Cdd:PHA03390  83 GHVLIMDYIKDGDLFD--LLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYdrAKDRI----YLCDYGL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  213 SDFIK-PGKrfHDivGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCGRRPFwDRTEDGIF-----KEVLRNKPDFSR 285
Cdd:PHA03390 157 CKIIGtPSC--YD--GTLDYFSPEKIKGHNYDVSfDWWAVGVLTYELLTGKHPF-KEDEDEELdleslLKRQQKKLPFIK 231
                        250       260
                 ....*....|....*....|....*..
gi 34098881  286 KpwatISDSAKDFVKKLLVKDPRARLT 312
Cdd:PHA03390 232 N----VSKNANDFVQSMLKYNINYRLT 254
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
49-265 5.97e-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: 87.39  E-value: 5.97e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  49 RTDFGYSKdfHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHN 128
Cdd:cd08229  15 RPDMGYNT--LANFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLN-HPNVIKYYA 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 129 AFEDDDYVYIVMELCEGGEL--LDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLdspLK 206
Cdd:cd08229  92 SFIEDNELNIVLELADAGDLsrMIKHFKKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGV---VK 168
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34098881 207 ATDFGLSDFIKPGKRF-HDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFW 265
Cdd:cd08229 169 LGDLGLGRFFSSKTTAaHSLVGTPYYMSPERIHENGyNFKSDIWSLGCLLYEMAALQSPFY 229
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
67-264 6.07e-19

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: 86.68  E-value: 6.07e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  67 LLGHGQFGYTYVAIHRpnGDRVAVKRL------DKSKMVlpiavEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVM 140
Cdd:cd14061   1 VIGVGGFGKVYRGIWR--GEEVAVKAArqdpdeDISVTL-----ENVRQEARLFWMLR-HPNIIALRGVCLQPPNLCLVM 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCEGGELlDRILSKKgnrysEKDAAVVVRQMLKVA-GECHLHG-----LVHRDMKPENFLFKSA-----QLDSPLKATD 209
Cdd:cd14061  73 EYARGGAL-NRVLAGR-----KIPPHVLVDWAIQIArGMNYLHNeapvpIIHRDLKSSNILILEAienedLENKTLKITD 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 34098881 210 FGLSDFIKPGKRFhDIVGSAYYVAPEVLK-RRSGPESDVWSIGVITYILLCGRRPF 264
Cdd:cd14061 147 FGLAREWHKTTRM-SAAGTYAWMAPEVIKsSTFSKASDVWSYGVLLWELLTGEVPY 201
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
68-320 6.80e-19

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: 86.69  E-value: 6.80e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKskmvlPIA-VEDVK---REVQILIALSGHENVVQFHNAFEDDDYVYIVMELC 143
Cdd:cd14051   8 IGSGEFGSVYKCINRLDGCVYAIKKSKK-----PVAgSVDEQnalNEVYAHAVLGKHPHVVRYYSAWAEDDHMIIQNEYC 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 144 EGGELLDRILS--KKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPEN-FLFKSAQLDSP---------------- 204
Cdd:cd14051  83 NGGSLADAISEneKAGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNiFISRTPNPVSSeeeeedfegeednpes 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 205 ----LKATDFGLSDFIKPGKrfhdiV--GSAYYVAPEVLKR--RSGPESDVWSIGvITYILLCGRRPF------WDRTED 270
Cdd:cd14051 163 nevtYKIGDLGHVTSISNPQ-----VeeGDCRFLANEILQEnySHLPKADIFALA-LTVYEAAGGGPLpkngdeWHEIRQ 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 34098881 271 GifkevlrNKPDFSRkpwatISDSAKDFVKKLLVKDPRARLTAAQALSHA 320
Cdd:cd14051 237 G-------NLPPLPQ-----CSPEFNELLRSMIHPDPEKRPSAAALLQHP 274
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
66-311 7.81e-19

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: 86.88  E-value: 7.81e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSGhENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd05607   8 RVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKMALLEKEILEKVNS-PFIVSLAYAFETKTHLCLVMSLMNG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRILSKkGNRYSEKDAAVVVRQMLkVAGECHLH--GLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKPGKRFH 223
Cdd:cd05607  87 GDLKYHIYNV-GERGIEMERVIFYSAQI-TCGILHLHslKIVYRDMKPENVLLDD---NGNCRLSDLGLAVEVKEGKPIT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 224 DIVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNK-PDFSRKPWATISDSAKDFVKK 301
Cdd:cd05607 162 QRAGTNGYMAPEILKEESYSYPvDWFAMGCSIYEMVAGRTPFRDHKEKVSKEELKRRTlEDEVKFEHQNFTEEAKDICRL 241
                       250
                ....*....|
gi 34098881 302 LLVKDPRARL 311
Cdd:cd05607 242 FLAKKPENRL 251
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
369-504 8.89e-19

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 82.53  E-value: 8.89e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 369 DLRDQFDAIDVDKNGVISLEEMRQALAKDLpwklkdsrvAEILEAIDSNTDGLVDFTEFVAAALHVHQLEEHDsekwqlR 448
Cdd:COG5126   6 KLDRRFDLLDADGDGVLERDDFEALFRRLW---------ATLFSEADTDGDGRISREEFVAGMESLFEATVEP------F 70
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 449 SRAAFEKFDLDKDGYITPEELRMH-TGLRGS---IDPLLDEADIDRDGKISLHEFRRLLR 504
Cdd:COG5126  71 ARAAFDLLDTDGDGKISADEFRRLlTALGVSeeeADELFARLDTDGDGKISFEEFVAAVR 130
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
68-333 1.07e-18

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: 87.53  E-value: 1.07e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLdksKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDD-------------- 133
Cdd:cd07854  13 LGCGSNGLVFSAVDSDCDKRVAVKKI---VLTDPQSVKHALREIKIIRRLD-HDNIVKVYEVLGPSgsdltedvgsltel 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 134 DYVYIVMELCEGGelLDRILSKkgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLdsPLKATDFGLS 213
Cdd:cd07854  89 NSVYIVQEYMETD--LANVLEQ--GPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDL--VLKIGDFGLA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 214 DFIKP-----GKRFHDIVgSAYYVAPEVL--KRRSGPESDVWSIGVITYILLCGRRPF-----------------WDRTE 269
Cdd:cd07854 163 RIVDPhyshkGYLSEGLV-TKWYRSPRLLlsPNNYTKAIDMWAAGCIFAEMLTGKPLFagaheleqmqlilesvpVVREE 241
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34098881 270 DgiFKEVLRNKPDF-------SRKPWA----TISDSAKDFVKKLLVKDPRARLTAAQALSHAWVREGGNATDIPV 333
Cdd:cd07854 242 D--RNELLNVIPSFvrndggePRRPLRdllpGVNPEALDFLEQILTFNPMDRLTAEEALMHPYMSCYSCPFDEPV 314
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
110-319 1.67e-18

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: 85.92  E-value: 1.67e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 110 EVQILIALSGHENVVQFHNAFEDDDYvyivmELCEGGELLDRILSKK-------------------------------GN 158
Cdd:cd13974  53 EYSLLSLLHDQDGVVHHHGLFQDRAC-----EIKEDKSSNVYTGRVRkrlclvldclcahdfsdktadlinlqhyvirEK 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 159 RYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKsaQLDSPLKATDFGLS-------DFIKpgkrfhDIVGSAYY 231
Cdd:cd13974 128 RLSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLN--KRTRKITITNFCLGkhlvsedDLLK------DQRGSPAY 199
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 232 VAPEVLKRR--SGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLR---NKPDFSRkpwatISDSAKDFVKKLLVKD 306
Cdd:cd13974 200 ISPDVLSGKpyLGKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAaeyTIPEDGR-----VSENTVCLIRKLLVLN 274
                       250
                ....*....|...
gi 34098881 307 PRARLTAAQALSH 319
Cdd:cd13974 275 PQKRLTASEVLDS 287
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
60-319 1.75e-18

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: 85.82  E-value: 1.75e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKmvlpiAVEDVK----REVQILIALSgHENVVQFHNAFEDDDY 135
Cdd:cd07848   1 NKFEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSE-----ENEEVKettlRELKMLRTLK-QENIVELKEAFRRRGK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 136 VYIVMELCEGGELldRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDF 215
Cdd:cd07848  75 LYLVFEYVEKNML--ELLEEMPNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISH---NDVLKLCDFGFARN 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 216 IKPGK--RFHDIVGSAYYVAPE-VLKRRSGPESDVWSIGVITYILLCGRRPFWDRTE-DGIFK-------------EVLR 278
Cdd:cd07848 150 LSEGSnaNYTEYVATRWYRSPElLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEiDQLFTiqkvlgplpaeqmKLFY 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 34098881 279 NKPDFS--------------RKPWATISDSAKDFVKKLLVKDPRARLTAAQALSH 319
Cdd:cd07848 230 SNPRFHglrfpavnhpqsleRRYLGILSGVLLDLMKNLLKLNPTDRYLTEQCLNH 284
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
68-280 1.79e-18

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: 85.74  E-value: 1.79e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVK--RLD---KSKmvlpiavEDVKREVQILIALSgHENVVQFHNAFED-----DDYVY 137
Cdd:cd14039   1 LGTGGFGNVCLYQNQETGEKIAIKscRLElsvKNK-------DRWCHEIQIMKKLN-HPNVVKACDVPEEmnflvNDVPL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 138 IVMELCEGGELlDRILSKKGNRYSEKDAAVVvrQMLKVAGE----CHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLS 213
Cdd:cd14039  73 LAMEYCSGGDL-RKLLNKPENCCGLKESQVL--SLLSDIGSgiqyLHENKIIHRDLKPENIVLQEINGKIVHKIIDLGYA 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34098881 214 DFIKPGKRFHDIVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNK 280
Cdd:cd14039 150 KDLDQGSLCTSFVGTLQYLAPELFENKSYTVTvDYWSFGTMVFECIAGFRPFLHNLQPFTWHEKIKKK 217
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
68-317 2.20e-18

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: 85.13  E-value: 2.20e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRpnGDRVAVKRLDKSKMVLPiAVEDVKREVQILiALSgHENVVQF---HNAFEDDDYVYIVMELCe 144
Cdd:cd13979  11 LGSGGFGSVYKATYK--GETVAVKIVRRRRKNRA-SRQSFWAELNAA-RLR-HENIVRVlaaETGTDFASLGLIIMEYC- 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 145 GGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFksAQLDSPlKATDFG----LSDFIKPGK 220
Cdd:cd13979  85 GNGTLQQLIYEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILI--SEQGVC-KLCDFGcsvkLGEGNEVGT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 221 RFHDIVGSAYYVAPEVLK-RRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRN-KPDFSRKPWATISDSAKDF 298
Cdd:cd13979 162 PRSHIGGTYTYRAPELLKgERVTPKADIYSFGITLWQMLTRELPYAGLRQHVLYAVVAKDlRPDLSGLEDSEFGQRLRSL 241
                       250
                ....*....|....*....
gi 34098881 299 VKKLLVKDPRARLTAAQAL 317
Cdd:cd13979 242 ISRCWSAQPAERPNADESL 260
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
62-321 2.69e-18

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


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 86.27  E-value: 2.69e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKskmvlpiAVEDVK------REVQILIALSgHENVVQF--------H 127
Cdd:cd07858   7 YVPIKPIGRGAYGIVCSAKNSETNEKVAIKKIAN-------AFDNRIdakrtlREIKLLRHLD-HENVIAIkdimppphR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 128 NAFEDddyVYIVMELCEGGelLDRILsKKGNRYSEKDAAVVVRQMLKvaGECHLH--GLVHRDMKPENFLFKSaqlDSPL 205
Cdd:cd07858  79 EAFND---VYIVYELMDTD--LHQII-RSSQTLSDDHCQYFLYQLLR--GLKYIHsaNVLHRDLKPSNLLLNA---NCDL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 206 KATDFGLSdfiKPGKRFHDI----VGSAYYVAPEVLKRRS--GPESDVWSIGVITYILLcGRRPFWD------------- 266
Cdd:cd07858 148 KICDFGLA---RTTSEKGDFmteyVVTRWYRAPELLLNCSeyTTAIDVWSVGCIFAELL-GRKPLFPgkdyvhqlklite 223
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 267 -----RTEDGIF------KEVLRNKPDFSRKP----WATISDSAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd07858 224 llgspSEEDLGFirnekaRRYIRSLPYTPRQSfarlFPHANPLAIDLLEKMLVFDPSKRITVEEALAHPY 293
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
66-311 2.84e-18

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


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 85.32  E-value: 2.84e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILiALSGHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd05608   7 RVLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKGYEGAMVEKRIL-AKVHSRFIVSLAYAFQTKTDLCLVMTIMNG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRI--LSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKPGK-RF 222
Cdd:cd05608  86 GDLRYHIynVDEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDD---DGNVRISDLGLAVELKDGQtKT 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 223 HDIVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDSAKDFVKK 301
Cdd:cd05608 163 KGYAGTPGFMAPELLLGEEYDYSvDYFTLGVTLYEMIAARGPFRARGEKVENKELKQRILNDSVTYSEKFSPASKSICEA 242
                       250
                ....*....|
gi 34098881 302 LLVKDPRARL 311
Cdd:cd05608 243 LLAKDPEKRL 252
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
68-319 3.75e-18

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: 84.78  E-value: 3.75e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVK--RLDKSKMVLP-IAVedvkREVQILIALSgHENVVQFHNAFEDDDYVYIVMEL-- 142
Cdd:cd07861   8 IGEGTYGVVYKGRNKKTGQIVAMKkiRLESEEEGVPsTAI----REISLLKELQ-HPNIVCLEDVLMQENRLYLVFEFls 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 143 CEGGELLDRILSKKgnrysEKDAAVV---VRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLdspLKATDFGLS-DFIKP 218
Cdd:cd07861  83 MDLKKYLDSLPKGK-----YMDAELVksyLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGV---IKLADFGLArAFGIP 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 GKRF-HDIVgSAYYVAPEVL---KRRSGPeSDVWSIGVItYILLCGRRPFW--DRTEDGIFK--EVLRNK---------- 280
Cdd:cd07861 155 VRVYtHEVV-TLWYRAPEVLlgsPRYSTP-VDIWSIGTI-FAEMATKKPLFhgDSEIDQLFRifRILGTPtediwpgvts 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 34098881 281 -PDFSRK--PWAT---------ISDSAKDFVKKLLVKDPRARLTAAQALSH 319
Cdd:cd07861 232 lPDYKNTfpKWKKgslrtavknLDEDGLDLLEKMLIYDPAKRISAKKALVH 282
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
69-264 5.30e-18

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: 83.47  E-value: 5.30e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  69 GHGQFGYTYVAIHRPNGDRVAVKRLDKskmvlpiavedVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEGGEL 148
Cdd:cd14060   2 GGGSFGSVYRAIWVSQDKEVAVKKLLK-----------IEKEAEILSVLS-HRNIIQFYGAILEAPNYGIVTEYASYGSL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 149 LDRILSkkgNRYSEKDAAVVVRQMLKVA-GECHLH-----GLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIkpGKRF 222
Cdd:cd14060  70 FDYLNS---NESEEMDMDQIMTWATDIAkGMHYLHmeapvKVIHRDLKSRNVVIAA---DGVLKICDFGASRFH--SHTT 141
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 34098881 223 H-DIVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCGRRPF 264
Cdd:cd14060 142 HmSLVGTFPWMAPEVIQSLPVSETcDTYSYGVVLWEMLTREVPF 185
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
68-319 5.41e-18

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: 84.21  E-value: 5.41e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRldKSKMVLPIAVEDVK-REVQILIALSGHENVVQFHNAFEDDDYVYIVMELCEGG 146
Cdd:cd14139   8 IGVGEFGSVYKCIKRLDGCVYAIKR--SMRPFAGSSNEQLAlHEVYAHAVLGHHPHVVRYYSAWAEDDHMIIQNEYCNGG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 147 ELLDRIL--SKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPEN-FLFKSAQLDSPLKATDFGLSDFIKPGKRFH 223
Cdd:cd14139  86 SLQDAISenTKSGNHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNiFICHKMQSSSGVGEEVSNEEDEFLSANVVY 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 224 DI---------------VGSAYYVAPEVLKR--RSGPESDVWSIGvITYILLCGRRPF------WDRTEDGifkevlrNK 280
Cdd:cd14139 166 KIgdlghvtsinkpqveEGDSRFLANEILQEdyRHLPKADIFALG-LTVALAAGAEPLptngaaWHHIRKG-------NF 237
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 34098881 281 PDFSRKpwatISDSAKDFVKKLLVKDPRARLTAAQALSH 319
Cdd:cd14139 238 PDVPQE----LPESFSSLLKNMIQPDPEQRPSATALARH 272
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
62-311 5.59e-18

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: 85.47  E-value: 5.59e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVaIHRPNGDRVAVKRLDKSKMVLPIA-VEDVKREVQILIALSGHENVVQFHNAFEDDDYVYIVM 140
Cdd:cd05618  22 FDLLRVIGRGSYAKVLL-VRLKKTERIYAMKVVKKELVNDDEdIDWVQTEKHVFEQASNHPFLVGLHSCFQTESRLFFVI 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCEGGELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGL-SDFIKPG 219
Cdd:cd05618 101 EYVNGGDLMFHM--QRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDS---EGHIKLTDYGMcKEGLRPG 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 220 KRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPF---------WDRTEDGIFKEVLRNKPDFSRkpwa 289
Cdd:cd05618 176 DTTSTFCGTPNYIAPEILRGEDyGFSVDWWALGVLMFEMMAGRSPFdivgssdnpDQNTEDYLFQVILEKQIRIPR---- 251
                       250       260
                ....*....|....*....|..
gi 34098881 290 TISDSAKDFVKKLLVKDPRARL 311
Cdd:cd05618 252 SLSVKAASVLKSFLNKDPKERL 273
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
61-320 7.32e-18

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: 84.27  E-value: 7.32e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGqfGYTYVAIHRPNGDRVAVKR--LDKSKMvlpiavEDVKR---EVQILIALSgHENVVQFHNAFEDDDY 135
Cdd:cd08216   3 LYEIGKCFKGG--GVVHLAKHKPTNTLVAVKKinLESDSK------EDLKFlqqEILTSRQLQ-HPNILPYVTSFVVDND 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 136 VYIVMELCEGGELLDRIlskkGNRYSEKDAAVVVRQMLK--VAGECHLH--GLVHRDMKPENFLfksaqLDSPLKATDFG 211
Cdd:cd08216  74 LYVVTPLMAYGSCRDLL----KTHFPEGLPELAIAFILRdvLNALEYIHskGYIHRSVKASHIL-----ISGDGKVVLSG 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 212 LSD---FIKPGKR---FHD----IVGSAYYVAPEVLK---RRSGPESDVWSIGVITYILLCGRRPF-------------- 264
Cdd:cd08216 145 LRYaysMVKHGKRqrvVHDfpksSEKNLPWLSPEVLQqnlLGYNEKSDIYSVGITACELANGVVPFsdmpatqmllekvr 224
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34098881 265 ------WDRT---------EDGIFKEVLRNKPDFSRKPWA--TISDSAKDFVKKLLVKDPRARLTAAQALSHA 320
Cdd:cd08216 225 gttpqlLDCStypleedsmSQSEDSSTEHPNNRDTRDIPYqrTFSEAFHQFVELCLQRDPELRPSASQLLAHS 297
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
62-315 8.04e-18

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: 84.53  E-value: 8.04e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLdksKMVLPIAVEDVKREVQILIAL-SGHENVVQFHNAFEDDD------ 134
Cdd:cd13977   2 YSLIREVGRGSYGVVYEAVVRRTGARVAVKKI---RCNAPENVELALREFWALSSIqRQHPNVIQLEECVLQRDglaqrm 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 135 ------------------------------YVYIVMELCEGGELLDRILSKKGNRYSEKDaavVVRQMLKVAGECHLHGL 184
Cdd:cd13977  79 shgssksdlylllvetslkgercfdprsacYLWFVMEFCDGGDMNEYLLSRRPDRQTNTS---FMLQLSSALAFLHRNQI 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 185 VHRDMKPENFLFKSAQLDSPLKATDFGLSDF-----IKPGK-------RFHDIVGSAYYVAPEVLKRRSGPESDVWSIGV 252
Cdd:cd13977 156 VHRDLKPDNILISHKRGEPILKVADFGLSKVcsgsgLNPEEpanvnkhFLSSACGSDFYMAPEVWEGHYTAKADIFALGI 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 253 ITYILLcGRRPFWD-------------RTEDGI-FKEVLRNKPDFS----RKPWATISDSAKDFVKKLLVKDPRARLTAA 314
Cdd:cd13977 236 IIWAMV-ERITFRDgetkkellgtyiqQGKEIVpLGEALLENPKLElqipLKKKKSMNDDMKQLLRDMLAANPQERPDAF 314

                .
gi 34098881 315 Q 315
Cdd:cd13977 315 Q 315
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
68-332 9.64e-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: 83.63  E-value: 9.64e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSkmvlpIAVEDVKR---EVQILIALSGHENVVQFHNA-FEDDDyVYIVMELC 143
Cdd:cd06617   9 LGRGAYGVVDKMRHVPTGTIMAVKRIRAT-----VNSQEQKRllmDLDISMRSVDCPYTVTFYGAlFREGD-VWICMEVM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 144 EGGelLDRILSK---KGNRYSE----KDAAVVVRqmlkvaGECHLH---GLVHRDMKPENFLfksAQLDSPLKATDFGLS 213
Cdd:cd06617  83 DTS--LDKFYKKvydKGLTIPEdilgKIAVSIVK------ALEYLHsklSVIHRDVKPSNVL---INRNGQVKLCDFGIS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 214 dfikpGKRFHDIV-----GSAYYVAPEvlkrRSGPE---------SDVWSIGvITYI-LLCGRRPF--WdRTEDGIFKEV 276
Cdd:cd06617 152 -----GYLVDSVAktidaGCKPYMAPE----RINPElnqkgydvkSDVWSLG-ITMIeLATGRFPYdsW-KTPFQQLKQV 220
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 34098881 277 LRNKPdfSRKPWATISDSAKDFVKKLLVKDPRARLTAAQALSHAWVREG-GNATDIP 332
Cdd:cd06617 221 VEEPS--PQLPAEKFSPEFQDFVNKCLKKNYKERPNYPELLQHPFFELHlSKNTDVA 275
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
68-324 1.07e-17

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 83.95  E-value: 1.07e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSkmVLPIAVEDVKREVQILialsgHE----NVVQFHNAFEDDDYVYIVMELC 143
Cdd:cd06650  13 LGAGNGGVVFKVSHKPSGLVMARKLIHLE--IKPAIRNQIIRELQVL-----HEcnspYIVGFYGAFYSDGEISICMEHM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 144 EGGELlDRILSKKGnRYSEKDAAVVVRQMLKvaGECHL---HGLVHRDMKPENFLFKSAqldSPLKATDFGLSDFIKPGK 220
Cdd:cd06650  86 DGGSL-DQVLKKAG-RIPEQILGKVSIAVIK--GLTYLrekHKIMHRDVKPSNILVNSR---GEIKLCDFGVSGQLIDSM 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 221 RfHDIVGSAYYVAPEVLK-RRSGPESDVWSIGVITYILLCGR------------RPFWDRTEDGIFKEVLRNKPDF---- 283
Cdd:cd06650 159 A-NSFVGTRSYMSPERLQgTHYSVQSDIWSMGLSLVEMAVGRypipppdakeleLMFGCQVEGDAAETPPRPRTPGrpls 237
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34098881 284 -----SRKPWA-------------------TISDSAKDFVKKLLVKDPRARLTAAQALSHAWVRE 324
Cdd:cd06650 238 sygmdSRPPMAifelldyivnepppklpsgVFSLEFQDFVNKCLIKNPAERADLKQLMVHAFIKR 302
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
68-324 1.48e-17

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: 82.79  E-value: 1.48e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDkskmVLPIAVEDVKREVQILIALSGHENVVQFHNAFEDDDYVYIVMELCEGGE 147
Cdd:cd06645  19 IGSGTYGDVYKARNVNTGELAAIKVIK----LEPGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICMEFCGGGS 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 148 LLDriLSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKP--GKRfHDI 225
Cdd:cd06645  95 LQD--IYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTD---NGHVKLADFGVSAQITAtiAKR-KSF 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 226 VGSAYYVAPEV--LKRRSGPES--DVWSIGVITYILLCGRRPFWD-RTEDGIFkevLRNKPDFSR---KPWATISDSAKD 297
Cdd:cd06645 169 IGTPYWMAPEVaaVERKGGYNQlcDIWAVGITAIELAELQPPMFDlHPMRALF---LMTKSNFQPpklKDKMKWSNSFHH 245
                       250       260
                ....*....|....*....|....*..
gi 34098881 298 FVKKLLVKDPRARLTAAQALSHAWVRE 324
Cdd:cd06645 246 FVKMALTKNPKKRPTAEKLLQHPFVTQ 272
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
71-319 1.77e-17

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: 82.36  E-value: 1.77e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  71 GQFGYTYVAIHRPNGDRVAVKRldkskmvlpIAVEDVK-REVQILiALSGHENVVQFHNAFEDDDYVYIVMELCEGGELL 149
Cdd:cd13995  15 GAFGKVYLAQDTKTKKRMACKL---------IPVEQFKpSDVEIQ-ACFRHENIAELYGALLWEETVHLFMEAGEGGSVL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 150 DRILSKKGNRysEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAqldsplKA--TDFGLSDFIKPGKRF-HDIV 226
Cdd:cd13995  85 EKLESCGPMR--EFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMST------KAvlVDFGLSVQMTEDVYVpKDLR 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 227 GSAYYVAPEV-LKRRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVL----RNKPDFSRKPwATISDSAKDFVKK 301
Cdd:cd13995 157 GTEIYMSPEViLCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAYPSYLyiihKQAPPLEDIA-QDCSPAMRELLEA 235
                       250
                ....*....|....*...
gi 34098881 302 LLVKDPRARLTAAQALSH 319
Cdd:cd13995 236 ALERNPNHRSSAAELLKH 253
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
62-317 1.92e-17

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 84.92  E-value: 1.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881   62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVlPIAVEDVKREVQILIALSgHENVVQFHNAFEDDD------- 134
Cdd:PTZ00283  34 YWISRVLGSGATGTVLCAKRVSDGEPFAVKVVDMEGMS-EADKNRAQAEVCCLLNCD-FFSIVKCHEDFAKKDprnpenv 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  135 -YVYIVMELCEGGELLDRILSK-KGNR-YSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLdspLKATDFG 211
Cdd:PTZ00283 112 lMIALVLDYANAGDLRQEIKSRaKTNRtFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGL---VKLGDFG 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  212 LSDFIKP------GKRFhdiVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFwdrteDGIFKEVLRNKP--- 281
Cdd:PTZ00283 189 FSKMYAAtvsddvGRTF---CGTPYYVAPEIWRRKPySKKADMFSLGVLLYELLTLKRPF-----DGENMEEVMHKTlag 260
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 34098881  282 DFSRKPwATISDSAKDFVKKLLVKDPRARLTAAQAL 317
Cdd:PTZ00283 261 RYDPLP-PSISPEMQEIVTALLSSDPKRRPSSSKLL 295
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
68-264 1.97e-17

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: 82.32  E-value: 1.97e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAiHRPNGDRVAVKRL-DKSKMVLpiaVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEGG 146
Cdd:cd14066   1 IGSGGFGTVYKG-VLENGTVVAVKRLnEMNCAAS---KKEFLTELEMLGRLR-HPNLVRLLGYCLESDEKLLVYEYMPNG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 147 ELLDRILSKKGNRysekdaAVVVRQMLKVA-----GECHLHG-----LVHRDMKPENFLfksaqLDSPL--KATDFGLS- 213
Cdd:cd14066  76 SLEDRLHCHKGSP------PLPWPQRLKIAkgiarGLEYLHEecpppIIHGDIKSSNIL-----LDEDFepKLTDFGLAr 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 34098881 214 --DFIKPGKRFHDIVGSAYYVAPEVLK-RRSGPESDVWSIGVITYILLCGRRPF 264
Cdd:cd14066 145 liPPSESVSKTSAVKGTIGYLAPEYIRtGRVSTKSDVYSFGVVLLELLTGKPAV 198
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
68-322 2.06e-17

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: 82.41  E-value: 2.06e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMvlPIAVEDVKREVQILiALSGHENVVQFHNAFEDDDYVYIVMELCEGGE 147
Cdd:cd06640  12 IGKGSFGEVFKGIDNRTQQVVAIKIIDLEEA--EDEIEDIQQEITVL-SQCDSPYVTKYYGSYLKGTKLWIIMEYLGGGS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 148 LLDRIlskKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFkSAQLDspLKATDFGLSDFIKPGK-RFHDIV 226
Cdd:cd06640  89 ALDLL---RAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLL-SEQGD--VKLADFGVAGQLTDTQiKRNTFV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 227 GSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKP-----DFSRkpwatisdSAKDFVK 300
Cdd:cd06640 163 GTPFWMAPEVIQQSAyDSKADIWSLGITAIELAKGEPPNSDMHPMRVLFLIPKNNPptlvgDFSK--------PFKEFID 234
                       250       260
                ....*....|....*....|..
gi 34098881 301 KLLVKDPRARLTAAQALSHAWV 322
Cdd:cd06640 235 ACLNKDPSFRPTAKELLKHKFI 256
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
59-322 2.13e-17

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: 82.38  E-value: 2.13e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  59 HDhYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLdksKMVLPIAVEDVKREVqILIALSGHENVVQFHNAFEDDDYVYI 138
Cdd:cd06646   9 HD-YELIQRVGSGTYGDVYKARNLHTGELAAVKII---KLEPGDDFSLIQQEI-FMVKECKHCNIVAYFGSYLSREKLWI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 139 VMELCEGGELLDrILSKKGNrYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKP 218
Cdd:cd06646  84 CMEYCGGGSLQD-IYHVTGP-LSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTD---NGDVKLADFGVAAKITA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 --GKRfHDIVGSAYYVAPEV--LKRRSGPES--DVWSIGVITYILLCGRRPFWD-RTEDGIFkevLRNKPDFS------R 285
Cdd:cd06646 159 tiAKR-KSFIGTPYWMAPEVaaVEKNGGYNQlcDIWAVGITAIELAELQPPMFDlHPMRALF---LMSKSNFQppklkdK 234
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 34098881 286 KPWATisdSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd06646 235 TKWSS---TFHNFVKISLTKNPKKRPTAERLLTHLFV 268
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
68-282 2.24e-17

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: 82.12  E-value: 2.24e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLdKSKMVLPIAVEDVKREVQILiALSGHENVVQFHNAFEDDDYVYIVMELCEGG- 146
Cdd:cd13978   1 LGSGGFGTVSKARHVSWFGMVAIKCL-HSSPNCIEERKALLKEAEKM-ERARHSYVLPLLGVCVERRSLGLVMEYMENGs 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 147 --ELLDRilskkgnRYSEKDAAVVVRQMLKVA-GECHLHG----LVHRDMKPENFLfksaqLDSPLKA--TDFGLSDF-- 215
Cdd:cd13978  79 lkSLLER-------EIQDVPWSLRFRIIHEIAlGMNFLHNmdppLLHHDLKPENIL-----LDNHFHVkiSDFGLSKLgm 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34098881 216 -IKPGKRFHD---IVGSAYYVAPEVLK---RRSGPESDVWSIGVITYILLCGRRPFWDRTEDG-IFKEVLR-NKPD 282
Cdd:cd13978 147 kSISANRRRGtenLGGTPIYMAPEAFDdfnKKPTSKSDVYSFAIVIWAVLTRKEPFENAINPLlIMQIVSKgDRPS 222
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
57-311 3.34e-17

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: 83.15  E-value: 3.34e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  57 DFHDHYTIGKLLGHGQFGYTYVaIHRPNGDRVAVKRLDKSKMVLPIAV---------ED---VKREVQILIALSGHENVV 124
Cdd:cd05617   1 DGMDGIKISQGLGLQDFDLIRV-IGRGSYAKVLLVRLKKNDQIYAMKVvkkelvhddEDidwVQTEKHVFEQASSNPFLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 125 QFHNAFEDDDYVYIVMELCEGGELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSP 204
Cdd:cd05617  80 GLHSCFQTTSRLFLVIEYVNGGDLMFHM--QRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDA---DGH 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 205 LKATDFGL-SDFIKPGKRFHDIVGSAYYVAPEVLK-RRSGPESDVWSIGVITYILLCGRRPFwD--------RTEDGIFK 274
Cdd:cd05617 155 IKLTDYGMcKEGLGPGDTTSTFCGTPNYIAPEILRgEEYGFSVDWWALGVLMFEMMAGRSPF-DiitdnpdmNTEDYLFQ 233
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 34098881 275 EVLRNKPDFSRkpwaTISDSAKDFVKKLLVKDPRARL 311
Cdd:cd05617 234 VILEKPIRIPR----FLSVKASHVLKGFLNKDPKERL 266
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
68-264 3.83e-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: 81.93  E-value: 3.83e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSkmvlpIAVEDVKR---EVQILIALSgHENVVQFHNAFED------DDYVYI 138
Cdd:cd14038   2 LGTGGFGNVLRWINQETGEQVAIKQCRQE-----LSPKNRERwclEIQIMKRLN-HPNVVAARDVPEGlqklapNDLPLL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 139 VMELCEGGELlDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHG--LVHRDMKPENFLFKSAQLDSPLKATDFGLSDFI 216
Cdd:cd14038  76 AMEYCQGGDL-RKYLNQFENCCGLREGAILTLLSDISSALRYLHEnrIIHRDLKPENIVLQQGEQRLIHKIIDLGYAKEL 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 34098881 217 KPGKRFHDIVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCGRRPF 264
Cdd:cd14038 155 DQGSLCTSFVGTLQYLAPELLEQQKYTVTvDYWSFGTLAFECITGFRPF 203
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
67-316 3.91e-17

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: 82.23  E-value: 3.91e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  67 LLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILiALSGHENVVQFHNAFEDDDYVYIVMELCEGG 146
Cdd:cd05585   1 VIGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRSEVTHTLAERTVL-AQVDCPFIVPLKFSFQSPEKLYLVLAFINGG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 147 ELLDRiLSKKGnRYSEKDAAVVVRQMLkVAGEChLHGL--VHRDMKPENFLFKSAqldSPLKATDFGLSDF-IKPGKRFH 223
Cdd:cd05585  80 ELFHH-LQREG-RFDLSRARFYTAELL-CALEC-LHKFnvIYRDLKPENILLDYT---GHIALCDFGLCKLnMKDDDKTN 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 224 DIVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSrkpwATISDSAKDFVKKL 302
Cdd:cd05585 153 TFCGTPEYLAPELLLGHGYTKAvDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFP----DGFDRDAKDLLIGL 228
                       250
                ....*....|....
gi 34098881 303 LVKDPRARLTAAQA 316
Cdd:cd05585 229 LNRDPTKRLGYNGA 242
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
107-320 4.86e-17

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: 80.87  E-value: 4.86e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 107 VKREVQILIALSgHENVVQFHnAF----EDDDY---VYIVMELCEGG---ELLDRILS---KKGNRYsekdaavvVRQML 173
Cdd:cd14012  45 LEKELESLKKLR-HPNLVSYL-AFsierRGRSDgwkVYLLTEYAPGGslsELLDSVGSvplDTARRW--------TLQLL 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 174 KVAGECHLHGLVHRDMKPEN-FLFKSAQlDSPLKATDFGLsdfikpGKRFHDIVG--------SAYYVAPEVLK--RRSG 242
Cdd:cd14012 115 EALEYLHRNGVVHKSLHAGNvLLDRDAG-TGIVKLTDYSL------GKTLLDMCSrgsldefkQTYWLPPELAQgsKSPT 187
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34098881 243 PESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFsrkpwatisdsaKDFVKKLLVKDPRARLTAAQALSHA 320
Cdd:cd14012 188 RKTDVWDLGLLFLQMLFGLDVLEKYTSPNPVLVSLDLSASL------------QDFLSKCLSLDPKKRPTALELLPHE 253
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
68-325 5.19e-17

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


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 82.87  E-value: 5.19e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLpIAVEDVKREVQILIALSgHENVVQ--------FHNAFEDddyVYIV 139
Cdd:cd07853   8 IGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNL-VSCKRVFRELKMLCFFK-HDNVLSaldilqppHIDPFEE---IYVV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGgELLDRILSKKgnRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKPG 219
Cdd:cd07853  83 TELMQS-DLHKIIVSPQ--PLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNS---NCVLKICDFGLARVEEPD 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 220 KRFHDI--VGSAYYVAPEVL--KRRSGPESDVWSIGVITYILLCGRRPFWDRTE-----------------------DGI 272
Cdd:cd07853 157 ESKHMTqeVVTQYYRAPEILmgSRHYTSAVDIWSVGCIFAELLGRRILFQAQSPiqqldlitdllgtpsleamrsacEGA 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 34098881 273 FKEVLRNK---PDFSR--KPWATISDSAKDFVKKLLVKDPRARLTAAQALSHAWVREG 325
Cdd:cd07853 237 RAHILRGPhkpPSLPVlyTLSSQATHEAVHLLCRMLVFDPDKRISAADALAHPYLDEG 294
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
67-310 5.23e-17

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: 80.80  E-value: 5.23e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  67 LLGHGQFGYTYVAIHRpnGDRVAVK--RLDKSKMVlPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCE 144
Cdd:cd14148   1 IIGVGGFGKVYKGLWR--GEEVAVKaaRQDPDEDI-AVTAENVRQEARLFWMLQ-HPNIIALRGVCLNPPHLCLVMEYAR 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 145 GGELlDRILSKKgnrysEKDAAVVVRQMLKVA-GECHLHG-----LVHRDMKPENFLFKSAQ-----LDSPLKATDFGLS 213
Cdd:cd14148  77 GGAL-NRALAGK-----KVPPHVLVNWAVQIArGMNYLHNeaivpIIHRDLKSSNILILEPIenddlSGKTLKITDFGLA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 214 -DFIKPGKRfhDIVGSAYYVAPEVLKRR-SGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNK-----PDFSRK 286
Cdd:cd14148 151 rEWHKTTKM--SAAGTYAWMAPEVIRLSlFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKltlpiPSTCPE 228
                       250       260
                ....*....|....*....|....
gi 34098881 287 PWATISDSAKDfvkkllvKDPRAR 310
Cdd:cd14148 229 PFARLLEECWD-------PDPHGR 245
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
68-321 5.29e-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: 80.73  E-value: 5.29e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKmVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVM--ELCEG 145
Cdd:cd13983   9 LGRGSFKTVYRAFDTEEGIEVAWNEIKLRK-LPKAERQRFKQEIEILKSLK-HPNIIKFYDSWESKSKKEVIFitELMTS 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRIlsKKGNRYSEKdaavVV----RQMLKvaGECHLHG----LVHRDMKPENFLFKSAQLDspLKATDFGLSDFIK 217
Cdd:cd13983  87 GTLKQYL--KRFKRLKLK----VIkswcRQILE--GLNYLHTrdppIIHRDLKCDNIFINGNTGE--VKIGDLGLATLLR 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 218 PGKRfHDIVGSAYYVAPEVLKRRSGPESDVWSIGVITYILLCGRRPFWDRTEDG-IFKEVLRN-KPD-FSRkpwaTISDS 294
Cdd:cd13983 157 QSFA-KSVIGTPEFMAPEMYEEHYDEKVDIYAFGMCLLEMATGEYPYSECTNAAqIYKKVTSGiKPEsLSK----VKDPE 231
                       250       260
                ....*....|....*....|....*..
gi 34098881 295 AKDFVKKLLVKdPRARLTAAQALSHAW 321
Cdd:cd13983 232 LKDFIEKCLKP-PDERPSARELLEHPF 257
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
58-317 5.35e-17

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: 81.40  E-value: 5.35e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  58 FHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEdVKREVQILIALSgHENVVQFHNAFEDDDY-- 135
Cdd:cd14049   4 YLNEFEEIARLGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMK-VLREVKVLAGLQ-HPNIVGYHTAWMEHVQlm 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 136 VYIVMELCEGgELLDRIL--SKKGNRYSEKDAA---VVVRQMLKV-----AGECHLH--GLVHRDMKPENfLFKSAQlDS 203
Cdd:cd14049  82 LYIQMQLCEL-SLWDWIVerNKRPCEEEFKSAPytpVDVDVTTKIlqqllEGVTYIHsmGIVHRDLKPRN-IFLHGS-DI 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 204 PLKATDFGLS---DFIKPGKRFHDI----------VGSAYYVAPEVLK-RRSGPESDVWSIGVITYILLcgrRPFWDRTE 269
Cdd:cd14049 159 HVRIGDFGLAcpdILQDGNDSTTMSrlnglthtsgVGTCLYAAPEQLEgSHYDFKSDMYSIGVILLELF---QPFGTEME 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 34098881 270 DGIFKEVLRNK--PDFSRKPWATISdsakDFVKKLLVKDPRARLTAAQAL 317
Cdd:cd14049 236 RAEVLTQLRNGqiPKSLCKRWPVQA----KYIKLLTSTEPSERPSASQLL 281
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
60-276 5.49e-17

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: 80.76  E-value: 5.49e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAiHRPNGDRVAVKRLDKSKMvlpiAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIV 139
Cdd:cd05112   4 SELTFVQEIGSGQFGLVHLG-YWLNKDKVAIKTIREGAM----SEEDFIEEAEVMMKLS-HPKLVQLYGVCLEQAPICLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGELLDRILSKKGnRYSEKdaaVVVRQMLKVA-GECHLH--GLVHRDMKPENFLFKSAQLdspLKATDFGLSDFI 216
Cdd:cd05112  78 FEFMEHGCLSDYLRTQRG-LFSAE---TLLGMCLDVCeGMAYLEeaSVIHRDLAARNCLVGENQV---VKVSDFGMTRFV 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34098881 217 KpGKRFHDIVGSAYYV---APEVLK-RRSGPESDVWSIGVITYILLC-GRRPFWDRTEDGIFKEV 276
Cdd:cd05112 151 L-DDQYTSSTGTKFPVkwsSPEVFSfSRYSSKSDVWSFGVLMWEVFSeGKIPYENRSNSEVVEDI 214
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
65-276 6.09e-17

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 81.39  E-value: 6.09e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  65 GKLLGHGQFGYTYVAihRPNGDRVAVKRLdkSKMVlPIAVEDVKR----EVQILIALSgHENVVQFHNAFEDDDYVYIVM 140
Cdd:cd14158  20 GNKLGEGGFGVVFKG--YINDKNVAVKKL--AAMV-DISTEDLTKqfeqEIQVMAKCQ-HENLVELLGYSCDGPQLCLVY 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCEGGELLDRILSKKGNrysekdAAVVVRQMLKVA-------GECHLHGLVHRDMKPENFLFKSAQLDsplKATDFGLS 213
Cdd:cd14158  94 TYMPNGSLLDRLACLNDT------PPLSWHMRCKIAqgtangiNYLHENNHIHRDIKSANILLDETFVP---KISDFGLA 164
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34098881 214 dfiKPGKRF------HDIVGSAYYVAPEVLKRRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEV 276
Cdd:cd14158 165 ---RASEKFsqtimtERIVGTTAYMAPEALRGEITPKSDIFSFGVVLLEIITGLPPVDENRDPQLLLDI 230
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
64-321 7.73e-17

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 81.73  E-value: 7.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881   64 IGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVK-----------REVQILIALSgHENVVQFHNAFED 132
Cdd:PTZ00024  13 KGAHLGEGTYGKVEKAYDTLTGKIVAIKKVKIIEISNDVTKDRQLvgmcgihfttlRELKIMNEIK-HENIMGLVDVYVE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  133 DDYVYIVMELCEGGelLDRILSKKgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLdspLKATDFGL 212
Cdd:PTZ00024  92 GDFINLVMDIMASD--LKKVVDRK-IRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGI---CKIADFGL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  213 S---------------DFIKPGKRFHDIVGSAYYVAPEVL--KRRSGPESDVWSIGVITYILLCGRRPFWDRTE----DG 271
Cdd:PTZ00024 166 ArrygyppysdtlskdETMQRREEMTSKVVTLWYRAPELLmgAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEidqlGR 245
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34098881  272 IFKevLRNKPDFSRKPWAT----------------------ISDSAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:PTZ00024 246 IFE--LLGTPNEDNWPQAKklplyteftprkpkdlktifpnASDDAIDLLQSLLKLNPLERISAKEALKHEY 315
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
68-321 8.61e-17

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: 80.82  E-value: 8.61e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVK--RLDKSKMVLPIAVedvkREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd07871  13 LGEGTYATVFKGRSKLTENLVALKeiRLEHEEGAPCTAI----REVSLLKNLK-HANIVTLHDIIHTERCLTLVFEYLDS 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GelLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAqldSPLKATDFGLSDFIK-PGKRFHD 224
Cdd:cd07871  88 D--LKQYLDNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEK---GELKLADFGLARAKSvPTKTYSN 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 225 IVGSAYYVAPEVL---KRRSGPeSDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNKPDFSRKPWATISDSAK----- 296
Cdd:cd07871 163 EVVTLWYRPPDVLlgsTEYSTP-IDMWGVGCILYEMATGRPMFPGSTVKEELHLIFRLLGTPTEETWPGVTSNEEfrsyl 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 34098881 297 ---------------------DFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd07871 242 fpqyraqplinhaprldtdgiDLLSSLLLYETKSRISAEAALRHSY 287
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
68-332 1.31e-16

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: 81.25  E-value: 1.31e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLpIAVEDVKREVQILIALSgHENVVQFHNAF------EDDDYVYIVME 141
Cdd:cd07878  23 VGSGAYGSVCSAYDTRLRQKVAVKKLSRPFQSL-IHARRTYRELRLLKHMK-HENVIGLLDVFtpatsiENFNEVYLVTN 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCegGELLDRILskKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFlfkSAQLDSPLKATDFGLSDfiKPGKR 221
Cdd:cd07878 101 LM--GADLNNIV--KCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNV---AVNEDCELRILDFGLAR--QADDE 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 222 FHDIVGSAYYVAPEVLKR--RSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLR----NKPDFSRK--------- 286
Cdd:cd07878 172 MTGYVATRWYRAPEIMLNwmHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIMEvvgtPSPEVLKKisseharky 251
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 287 ----PWATISDSAK----------DFVKKLLVKDPRARLTAAQALSHAWVREGGNATDIP 332
Cdd:cd07878 252 iqslPHMPQQDLKKifrganplaiDLLEKMLVLDSDKRISASEALAHPYFSQYHDPEDEP 311
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
66-252 1.92e-16

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: 79.31  E-value: 1.92e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAI-HRPNGDR--VAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDyVYIVMEL 142
Cdd:cd05040   1 EKLGDGSFGVVRRGEwTTPSGKViqVAVKCLKSDVLSQPNAMDDFLKEVNAMHSLD-HPNLIRLYGVVLSSP-LMMVTEL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 143 CEGGELLDRiLSKKGNRYSEK---DAAVvvrQMLKVAGECHLHGLVHRDMKPENFLFKSAQLdspLKATDFGLSDFIKPG 219
Cdd:cd05040  79 APLGSLLDR-LRKDQGHFLIStlcDYAV---QIANGMAYLESKRFIHRDLAARNILLASKDK---VKIGDFGLMRALPQN 151
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 34098881 220 K-----RFHDIVGSAyYVAPEVLK-RRSGPESDVWSIGV 252
Cdd:cd05040 152 EdhyvmQEHRKVPFA-WCAPESLKtRKFSHASDVWMFGV 189
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
61-264 2.25e-16

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: 78.93  E-value: 2.25e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRpnGDRVAVKRL-DKSKmvlpiAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIV 139
Cdd:cd05039   7 DLKLGELIGKGEFGDVMLGDYR--GQKVAVKCLkDDST-----AAQAFLAEASVMTTLR-HPNLVQLLGVVLEGNGLYIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGELLDRILSkkgnryseKDAAVVVRQMLK------VAGECHLHG--LVHRDMKPENFLFKSaqlDSPLKATDFG 211
Cdd:cd05039  79 TEYMAKGSLVDYLRS--------RGRAVITRKDQLgfaldvCEGMEYLESkkFVHRDLAARNVLVSE---DNVAKVSDFG 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 34098881 212 LSdfiKPGKRFHDivGSAYYV---APEVLK-RRSGPESDVWSIGVITY-ILLCGRRPF 264
Cdd:cd05039 148 LA---KEASSNQD--GGKLPIkwtAPEALReKKFSTKSDVWSFGILLWeIYSFGRVPY 200
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
61-320 2.37e-16

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 79.01  E-value: 2.37e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLD---KSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVY 137
Cdd:cd06630   1 HWLKGPLLGTGAFSSCYQARDVKTGTLMAVKQVSfcrNSSSEQEEVVEAIREEIRMMARLN-HPNIVRMLGATQHKSHFN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 138 IVMELCEGGElLDRILSKKGnRYSEkdaAVVVRQMLKV-AGECHLHG--LVHRDMKPENFLFKSAQLDspLKATDFGL-- 212
Cdd:cd06630  80 IFVEWMAGGS-VASLLSKYG-AFSE---NVIINYTLQIlRGLAYLHDnqIIHRDLKGANLLVDSTGQR--LRIADFGAaa 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 213 ---SDFIKPGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPfWDRTEDG-----IFKEVLRNKPDF 283
Cdd:cd06630 153 rlaSKGTGAGEFQGQLLGTIAFMAPEVLRGEQyGRSCDVWSVGCVIIEMATAKPP-WNAEKISnhlalIFKIASATTPPP 231
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 34098881 284 SRKpwaTISDSAKDFVKKLLVKDPRARLTAAQALSHA 320
Cdd:cd06630 232 IPE---HLSPGLRDVTLRCLELQPEDRPPARELLKHP 265
PTZ00184 PTZ00184
calmodulin; Provisional
358-503 2.63e-16

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 75.95  E-value: 2.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  358 LASTLDEAEISDLRDQFDAIDVDKNGVISLEEMRQALaKDLPWKLKDSRVAEILEAIDSNTDGLVDFTEFVAaaLHVHQL 437
Cdd:PTZ00184   1 MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVM-RSLGQNPTEAELQDMINEVDADGNGTIDFPEFLT--LMARKM 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34098881  438 EEHDSEKwqlRSRAAFEKFDLDKDGYITPEELR---MHTGLRGS---IDPLLDEADIDRDGKISLHEFRRLL 503
Cdd:PTZ00184  78 KDTDSEE---EIKEAFKVFDRDGNGFISAAELRhvmTNLGEKLTdeeVDEMIREADVDGDGQINYEEFVKMM 146
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
58-322 2.76e-16

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: 79.72  E-value: 2.76e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  58 FHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVK----REVQILIALSgHENVVQFHNAFE-D 132
Cdd:cd14041   4 LNDRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEKKENYHkhacREYRIHKELD-HPRIVKLYDYFSlD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 133 DDYVYIVMELCEGGELlDRILsKKGNRYSEKDAAVVVRQM---LKVAGECHlHGLVHRDMKPENFLFKSAQLDSPLKATD 209
Cdd:cd14041  83 TDSFCTVLEYCEGNDL-DFYL-KQHKLMSEKEARSIIMQIvnaLKYLNEIK-PPIIHYDLKPGNILLVNGTACGEIKITD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 210 FGLSDfIKPGKRFHDI---------VGSAYYVAPEVLKRRSGP-----ESDVWSIGVITYILLCGRRPF-WDRTEDGIFK 274
Cdd:cd14041 160 FGLSK-IMDDDSYNSVdgmeltsqgAGTYWYLPPECFVVGKEPpkisnKVDVWSVGVIFYQCLYGRKPFgHNQSQQDILQ 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 34098881 275 E-VLRNKPDFSRKPWATISDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14041 239 EnTILKATEVQFPPKPVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYL 287
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
57-272 2.90e-16

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: 78.93  E-value: 2.90e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  57 DFHDhYTIGKLLGHGQFGYTYVAIHrpNGDRVAVK--RLDKSKMVlPIAVEDVKREVQiLIALSGHENVVQFHNAFEDDD 134
Cdd:cd14145   4 DFSE-LVLEEIIGIGGFGKVYRAIW--IGDEVAVKaaRHDPDEDI-SQTIENVRQEAK-LFAMLKHPNIIALRGVCLKEP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 135 YVYIVMELCEGGELlDRILSKKgnrysEKDAAVVVRQMLKVA-GECHLHG-----LVHRDMKPENFLF----KSAQLDSP 204
Cdd:cd14145  79 NLCLVMEFARGGPL-NRVLSGK-----RIPPDILVNWAVQIArGMNYLHCeaivpVIHRDLKSSNILIlekvENGDLSNK 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34098881 205 -LKATDFGLSdfikpgKRFH-----DIVGSAYYVAPEVLKRRSGPE-SDVWSIGVITYILLCGRRPFwdRTEDGI 272
Cdd:cd14145 153 iLKITDFGLA------REWHrttkmSAAGTYAWMAPEVIRSSMFSKgSDVWSYGVLLWELLTGEVPF--RGIDGL 219
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
67-272 4.65e-16

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: 78.16  E-value: 4.65e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  67 LLGHGQFGYTYVAIHRpnGDRVAVK--RLDKSKMVLPIAvEDVKREVQiLIALSGHENVVQFHNAFEDDDYVYIVMELCE 144
Cdd:cd14146   1 IIGVGGFGKVYRATWK--GQEVAVKaaRQDPDEDIKATA-ESVRQEAK-LFSMLRHPNIIKLEGVCLEEPNLCLVMEFAR 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 145 GGELlDRILSKKGNRYSEKDAA-----VVVRQMLKVA-GECHLHG-----LVHRDMKPEN-FLFKSAQLD----SPLKAT 208
Cdd:cd14146  77 GGTL-NRALAAANAAPGPRRARripphILVNWAVQIArGMLYLHEeavvpILHRDLKSSNiLLLEKIEHDdicnKTLKIT 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 209 DFGLSdfikpgKRFH-----DIVGSAYYVAPEVLKRRSGPE-SDVWSIGVITYILLCGRRPFwdRTEDGI 272
Cdd:cd14146 156 DFGLA------REWHrttkmSAAGTYAWMAPEVIKSSLFSKgSDIWSYGVLLWELLTGEVPY--RGIDGL 217
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
67-333 5.66e-16

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: 78.56  E-value: 5.66e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  67 LLGHGQFGYTYVAIHRPNGDRVAVKRL----DKSKMvlpiavEDVKREVQILIALSGHENVVQFHNA-FEDDDyVYIVME 141
Cdd:cd06616  13 EIGRGAFGTVNKMLHKPSGTIMAVKRIrstvDEKEQ------KRLLMDLDVVMRSSDCPYIVKFYGAlFREGD-CWICME 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGG-ELLDRILSKKGNRYSEKD-----AAVVVRQM--LKVAgechlHGLVHRDMKPENFLfksaqLD--SPLKATDFG 211
Cdd:cd06616  86 LMDISlDKFYKYVYEVLDSVIPEEilgkiAVATVKALnyLKEE-----LKIIHRDVKPSNIL-----LDrnGNIKLCDFG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 212 LS-DFIKPGKRFHDiVGSAYYVAPEVLKRRSGPE-----SDVWSIGVITYILLCGRRPF--WDRTEDGIFKEVLRNKPDF 283
Cdd:cd06616 156 ISgQLVDSIAKTRD-AGCRPYMAPERIDPSASRDgydvrSDVWSLGITLYEVATGKFPYpkWNSVFDQLTQVVKGDPPIL 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 34098881 284 SRKPWATISDSAKDFVKKLLVKDPRARLTAAQALSHAWVREgGNATDIPV 333
Cdd:cd06616 235 SNSEEREFSPSFVNFVNLCLIKDESKRPKYKELLKHPFIKM-YEERNVDV 283
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
63-278 5.94e-16

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: 77.87  E-value: 5.94e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  63 TIGKLLGHGQFGYTYVAIHRpNGDRVAVKRLDKSKMvlpiAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMEL 142
Cdd:cd05059   7 TFLKELGSGQFGVVHLGKWR-GKIDVAIKMIKEGSM----SEDDFIEEAKVMMKLS-HPKLVQLYGVCTKQRPIFIVTEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 143 CEGGELLDRILSKKGNRYSEK--DAAVVVRQMLKVAGEchlHGLVHRDMKPENFLFKSAQLdspLKATDFGLSDFI---- 216
Cdd:cd05059  81 MANGCLLNYLRERRGKFQTEQllEMCKDVCEAMEYLES---NGFIHRDLAARNCLVGEQNV---VKVSDFGLARYVldde 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34098881 217 ---KPGKRFhdivgSAYYVAPEVLKR-RSGPESDVWSIGVITY-ILLCGRRPFWDRTEDGIFKEVLR 278
Cdd:cd05059 155 ytsSVGTKF-----PVKWSPPEVFMYsKFSSKSDVWSFGVLMWeVFSEGKMPYERFSNSEVVEHISQ 216
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
60-321 9.11e-16

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 77.95  E-value: 9.11e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVK--RLDKSKMVLPiavEDVKREVQILIALSGHENVVQF----HNAFEDD 133
Cdd:cd07837   1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVALKktRLEMEEEGVP---STALREVSLLQMLSQSIYIVRLldveHVEENGK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 134 DYVYIVMELCEGG--ELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQldSPLKATDFG 211
Cdd:cd07837  78 PLLYLVFEYLDTDlkKFIDSYGRGPHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQK--GLLKIADLG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 212 LSD-FIKPGKRF-HDIVgSAYYVAPEVL---KRRSGPeSDVWSIGVItYILLCGRRPFWDRTED-----GIFK------- 274
Cdd:cd07837 156 LGRaFTIPIKSYtHEIV-TLWYRAPEVLlgsTHYSTP-VDMWSVGCI-FAEMSRKQPLFPGDSElqqllHIFRllgtpne 232
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 275 EV------LRN-------KPDFSRKPWATISDSAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd07837 233 EVwpgvskLRDwheypqwKPQDLSRAVPDLEPEGVDLLTKMLAYDPAKRISAKAALQHPY 292
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
66-322 1.35e-15

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: 78.15  E-value: 1.35e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKskmvlPIAVED-VKREVQILIALS--GHENVVQFHNAF------EDDDYV 136
Cdd:cd07876  27 KPIGSGAQGIVCAAFDTVLGINVAVKKLSR-----PFQNQThAKRAYRELVLLKcvNHKNIISLLNVFtpqkslEEFQDV 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 137 YIVMELCEGG--ELLDRILSKKGNRYsekdaavVVRQMLkvAGECHLH--GLVHRDMKPENFLFKSaqlDSPLKATDFGL 212
Cdd:cd07876 102 YLVMELMDANlcQVIHMELDHERMSY-------LLYQML--CGIKHLHsaGIIHRDLKPSNIVVKS---DCTLKILDFGL 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 213 SDFIKPGKRFHDIVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCGRRPF--------WDRTEDGI----------F 273
Cdd:cd07876 170 ARTACTNFMMTPYVVTRYYRAPEVILGMGYKENvDIWSVGCIMGELVKGSVIFqgtdhidqWNKVIEQLgtpsaefmnrL 249
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34098881 274 KEVLRN----KPDFSR-------KPWATISDS---------AKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd07876 250 QPTVRNyvenRPQYPGisfeelfPDWIFPSESerdklktsqARDLLSKMLVIDPDKRISVDEALRHPYI 318
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
64-317 2.77e-15

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: 76.39  E-value: 2.77e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  64 IGKLLGHGQFGYTYVAIHRPNGDRVAVKRL-----DKSKMVLpiavedvkREVQILIALSGHENVVQFHNAF-----EDD 133
Cdd:cd14036   4 IKRVIAEGGFAFVYEAQDVGTGKEYALKRLlsneeEKNKAII--------QEINFMKKLSGHPNIVQFCSAAsigkeESD 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 134 ---DYVYIVMELCEGGeLLDRIlsKKGNRYSEKDAAVVVR---QMLKVAGecHLHG----LVHRDMKPENFLFKSaqlDS 203
Cdd:cd14036  76 qgqAEYLLLTELCKGQ-LVDFV--KKVEAPGPFSPDTVLKifyQTCRAVQ--HMHKqsppIIHRDLKIENLLIGN---QG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 204 PLKATDFGLSDFI--------KPGKRF---HDI--VGSAYYVAPEVLKRRS----GPESDVWSIGVITYiLLCGRR-PFw 265
Cdd:cd14036 148 QIKLCDFGSATTEahypdyswSAQKRSlveDEItrNTTPMYRTPEMIDLYSnypiGEKQDIWALGCILY-LLCFRKhPF- 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 34098881 266 drtEDGIFKEVLRNKpdFSRKPWATISDSAKDFVKKLLVKDPRARLTAAQAL 317
Cdd:cd14036 226 ---EDGAKLRIINAK--YTIPPNDTQYTVFHDLIRSTLKVNPEERLSITEIV 272
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
62-213 3.10e-15

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: 75.76  E-value: 3.10e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVK--RLDKSKMVLpiavedvKREVQILIALSGHENVVQFHNAFEDDDYVYIV 139
Cdd:cd14017   2 WKVVKKIGGGGFGEIYKVRDVVDGEEVAMKveSKSQPKQVL-------KMEVAVLKKLQGKPHFCRLIGCGRTERYNYIV 74
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34098881 140 MELCegGELLDRiLSKKGNR--YSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLF-KSAQLDSPLKATDFGLS 213
Cdd:cd14017  75 MTLL--GPNLAE-LRRSQPRgkFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIgRGPSDERTVYILDFGLA 148
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
54-319 3.33e-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: 76.97  E-value: 3.33e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  54 YSKDFHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLpiavEDVKREVQILIALSGHE-----NVVQFHN 128
Cdd:cd14226   7 NGEKWMDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNKKAFL----NQAQIEVRLLELMNKHDtenkyYIVRLKR 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 129 AFEDDDYVYIVMELCEGgELLDrILSKKGNRysekdaAVVVRQMLKVAGE--CHLHGL-------VHRDMKPENFLFKSA 199
Cdd:cd14226  83 HFMFRNHLCLVFELLSY-NLYD-LLRNTNFR------GVSLNLTRKFAQQlcTALLFLstpelsiIHCDLKPENILLCNP 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 200 QLdSPLKATDFGLSdfIKPGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGR----------------- 261
Cdd:cd14226 155 KR-SAIKIIDFGSS--CQLGQRIYQYIQSRFYRSPEVLLGLPyDLAIDMWSLGCILVEMHTGEplfsganevdqmnkive 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 262 ----------------RPFWDRTEDGIF-----KEVLRNKPDFSRK-------------------PWATISDSAK--DFV 299
Cdd:cd14226 232 vlgmppvhmldqapkaRKFFEKLPDGTYylkktKDGKKYKPPGSRKlheilgvetggpggrragePGHTVEDYLKfkDLI 311
                       330       340
                ....*....|....*....|
gi 34098881 300 KKLLVKDPRARLTAAQALSH 319
Cdd:cd14226 312 LRMLDYDPKTRITPAEALQH 331
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
62-323 3.36e-15

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: 76.74  E-value: 3.36e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEdVKREVQILIALSgHENVVQF--------HNAFEDd 133
Cdd:cd07859   2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINDVFEHVSDATR-ILREIKLLRLLR-HPDIVEIkhimlppsRREFKD- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 134 dyVYIVMELCEGGelLDRILsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLfksAQLDSPLKATDFGLS 213
Cdd:cd07859  79 --IYVVFELMESD--LHQVI-KANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNIL---ANADCKLKICDFGLA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 214 DFI---KPGKRF-HDIVGSAYYVAPEV---LKRRSGPESDVWSIGVITYILLCGRRPFWDR------------------- 267
Cdd:cd07859 151 RVAfndTPTAIFwTDYVATRWYRAPELcgsFFSKYTPAIDIWSIGCIFAEVLTGKPLFPGKnvvhqldlitdllgtpspe 230
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34098881 268 TEDGI-------FKEVLRNKP--DFSRKpWATISDSAKDFVKKLLVKDPRARLTAAQALSHAWVR 323
Cdd:cd07859 231 TISRVrnekarrYLSSMRKKQpvPFSQK-FPNADPLALRLLERLLAFDPKDRPTAEEALADPYFK 294
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
53-322 4.27e-15

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: 76.66  E-value: 4.27e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  53 GYSKDFHDH----YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVedvkREVQILIALSGHENVVQfHN 128
Cdd:cd14225  32 SYLKVLHDHiayrYEILEVIGKGSFGQVVKALDHKTNEHVAIKIIRNKKRFHHQAL----VEVKILDALRRKDRDNS-HN 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 129 AFEDDDYVYIVMELCEGGELLDRILSK--KGNRYSEKDAAVVVR---QMLKVAGECHLHGLVHRDMKPENFLFKSaQLDS 203
Cdd:cd14225 107 VIHMKEYFYFRNHLCITFELLGMNLYEliKKNNFQGFSLSLIRRfaiSLLQCLRLLYRERIIHCDLKPENILLRQ-RGQS 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 204 PLKATDFGLSDFIKpgKRFHDIVGSAYYVAPEV-LKRRSGPESDVWSIGVITYILLCG---------------------- 260
Cdd:cd14225 186 SIKVIDFGSSCYEH--QRVYTYIQSRFYRSPEViLGLPYSMAIDMWSLGCILAELYTGyplfpgeneveqlacimevlgl 263
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 261 -----------RRPFWDrtEDGIFKEVLRNKpdfSRKPWATISDSAK----------DFVKKLLVKDPRARLTAAQALSH 319
Cdd:cd14225 264 pppelienaqrRRLFFD--SKGNPRCITNSK---GKKRRPNSKDLASalktsdplflDFIRRCLEWDPSKRMTPDEALQH 338

                ...
gi 34098881 320 AWV 322
Cdd:cd14225 339 EWI 341
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
68-326 5.77e-15

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: 75.42  E-value: 5.77e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVK--RLDKSKMVLPIAVedvkREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd07873  10 LGEGTYATVYKGRSKLTDNLVALKeiRLEHEEGAPCTAI----REVSLLKDLK-HANIVTLHDIIHTEKSLTLVFEYLDK 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GelLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAqldSPLKATDFGLSDFIK-PGKRFHD 224
Cdd:cd07873  85 D--LKQYLDDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINER---GELKLADFGLARAKSiPTKTYSN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 225 IVGSAYYVAPEVL--KRRSGPESDVWSIGVITYILLCGRRPFWDRTEDG----IFK-----------EVLRN-------- 279
Cdd:cd07873 160 EVVTLWYRPPDILlgSTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEqlhfIFRilgtpteetwpGILSNeefksyny 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 34098881 280 ---KPDFSRKPWATISDSAKDFVKKLLVKDPRARLTAAQALSHAWVREGG 326
Cdd:cd07873 240 pkyRADALHNHAPRLDSDGADLLSKLLQFEGRKRISAEEAMKHPYFHSLG 289
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
54-320 7.12e-15

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: 75.06  E-value: 7.12e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  54 YSKDFHDHYTIGKllghGQFGYTYVAIHRPNGDRVAVKRlDKSKMVLPIAVEDVKREVQILIALSGHENVVQFHNAFEDD 133
Cdd:cd14138   3 YATEFHELEKIGS----GEFGSVFKCVKRLDGCIYAIKR-SKKPLAGSVDEQNALREVYAHAVLGQHSHVVRYYSAWAED 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 134 DYVYIVMELCEGGELLDRIlsKKGNR----YSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLdsPLKATD 209
Cdd:cd14138  78 DHMLIQNEYCNGGSLADAI--SENYRimsyFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISRTSI--PNAASE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 210 FGLSDFIKPGKRFHDI---------------VGSAYYVAPEVLKRRSG--PESDVWSIGvITYILLCGRRPF------WD 266
Cdd:cd14138 154 EGDEDEWASNKVIFKIgdlghvtrvsspqveEGDSRFLANEVLQENYThlPKADIFALA-LTVVCAAGAEPLptngdqWH 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 34098881 267 RTEDGIFKEVLRnkpdfsrkpwaTISDSAKDFVKKLLVKDPRARLTAAQALSHA 320
Cdd:cd14138 233 EIRQGKLPRIPQ-----------VLSQEFLDLLKVMIHPDPERRPSAVALVKHS 275
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
68-258 8.69e-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: 74.97  E-value: 8.69e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDR----VAVKRLDKSKMVLPIAveDVKREVQILIALSgHENVVQFHNAFEDD--DYVYIVME 141
Cdd:cd05079  12 LGEGHFGKVELCRYDPEGDNtgeqVAVKSLKPESGGNHIA--DLKKEIEILRNLY-HENIVKYKGICTEDggNGIKLIME 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELlDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLdspLKATDFGLSDFIKPGKR 221
Cdd:cd05079  89 FLPSGSL-KEYLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQ---VKIGDFGLTKAIETDKE 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 34098881 222 FH----DIVGSAYYVAPEVL-KRRSGPESDVWSIGVITYILL 258
Cdd:cd05079 165 YYtvkdDLDSPVFWYAPECLiQSKFYIASDVWSFGVTLYELL 206
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
63-274 8.73e-15

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: 74.38  E-value: 8.73e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  63 TIGKLLGHGQFGYTYVAI-HRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDyVYIVME 141
Cdd:cd05056   9 TLGRCIGEGQFGDVYQGVyMSPENEKIAVAVKTCKNCTSPSVREKFLQEAYIMRQFD-HPHIVKLIGVITENP-VWIVME 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELldRILSKKgNRYSEKDAAVVV--RQMLKVAGECHLHGLVHRDMKPENFLFKSAQLdspLKATDFGLSDFIKPG 219
Cdd:cd05056  87 LAPLGEL--RSYLQV-NKYSLDLASLILyaYQLSTALAYLESKRFVHRDIAARNVLVSSPDC---VKLGDFGLSRYMEDE 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 220 KRFHDIVGS--AYYVAPEVLK-RRSGPESDVWSIGVITY-ILLCGRRPF-WDRTEDGIFK 274
Cdd:cd05056 161 SYYKASKGKlpIKWMAPESINfRRFTSASDVWMFGVCMWeILMLGVKPFqGVKNNDVIGR 220
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
68-321 1.20e-14

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: 74.34  E-value: 1.20e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVK--RLDKSKMVLPIAVedvkREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd07844   8 LGEGSYATVYKGRSKLTGQLVALKeiRLEHEEGAPFTAI----REASLLKDLK-HANIVTLHDIIHTKKTLTLVFEYLDT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GelLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAqldSPLKATDFGLSDfIK--PGKRFH 223
Cdd:cd07844  83 D--LKQYMDDCGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISER---GELKLADFGLAR-AKsvPSKTYS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 224 DIVGSAYYVAPEVL--KRRSGPESDVWSIGVITYILLCGRRPFWDRTE-----DGIFK-----------EVLRNK----- 280
Cdd:cd07844 157 NEVVTLWYRPPDVLlgSTEYSTSLDMWGVGCIFYEMATGRPLFPGSTDvedqlHKIFRvlgtpteetwpGVSSNPefkpy 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 34098881 281 --PDFSRKP----WATISD--SAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd07844 237 sfPFYPPRPlinhAPRLDRipHGEELALKFLQYEPKKRISAAEAMKHPY 285
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
58-315 1.88e-14

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: 73.94  E-value: 1.88e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  58 FHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVK----REVQILIALSgHENVVQFHNAFE-D 132
Cdd:cd14040   4 LNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENYHkhacREYRIHKELD-HPRIVKLYDYFSlD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 133 DDYVYIVMELCEGGELlDRILsKKGNRYSEKDAAVVVRQM---LKVAGECHlHGLVHRDMKPENFLFKSAQLDSPLKATD 209
Cdd:cd14040  83 TDTFCTVLEYCEGNDL-DFYL-KQHKLMSEKEARSIVMQIvnaLRYLNEIK-PPIIHYDLKPGNILLVDGTACGEIKITD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 210 FGLSDFIKP---GKRFHDIV----GSAYYVAPEVLKRRSGP-----ESDVWSIGVITYILLCGRRPF-WDRTEDGIFKE- 275
Cdd:cd14040 160 FGLSKIMDDdsyGVDGMDLTsqgaGTYWYLPPECFVVGKEPpkisnKVDVWSVGVIFFQCLYGRKPFgHNQSQQDILQEn 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 34098881 276 -VLR-NKPDFSRKPwaTISDSAKDFVKKLLVKDPRARLTAAQ 315
Cdd:cd14040 240 tILKaTEVQFPVKP--VVSNEAKAFIRRCLAYRKEDRFDVHQ 279
pknD PRK13184
serine/threonine-protein kinase PknD;
61-317 2.17e-14

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 76.35  E-value: 2.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881   61 HYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVM 140
Cdd:PRK13184   3 RYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLI-HPGIVPVYSICSDGDPVYYTM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  141 ELCEGgELLDRIL-------SKKGNRYSEKDAAVVVRQMLKVageC------HLHGLVHRDMKPENFL------------ 195
Cdd:PRK13184  82 PYIEG-YTLKSLLksvwqkeSLSKELAEKTSVGAFLSIFHKI---CatieyvHSKGVLHRDLKPDNILlglfgevvildw 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  196 ----FKSA----QLDSPLKATDFGLSDFIKPGKrfhdIVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCGRRPFwd 266
Cdd:PRK13184 158 gaaiFKKLeeedLLDIDVDERNICYSSMTIPGK----IVGTPDYMAPERLLGVPASEStDIYALGVILYQMLTLSFPY-- 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 34098881  267 RTEDG---IFKEVLRNKPDFSrkPWATISDSAKDFVKKLLVKDPRARLTAAQAL 317
Cdd:PRK13184 232 RRKKGrkiSYRDVILSPIEVA--PYREIPPFLSQIAMKALAVDPAERYSSVQEL 283
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
68-339 2.30e-14

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: 73.87  E-value: 2.30e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVK--RLDKSKMVLPIAVedvkREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEg 145
Cdd:cd07872  14 LGEGTYATVFKGRSKLTENLVALKeiRLEHEEGAPCTAI----REVSLLKDLK-HANIVTLHDIVHTDKSLTLVFEYLD- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 gELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAqldSPLKATDFGLSDFIK-PGKRFHD 224
Cdd:cd07872  88 -KDLKQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINER---GELKLADFGLARAKSvPTKTYSN 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 225 IVGSAYYVAPEVLKRRS--GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLR----------------------NK 280
Cdd:cd07872 164 EVVTLWYRPPDVLLGSSeySTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFRllgtpteetwpgissndefknyNF 243
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34098881 281 PDFSRKPWAT----ISDSAKDFVKKLLVKDPRARLTAAQALSHAWVRE-GGNATDIPVDISVLN 339
Cdd:cd07872 244 PKYKPQPLINhaprLDTEGIELLTKFLQYESKKRISAEEAMKHAYFRSlGTRIHSLPESISIFS 307
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
66-264 3.24e-14

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: 72.32  E-value: 3.24e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRpNGDRVAVKRLDKSKMvlpiAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd05034   1 KKLGAGQFGEVWMGVWN-GTTKVAVKTLKPGTM----SPEAFLQEAQIMKKLR-HDKLVQLYAVCSDEEPIYIVTELMSK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRILSKKGNRYSEKDaavVVRQMLKVA-GECHL--HGLVHRDMKPENFLFkSAQLDspLKATDFGLSDFIKP---- 218
Cdd:cd05034  75 GSLLDYLRTGEGRALRLPQ---LIDMAAQIAsGMAYLesRNYIHRDLAARNILV-GENNV--CKVADFGLARLIEDdeyt 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 34098881 219 ---GKRFhdivgSAYYVAPE-VLKRRSGPESDVWSIGVITY-ILLCGRRPF 264
Cdd:cd05034 149 areGAKF-----PIKWTAPEaALYGRFTIKSDVWSFGILLYeIVTYGRVPY 194
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
66-264 3.44e-14

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: 72.82  E-value: 3.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRpNGDRVAVKRLDKSKMvlpiAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd05068  14 RKLGSGQFGEVWEGLWN-NTTPVAVKTLKPGTM----DPEDFLREAQIMKKLR-HPKLIQLYAVCTLEEPIYIITELMKH 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRILSKKGnrysekdaAVVVRQMLKVA-----GECHL--HGLVHRDMKPENFLFKSAQLdspLKATDFGLSDFIKP 218
Cdd:cd05068  88 GSLLEYLQGKGR--------SLQLPQLIDMAaqvasGMAYLesQNYIHRDLAARNVLVGENNI---CKVADFGLARVIKV 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 34098881 219 GKRFHDIVGSAY---YVAPE-VLKRRSGPESDVWSIGV-ITYILLCGRRPF 264
Cdd:cd05068 157 EDEYEAREGAKFpikWTAPEaANYNRFSIKSDVWSFGIlLTEIVTYGRIPY 207
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
68-255 3.53e-14

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: 72.48  E-value: 3.53e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKrldKSKMVLPiavEDVKR----EVQILIALSgHENVVQFHNAFEDDDYVYIVMELC 143
Cdd:cd05041   3 IGRGNFGDVYRGVLKPDNTEVAVK---TCRETLP---PDLKRkflqEARILKQYD-HPNIVKLIGVCVQKQPIMIVMELV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 144 EGGELLDrILSKKGNRYSekdaavvVRQMLKV-----AGECHLHG--LVHRDMKPENFLfksAQLDSPLKATDFGLSdfi 216
Cdd:cd05041  76 PGGSLLT-FLRKKGARLT-------VKQLLQMcldaaAGMEYLESknCIHRDLAARNCL---VGENNVLKISDFGMS--- 141
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 34098881 217 kpgKRFHDIVGSAY---------YVAPEVLKR-RSGPESDVWSIGVITY 255
Cdd:cd05041 142 ---REEEDGEYTVSdglkqipikWTAPEALNYgRYTSESDVWSFGILLW 187
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
68-265 3.54e-14

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: 72.88  E-value: 3.54e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHR---PNGDR--VAVKRLdkSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMEL 142
Cdd:cd05049  13 LGEGAFGKVFLGECYnlePEQDKmlVAVKTL--KDASSPDARKDFEREAELLTNLQ-HENIVKFYGVCTEGDPLLMVFEY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 143 CEGGELlDRILSKKGnryseKDAAVVVR-----------QMLKVA-----GECHLHGL--VHRDMKPENFLFKSAQLdsp 204
Cdd:cd05049  90 MEHGDL-NKFLRSHG-----PDAAFLASedsapgeltlsQLLHIAvqiasGMVYLASQhfVHRDLATRNCLVGTNLV--- 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34098881 205 LKATDFGLSdfikpgkrfHDIVGSAYY------------VAPE-VLKRRSGPESDVWSIGVITY-ILLCGRRPFW 265
Cdd:cd05049 161 VKIGDFGMS---------RDIYSTDYYrvgghtmlpirwMPPEsILYRKFTTESDVWSFGVVLWeIFTYGKQPWF 226
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
66-264 3.74e-14

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 72.75  E-value: 3.74e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNgDRVAVKRLDKSKMvlpiAVEDVKREVQILIALSgHENVVQFHnAFEDDDYVYIVMELCEG 145
Cdd:cd05073  17 KKLGAGQFGEVWMATYNKH-TKVAVKTMKPGSM----SVEAFLAEANVMKTLQ-HDKLVKLH-AVVTKEPIYIITEFMAK 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLdspLKATDFGLSDFI-------KP 218
Cdd:cd05073  90 GSLLDFLKSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLV---CKIADFGLARVIedneytaRE 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 34098881 219 GKRFhdivgSAYYVAPEVLKRRSGP-ESDVWSIGV-ITYILLCGRRPF 264
Cdd:cd05073 167 GAKF-----PIKWTAPEAINFGSFTiKSDVWSFGIlLMEIVTYGRIPY 209
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
85-317 4.92e-14

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: 75.27  E-value: 4.92e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881     85 GDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFE-DDDYVYIVMELCEGGELLDRiLSKKGnrysEK 163
Cdd:TIGR03903    3 GHEVAIKLLRTDAPEEEHQRARFRRETALCARLY-HPNIVALLDSGEaPPGLLFAVFEYVPGRTLREV-LAADG----AL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881    164 DAAVVVRQMLKV--AGEC-HLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLSDFIkPG---------KRFHDIVGSAYY 231
Cdd:TIGR03903   77 PAGETGRLMLQVldALACaHNQGIVHRDLKPQNIMVSQTGVRPHAKVLDFGIGTLL-PGvrdadvatlTRTTEVLGTPTY 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881    232 VAPEVLKRRS-GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLrNKPDFSRKPWATiSDSAKDFVKKLLVKDPRAR 310
Cdd:TIGR03903  156 CAPEQLRGEPvTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQL-SPVDVSLPPWIA-GHPLGQVLRKALNKDPRQR 233

                   ....*..
gi 34098881    311 LTAAQAL 317
Cdd:TIGR03903  234 AASAPAL 240
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
64-264 5.16e-14

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: 72.45  E-value: 5.16e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  64 IGKLLGHGQFGYTYVAIHRPNGDR----VAVKRLDKSKMvlPIAVEDVKREVQIlIALSGHENVVQFHnAFEDDDYVYIV 139
Cdd:cd05057  11 KGKVLGSGAFGTVYKGVWIPEGEKvkipVAIKVLREETG--PKANEEILDEAYV-MASVDHPHLVRLL-GICLSSQVQLI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGELLDRILSKKGNRYSeKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLdspLKATDFGLSDFIKPG 219
Cdd:cd05057  87 TQLMPLGCLLDYVRNHRDNIGS-QLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNH---VKITDFGLAKLLDVD 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 34098881 220 KRFHDIVGSAY---YVAPE-VLKRRSGPESDVWSIGVITYILLC-GRRPF 264
Cdd:cd05057 163 EKEYHAEGGKVpikWMALEsIQYRIYTHKSDVWSYGVTVWELMTfGAKPY 212
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
59-279 6.38e-14

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: 71.70  E-value: 6.38e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  59 HDHYTIGKLLGHGQFGYTYVAIHRpNGDRVAVKRLdKSKMVLpiAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYI 138
Cdd:cd05148   5 REEFTLERKLGSGYFGEVWEGLWK-NRVRVAIKIL-KSDDLL--KQQDFQKEVQALKRLR-HKHLISLFAVCSVGEPVYI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 139 VMELCEGGELLDRILSKKGNrysEKDAAVVVRQMLKVA-GECHL--HGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDF 215
Cdd:cd05148  80 ITELMEKGSLLAFLRSPEGQ---VLPVASLIDMACQVAeGMAYLeeQNSIHRDLAARNILVGE---DLVCKVADFGLARL 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34098881 216 IK-PGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITY-ILLCGRRPFWDRTEDGIFKEVLRN 279
Cdd:cd05148 154 IKeDVYLSSDKKIPYKWTAPEAASHGTfSTKSDVWSFGILLYeMFTYGQVPYPGMNNHEVYDQITAG 220
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
68-328 6.60e-14

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 72.22  E-value: 6.60e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLdkskmVLPIAVE---DVKREVQILIALSGhENVVQFHNAFEDDDYVYIVMELCE 144
Cdd:cd06619   9 LGHGNGGTVYKAYHLLTRRILAVKVI-----PLDITVElqkQIMSELEILYKCDS-PYIIGFYGAFFVENRISICTEFMD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 145 GGELldrilskkgNRYSEKDAAVVVRQMLKVA-GECHLHGL--VHRDMKPENFLFKSAqldSPLKATDFGLSDFI--KPG 219
Cdd:cd06619  83 GGSL---------DVYRKIPEHVLGRIAVAVVkGLTYLWSLkiLHRDVKPSNMLVNTR---GQVKLCDFGVSTQLvnSIA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 220 KRFhdiVGSAYYVAPE-VLKRRSGPESDVWSIGVITYILLCGRRPFWDrtedgIFKEVLRNKP----------DFSRKPW 288
Cdd:cd06619 151 KTY---VGTNAYMAPErISGEQYGIHSDVWSLGISFMELALGRFPYPQ-----IQKNQGSLMPlqllqcivdeDPPVLPV 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 34098881 289 ATISDSAKDFVKKLLVKDPRARLTAAQALSHAWVRE--GGNA 328
Cdd:cd06619 223 GQFSEKFVHFITQCMRKQPKERPAPENLMDHPFIVQynDGNA 264
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
66-278 7.32e-14

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: 72.00  E-value: 7.32e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRpNGDRVAVKRLDKSKMvlpiAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd05072  13 KKLGAGQFGEVWMGYYN-NSTKVAVKTLKPGTM----SVQAFLEEANLMKTLQ-HDKLVRLYAVVTKEEPIYIITEYMAK 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLdspLKATDFGLSDFI-------KP 218
Cdd:cd05072  87 GSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLM---CKIADFGLARVIedneytaRE 163
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34098881 219 GKRFhdivgSAYYVAPEVLKRRSGP-ESDVWSIGVITY-ILLCGRRPFWDRTEDGIFKEVLR 278
Cdd:cd05072 164 GAKF-----PIKWTAPEAINFGSFTiKSDVWSFGILLYeIVTYGKIPYPGMSNSDVMSALQR 220
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
63-285 8.45e-14

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: 71.63  E-value: 8.45e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  63 TIGKLLGHGQFGYTYVAihRPNGDrVAVKRLDKSKMVlPIAVEDVKREVQILIAlSGHENVVQFHnAFEDDDYVYIVMEL 142
Cdd:cd14151  11 TVGQRIGSGSFGTVYKG--KWHGD-VAVKMLNVTAPT-PQQLQAFKNEVGVLRK-TRHVNILLFM-GYSTKPQLAIVTQW 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 143 CEGGELLDRiLSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDfIKP---- 218
Cdd:cd14151  85 CEGSSLYHH-LHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHE---DLTVKIGDFGLAT-VKSrwsg 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34098881 219 GKRFHDIVGSAYYVAPEVLK-RRSGP---ESDVWSIGVITYILLCGRRPFWD-RTEDGIFKEVLRN--KPDFSR 285
Cdd:cd14151 160 SHQFEQLSGSILWMAPEVIRmQDKNPysfQSDVYAFGIVLYELMTGQLPYSNiNNRDQIIFMVGRGylSPDLSK 233
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
68-265 1.16e-13

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: 71.54  E-value: 1.16e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVA-IHR--PNGDR--VAVKRLdksKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMEL 142
Cdd:cd05092  13 LGEGAFGKVFLAeCHNllPEQDKmlVAVKAL---KEATESARQDFQREAELLTVLQ-HQHIVRFYGVCTEGEPLIMVFEY 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 143 CEGGELlDRILSKKG-------NRYSEKDAAVVVRQMLKVA-----GECHLHGL--VHRDMKPENFLFKSaqlDSPLKAT 208
Cdd:cd05092  89 MRHGDL-NRFLRSHGpdakildGGEGQAPGQLTLGQMLQIAsqiasGMVYLASLhfVHRDLATRNCLVGQ---GLVVKIG 164
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34098881 209 DFGLSdfikpgkrfHDIVGSAYY------------VAPE-VLKRRSGPESDVWSIGVITY-ILLCGRRPFW 265
Cdd:cd05092 165 DFGMS---------RDIYSTDYYrvggrtmlpirwMPPEsILYRKFTTESDIWSFGVVLWeIFTYGKQPWY 226
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
35-322 1.18e-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: 72.47  E-value: 1.18e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  35 ASTKRRTGSIpcGKRTDFGYSKD-------FHDH----YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIA 103
Cdd:cd14224  31 PNAKKRQGVI--GGPNNGGYDDEqgsyihvPHDHiayrYEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVRNEKRFHRQA 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 104 VEdvkrEVQILIALSGHE-----NVVQFHNAFEDDDYVYIVMELCEGgELLDRILSKKGNRYSEKDAAVVVRQMLKVAGE 178
Cdd:cd14224 109 AE----EIRILEHLKKQDkdntmNVIHMLESFTFRNHICMTFELLSM-NLYELIKKNKFQGFSLQLVRKFAHSILQCLDA 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 179 CHLHGLVHRDMKPENFLFKSaQLDSPLKATDFGLSDFIKpgKRFHDIVGSAYYVAPEV-LKRRSGPESDVWSIGVITYIL 257
Cdd:cd14224 184 LHRNKIIHCDLKPENILLKQ-QGRSGIKVIDFGSSCYEH--QRIYTYIQSRFYRAPEViLGARYGMPIDMWSFGCILAEL 260
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 258 LCGRRPFWDRTED---GIFKEVL-----------------------------RNKPDFS------------------RKP 287
Cdd:cd14224 261 LTGYPLFPGEDEGdqlACMIELLgmppqklletskraknfisskgypryctvTTLPDGSvvlnggrsrrgkmrgppgSKD 340
                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 34098881 288 WATISDSAKD-----FVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14224 341 WVTALKGCDDplfldFLKRCLEWDPAARMTPSQALRHPWL 380
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
66-264 1.22e-13

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: 71.21  E-value: 1.22e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRpnGDRVAVK--RLDKSKMVlPIAVEDVKREVQiLIALSGHENVVQFHNAFEDDDYVYIVMELC 143
Cdd:cd14147   9 EVIGIGGFGKVYRGSWR--GELVAVKaaRQDPDEDI-SVTAESVRQEAR-LFAMLAHPNIIALKAVCLEEPNLCLVMEYA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 144 EGGELlDRILSkkGNRYSEKdaaVVVRQMLKVA-GECHLHG-----LVHRDMKPENFLF-----KSAQLDSPLKATDFGL 212
Cdd:cd14147  85 AGGPL-SRALA--GRRVPPH---VLVNWAVQIArGMHYLHCealvpVIHRDLKSNNILLlqpieNDDMEHKTLKITDFGL 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 34098881 213 SdfikpgKRFHDIV-----GSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPF 264
Cdd:cd14147 159 A------REWHKTTqmsaaGTYAWMAPEVIKASTfSKGSDVWSFGVLLWELLTGEVPY 210
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
60-311 1.23e-13

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


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 72.02  E-value: 1.23e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAvEDVKREVQILIALSGHEN---VVQFHNAFEDDDYV 136
Cdd:cd05633   5 NDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQG-ETLALNERIMLSLVSTGDcpfIVCMTYAFHTPDKL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 137 YIVMELCEGGELlDRILSKKGnRYSEKDAAVVVRQMlkVAGECHLHG--LVHRDMKPENFLFKSaqlDSPLKATDFGLS- 213
Cdd:cd05633  84 CFILDLMNGGDL-HYHLSQHG-VFSEKEMRFYATEI--ILGLEHMHNrfVVYRDLKPANILLDE---HGHVRISDLGLAc 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 214 DFIKpgKRFHDIVGSAYYVAPEVLKRRSGPES--DVWSIGVITYILLCGRRPFWD-RTEDGifKEVLRNKPDFSRKPWAT 290
Cdd:cd05633 157 DFSK--KKPHASVGTHGYMAPEVLQKGTAYDSsaDWFSLGCMLFKLLRGHSPFRQhKTKDK--HEIDRMTLTVNVELPDS 232
                       250       260
                ....*....|....*....|.
gi 34098881 291 ISDSAKDFVKKLLVKDPRARL 311
Cdd:cd05633 233 FSPELKSLLEGLLQRDVSKRL 253
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
68-270 1.48e-13

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: 70.60  E-value: 1.48e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLdkskmVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEGGE 147
Cdd:cd14065   1 LGKGFFGEVYKVTHRETGKVMVMKEL-----KRFDEQRSFLKEVKLMRRLS-HPNILRFIGVCVKDNKLNFITEYVNGGT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 148 LlDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLSDFI------KPG-K 220
Cdd:cd14065  75 L-EELLKSMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRNAVVADFGLAREMpdektkKPDrK 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 34098881 221 RFHDIVGSAYYVAPEVLKRRSGPE-SDVWSIGvityILLC---GRRP----FWDRTED 270
Cdd:cd14065 154 KRLTVVGSPYWMAPEMLRGESYDEkVDVFSFG----IVLCeiiGRVPadpdYLPRTMD 207
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
66-322 1.51e-13

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: 72.04  E-value: 1.51e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAvEDVKREVqILIALSGHENVVQFHNAF------EDDDYVYIV 139
Cdd:cd07874  23 KPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHA-KRAYREL-VLMKCVNHKNIISLLNVFtpqkslEEFQDVYLV 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGelLDRILSKKgnrYSEKDAAVVVRQMLkvAGECHLH--GLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIK 217
Cdd:cd07874 101 MELMDAN--LCQVIQME---LDHERMSYLLYQML--CGIKHLHsaGIIHRDLKPSNIVVKS---DCTLKILDFGLARTAG 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 218 PGKRFHDIVGSAYYVAPEVLKRRSGPES-DVWSIGVIT------YILLCGRRPF--WDRTEDGI--------------FK 274
Cdd:cd07874 171 TSFMMTPYVVTRYYRAPEVILGMGYKENvDIWSVGCIMgemvrhKILFPGRDYIdqWNKVIEQLgtpcpefmkklqptVR 250
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34098881 275 EVLRNKPDFSRKPWATI----------------SDSAKDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd07874 251 NYVENRPKYAGLTFPKLfpdslfpadsehnklkASQARDLLSKMLVIDPAKRISVDEALQHPYI 314
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
62-321 1.63e-13

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: 71.55  E-value: 1.63e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPN--GDRVAVKRLDKSKM----VLPIAVedvkREVQILIALSgHENVVQFHNAF--EDD 133
Cdd:cd07842   2 YEIEGCIGRGTYGRVYKAKRKNGkdGKEYAIKKFKGDKEqytgISQSAC----REIALLRELK-HENVVSLVEVFleHAD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 134 DYVYIVMELCEGgELLDRIlskkgNRYSEKDAAVVVRQMLKVAGECHLHGL--------VHRDMKPENFLFKSAQLDS-P 204
Cdd:cd07842  77 KSVYLLFDYAEH-DLWQII-----KFHRQAKRVSIPPSMVKSLLWQILNGIhylhsnwvLHRDLKPANILVMGEGPERgV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 205 LKATDFGLSD-FIKPGKRFHD---IVGSAYYVAPEVL--KRRSGPESDVWSIGVITYILLCGRRPFWDRTED-------- 270
Cdd:cd07842 151 VKIGDLGLARlFNAPLKPLADldpVVVTIWYRAPELLlgARHYTKAIDIWAIGCIFAELLTLEPIFKGREAKikksnpfq 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 271 -----GIFK-----------------EVLRNKPDFSRKP------------WATISDSAKDFVKKLLVKDPRARLTAAQA 316
Cdd:cd07842 231 rdqleRIFEvlgtptekdwpdikkmpEYDTLKSDTKASTypnsllakwmhkHKKPDSQGFDLLRKLLEYDPTKRITAEEA 310

                ....*
gi 34098881 317 LSHAW 321
Cdd:cd07842 311 LEHPY 315
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
68-319 1.72e-13

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: 70.22  E-value: 1.72e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRpnGDRVAVKRLDKSKMVlpiaveDVK--REVQilialsgHENVVQFHNAFEDDDYVYIVMELCEG 145
Cdd:cd14059   1 LGSGAQGAVFLGKFR--GEEVAVKKVRDEKET------DIKhlRKLN-------HPNIIKFKGVCTQAPCYCILMEYCPY 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKPGKRFHDI 225
Cdd:cd14059  66 GQLYEVL--RAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTY---NDVLKISDFGTSKELSEKSTKMSF 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 226 VGSAYYVAPEVLkrRSGPES---DVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRNK-----PDfsrkpwaTISDSAKD 297
Cdd:cd14059 141 AGTVAWMAPEVI--RNEPCSekvDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVGSNSlqlpvPS-------TCPDGFKL 211
                       250       260
                ....*....|....*....|..
gi 34098881 298 FVKKLLVKDPRARLTAAQALSH 319
Cdd:cd14059 212 LMKQCWNSKPRNRPSFRQILMH 233
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
66-278 2.75e-13

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: 70.14  E-value: 2.75e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTY----VAIHRPNGD--RVAVKRLDKSkmvlpiAVEDVKREV---QILIALSGHENVVQFHNAFEDDDYV 136
Cdd:cd05044   1 KFLGSGAFGEVFegtaKDILGDGSGetKVAVKTLRKG------ATDQEKAEFlkeAHLMSNFKHPNILKLLGVCLDNDPQ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 137 YIVMELCEGGELLDRI-LSKKGNRYSEKDAAVVVRQM-LKVAGECH----LHgLVHRDMKPENFLFKSAQLDS-PLKATD 209
Cdd:cd05044  75 YIILELMEGGDLLSYLrAARPTAFTPPLLTLKDLLSIcVDVAKGCVyledMH-FVHRDLAARNCLVSSKDYRErVVKIGD 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 210 FGLSdfikpgkrfHDIVGSAYY------------VAPEVLKrrSG---PESDVWSIGVITY-ILLCGRRPFWDRTEdgif 273
Cdd:cd05044 154 FGLA---------RDIYKNDYYrkegegllpvrwMAPESLV--DGvftTQSDVWAFGVLMWeILTLGQQPYPARNN---- 218

                ....*
gi 34098881 274 KEVLR 278
Cdd:cd05044 219 LEVLH 223
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
107-311 2.78e-13

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 70.91  E-value: 2.78e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 107 VKREVQILIALSGHENVVQFHNAFEDDDYVYIVMELCEGGELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVH 186
Cdd:cd05588  42 VQTEKHVFETASNHPFLVGLHSCFQTESRLFFVIEFVNGGDLMFHM--QRQRRLPEEHARFYSAEISLALNFLHEKGIIY 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 187 RDMKPENFLFKSaqlDSPLKATDFGL-SDFIKPGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPF 264
Cdd:cd05588 120 RDLKLDNVLLDS---EGHIKLTDYGMcKEGLRPGDTTSTFCGTPNYIAPEILRGEDyGFSVDWWALGVLMFEMLAGRSPF 196
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 34098881 265 ---------WDRTEDGIFKEVLRNKPDFSRkpwaTISDSAKDFVKKLLVKDPRARL 311
Cdd:cd05588 197 divgssdnpDQNTEDYLFQVILEKPIRIPR----SLSVKAASVLKGFLNKNPAERL 248
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
58-321 3.70e-13

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: 70.30  E-value: 3.70e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  58 FHDHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKrLDKSKMVLPIAVEDvkrEVQILIALS-------GHENVVQFHNAF 130
Cdd:cd14136   8 YNGRYHVVRKLGWGHFSTVWLCWDLQNKRFVALK-VVKSAQHYTEAALD---EIKLLKCVReadpkdpGREHVVQLLDDF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 131 E----DDDYVYIVMELCeGGELLDRIlskkgNRYSEKDAAV-----VVRQMLKvaGECHLH---GLVHRDMKPENFLFKS 198
Cdd:cd14136  84 KhtgpNGTHVCMVFEVL-GPNLLKLI-----KRYNYRGIPLplvkkIARQVLQ--GLDYLHtkcGIIHTDIKPENVLLCI 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 199 AQLDSplKATDFGLSDFIKpgKRFHDIVGSAYYVAPEV-LKRRSGPESDVWSIGVITYILLCGRRPF-------WDRTED 270
Cdd:cd14136 156 SKIEV--KIADLGNACWTD--KHFTEDIQTRQYRSPEViLGAGYGTPADIWSTACMAFELATGDYLFdphsgedYSRDED 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 271 GI-----------------------------------------FKEVLRNKPDFSRKPWATISdsakDFVKKLLVKDPRA 309
Cdd:cd14136 232 HLaliiellgriprsiilsgkysreffnrkgelrhisklkpwpLEDVLVEKYKWSKEEAKEFA----SFLLPMLEYDPEK 307
                       330
                ....*....|..
gi 34098881 310 RLTAAQALSHAW 321
Cdd:cd14136 308 RATAAQCLQHPW 319
PTZ00183 PTZ00183
centrin; Provisional
362-509 3.74e-13

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 67.02  E-value: 3.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  362 LDEAEISDLRDQFDAIDVDKNGVISLEEMRQALaKDLPWKLKDSRVAEILEAIDSNTDGLVDFTEFVAAAlhVHQLEEHD 441
Cdd:PTZ00183  11 LTEDQKKEIREAFDLFDTDGSGTIDPKELKVAM-RSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDIM--TKKLGERD 87
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34098881  442 SEKWQLRsraAFEKFDLDKDGYITPEEL-RMHTGLRGSID-----PLLDEADIDRDGKISLHEFRRLLRTASIS 509
Cdd:PTZ00183  88 PREEILK---AFRLFDDDKTGKISLKNLkRVAKELGETITdeelqEMIDEADRNGDGEISEEEFYRIMKKTNLF 158
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
61-258 3.89e-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: 70.04  E-value: 3.89e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRP----NGDRVAVKRLDKSKMVlpiAVEDVKREVQILIALSgHENVVQF----HNAFED 132
Cdd:cd14205   5 HLKFLQQLGKGNFGSVEMCRYDPlqdnTGEVVAVKKLQHSTEE---HLRDFEREIEILKSLQ-HDNIVKYkgvcYSAGRR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 133 DdyVYIVMELCEGGELLDrILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGL 212
Cdd:cd14205  81 N--LRLIMEYLPYGSLRD-YLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVEN---ENRVKIGDFGL 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 34098881 213 SDFIKPGKRFHDIV----GSAYYVAPEVL-KRRSGPESDVWSIGVITYILL 258
Cdd:cd14205 155 TKVLPQDKEYYKVKepgeSPIFWYAPESLtESKFSVASDVWSFGVVLYELF 205
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
68-263 4.20e-13

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: 70.46  E-value: 4.20e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSkmVLPIAVEDVKREVQILialsgHE----NVVQFHNAFEDDDYVYIVMELC 143
Cdd:cd06649  13 LGAGNGGVVTKVQHKPSGLIMARKLIHLE--IKPAIRNQIIRELQVL-----HEcnspYIVGFYGAFYSDGEISICMEHM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 144 EGGELlDRILsKKGNRYSEKDAAVVVRQMLKvaGECHL---HGLVHRDMKPENFLFKSAqldSPLKATDFGLSDFIKPGK 220
Cdd:cd06649  86 DGGSL-DQVL-KEAKRIPEEILGKVSIAVLR--GLAYLrekHQIMHRDVKPSNILVNSR---GEIKLCDFGVSGQLIDSM 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 34098881 221 RfHDIVGSAYYVAPEVLK-RRSGPESDVWSIGVITYILLCGRRP 263
Cdd:cd06649 159 A-NSFVGTRSYMSPERLQgTHYSVQSDIWSMGLSLVELAIGRYP 201
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
63-276 7.01e-13

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: 68.94  E-value: 7.01e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  63 TIGKLLGHGQFGYTYVAIHRPNGDR---VAVKRL-----DKSKMvlpiaveDVKREVQILIALSgHENVVQFHNAFEDDD 134
Cdd:cd05033   7 TIEKVIGGGEFGEVCSGSLKLPGKKeidVAIKTLksgysDKQRL-------DFLTEASIMGQFD-HPNVIRLEGVVTKSR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 135 YVYIVMELCEGGELlDRILSkkgnrysEKDAAVVVRQMLKV-----AGECHL--HGLVHRDMKPENFLfksaqLDSPL-- 205
Cdd:cd05033  79 PVMIVTEYMENGSL-DKFLR-------ENDGKFTVTQLVGMlrgiaSGMKYLseMNYVHRDLAARNIL-----VNSDLvc 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34098881 206 KATDFGLSDFIKPGKRFHDIVG---SAYYVAPEVLK-RRSGPESDVWSIGVITY-ILLCGRRPFWDRTEDGIFKEV 276
Cdd:cd05033 146 KVSDFGLSRRLEDSEATYTTKGgkiPIRWTAPEAIAyRKFTSASDVWSFGIVMWeVMSYGERPYWDMSNQDVIKAV 221
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
68-321 8.46e-13

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: 68.84  E-value: 8.46e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVK--RLDKSKMVLPIAVedvKREVQILIALSG--HENVVQFHNA-------------- 129
Cdd:cd07863   8 IGVGAYGTVYKARDPHSGHFVALKsvRVQTNEDGLPLST---VREVALLKRLEAfdHPNIVRLMDVcatsrtdretkvtl 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 130 -FE--DDDYVYIVMELCEGGELLDRIlskkgnryseKDaavVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAqldSPLK 206
Cdd:cd07863  85 vFEhvDQDLRTYLDKVPPPGLPAETI----------KD---LMRQFLRGLDFLHANCIVHRDLKPENILVTSG---GQVK 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 207 ATDFGLSDFIKPGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVItYILLCGRRPFW------DR-----------T 268
Cdd:cd07863 149 LADFGLARIYSCQMALTPVVVTLWYRAPEVLLQSTyATPVDMWSVGCI-FAEMFRRKPLFcgnseaDQlgkifdliglpP 227
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 269 EDGIFKEVLRNKPDFS-RKPWAT------ISDSAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd07863 228 EDDWPRDVTLPRGAFSpRGPRPVqsvvpeIEESGAQLLLEMLTFNPHKRISAFRALQHPF 287
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
68-272 8.87e-13

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: 68.68  E-value: 8.87e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIhRPNGDRVAVKRLDKSKmvlPIAVE-DVKREVQILiALSGHENVVQFHNAFEDDDYVYIVMELCEGG 146
Cdd:cd14664   1 IGRGGAGTVYKGV-MPNGTLVAVKRLKGEG---TQGGDhGFQAEIQTL-GMIRHRNIVRLRGYCSNPTTNLLVYEYMPNG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 147 ELlDRILSKKGNRYSEKDAAVVVRQMLKVA-GECHLHG-----LVHRDMKPENFLfksaqLDSPLKA--TDFGLSDFIKP 218
Cdd:cd14664  76 SL-GELLHSRPESQPPLDWETRQRIALGSArGLAYLHHdcsplIIHRDVKSNNIL-----LDEEFEAhvADFGLAKLMDD 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 34098881 219 GKR--FHDIVGSAYYVAPEVLKR-RSGPESDVWSIGVITYILLCGRRPF-WDRTEDGI 272
Cdd:cd14664 150 KDShvMSSVAGSYGYIAPEYAYTgKVSEKSDVYSYGVVLLELITGKRPFdEAFLDDGV 207
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
109-322 9.94e-13

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: 69.69  E-value: 9.94e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 109 REVqILIALSGHENVVQFHNAF------EDDDYVYIVMELCEGGelLDRILSKKgnrYSEKDAAVVVRQMLkvAGECHLH 182
Cdd:cd07875  72 REL-VLMKCVNHKNIIGLLNVFtpqkslEEFQDVYIVMELMDAN--LCQVIQME---LDHERMSYLLYQML--CGIKHLH 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 183 --GLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKPGKRFHDIVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLC 259
Cdd:cd07875 144 saGIIHRDLKPSNIVVKS---DCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENvDIWSVGCIMGEMIK 220
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 260 GRRPF--------WDRTEDGI--------------FKEVLRNKPDFSRKPWATI----------------SDSAKDFVKK 301
Cdd:cd07875 221 GGVLFpgtdhidqWNKVIEQLgtpcpefmkklqptVRTYVENRPKYAGYSFEKLfpdvlfpadsehnklkASQARDLLSK 300
                       250       260
                ....*....|....*....|.
gi 34098881 302 LLVKDPRARLTAAQALSHAWV 322
Cdd:cd07875 301 MLVIDASKRISVDEALQHPYI 321
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
61-276 1.37e-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: 68.08  E-value: 1.37e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDR---VAVKRL-----DKSKmvlpiavEDVKREVQILIALSgHENVVQFHNAFED 132
Cdd:cd05063   6 HITKQKVIGAGEFGEVFRGILKMPGRKevaVAIKTLkpgytEKQR-------QDFLSEASIMGQFS-HHNIIRLEGVVTK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 133 DDYVYIVMELCEGGELlDRILSKKGNRYSEKDAAVVVRQMlkVAGECHLHGL--VHRDMKPENFLFKSaQLDSplKATDF 210
Cdd:cd05063  78 FKPAMIITEYMENGAL-DKYLRDHDGEFSSYQLVGMLRGI--AAGMKYLSDMnyVHRDLAARNILVNS-NLEC--KVSDF 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34098881 211 GLSDFIK--PGKRFHDIVGSA--YYVAPEVLK-RRSGPESDVWSIGVITY-ILLCGRRPFWDRTEDGIFKEV 276
Cdd:cd05063 152 GLSRVLEddPEGTYTTSGGKIpiRWTAPEAIAyRKFTSASDVWSFGIVMWeVMSFGERPYWDMSNHEVMKAI 223
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
68-312 1.43e-12

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: 67.91  E-value: 1.43e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGdRVAVKRLDKSKMVLPIAvEDVKREVQILIALSgHENVVQFHNA-FEDDDYVyIVMELCEGG 146
Cdd:cd14027   1 LDSGGFGKVSLCFHRTQG-LVVLKTVYTGPNCIEHN-EALLEEGKMMNRLR-HSRVVKLLGViLEEGKYS-LVMEYMEKG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 147 ELLdRILSKKGNRYSEKDaavvvRQMLKV-AGECHLH--GLVHRDMKPENFLFKSaqlDSPLKATDFGLSDF-------I 216
Cdd:cd14027  77 NLM-HVLKKVSVPLSVKG-----RIILEIiEGMAYLHgkGVIHKDLKPENILVDN---DFHIKIADLGLASFkmwskltK 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 217 KPGKRFHDIVGSA-------YYVAPEVLKR---RSGPESDVWSIGVITYILLCGRRPFWD-RTEDGIFKEVLR-NKPDFS 284
Cdd:cd14027 148 EEHNEQREVDGTAkknagtlYYMAPEHLNDvnaKPTEKSDVYSFAIVLWAIFANKEPYENaINEDQIIMCIKSgNRPDVD 227
                       250       260
                ....*....|....*....|....*...
gi 34098881 285 RKPWATISDsAKDFVKKLLVKDPRARLT 312
Cdd:cd14027 228 DITEYCPRE-IIDLMKLCWEANPEARPT 254
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
64-285 2.41e-12

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: 67.34  E-value: 2.41e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  64 IGKLLGHGQFGYTYVAihRPNGDrVAVKRLDKSKMVLPiAVEDVKREVqILIALSGHENVVQFHNAFEDDDYVYIVMELC 143
Cdd:cd14153   4 IGELIGKGRFGQVYHG--RWHGE-VAIRLIDIERDNEE-QLKAFKREV-MAYRQTRHENVVLFMGACMSPPHLAIITSLC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 144 EGGELLDRIlskkgnryseKDAAVVV---------RQMLKVAGECHLHGLVHRDMKPENFLFKSAQldspLKATDFGL-- 212
Cdd:cd14153  79 KGRTLYSVV----------RDAKVVLdvnktrqiaQEIVKGMGYLHAKGILHKDLKSKNVFYDNGK----VVITDFGLft 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 213 -SDFIKPGKRFHDI---VGSAYYVAPEVLKRRSgPE-----------SDVWSIGVITYILLCGRRPFWDRTEDGIFKEVL 277
Cdd:cd14153 145 iSGVLQAGRREDKLriqSGWLCHLAPEIIRQLS-PEteedklpfskhSDVFAFGTIWYELHAREWPFKTQPAEAIIWQVG 223

                ....*....
gi 34098881 278 RN-KPDFSR 285
Cdd:cd14153 224 SGmKPNLSQ 232
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
62-311 2.63e-12

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 67.77  E-value: 2.63e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAvEDVKREVQILIALSGHEN---VVQFHNAFEDDDYVYI 138
Cdd:cd14223   2 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQG-ETLALNERIMLSLVSTGDcpfIVCMSYAFHTPDKLSF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 139 VMELCEGGELlDRILSKKGnRYSEKDAAVVVRQMlkVAGECHLHG--LVHRDMKPENFLFKSaqlDSPLKATDFGLS-DF 215
Cdd:cd14223  81 ILDLMNGGDL-HYHLSQHG-VFSEAEMRFYAAEI--ILGLEHMHSrfVVYRDLKPANILLDE---FGHVRISDLGLAcDF 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 216 IKpgKRFHDIVGSAYYVAPEVLKRRSGPES--DVWSIGVITYILLCGRRPFWD-RTEDGifKEVLRNKPDFSRKPWATIS 292
Cdd:cd14223 154 SK--KKPHASVGTHGYMAPEVLQKGVAYDSsaDWFSLGCMLFKLLRGHSPFRQhKTKDK--HEIDRMTLTMAVELPDSFS 229
                       250
                ....*....|....*....
gi 34098881 293 DSAKDFVKKLLVKDPRARL 311
Cdd:cd14223 230 PELRSLLEGLLQRDVNRRL 248
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
62-318 3.36e-12

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 68.52  E-value: 3.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881   62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLdkskmvlpiaVEDVK---REVQILIALSgHENVVQFHNAF-------- 130
Cdd:PTZ00036  68 YKLGNIIGNGSFGVVYEAICIDTSEKVAIKKV----------LQDPQyknRELLIMKNLN-HINIIFLKDYYytecfkkn 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  131 EDDDYVYIVMelceggELLDRILSKKGNRYSEKDAAV---VVR----QMLKVAGECHLHGLVHRDMKPENFLFKSAQldS 203
Cdd:PTZ00036 137 EKNIFLNVVM------EFIPQTVHKYMKHYARNNHALplfLVKlysyQLCRALAYIHSKFICHRDLKPQNLLIDPNT--H 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  204 PLKATDFGLSDFIKPGKRFHDIVGSAYYVAPEVLKRRSGPES--DVWSIGVITYILLCGRRPFWDR-------------- 267
Cdd:PTZ00036 209 TLKLCDFGSAKNLLAGQRSVSYICSRFYRAPELMLGATNYTThiDLWSLGCIIAEMILGYPIFSGQssvdqlvriiqvlg 288
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34098881  268 --TEDGIfKEVLRNK-----PDFSRK------PWATiSDSAKDFVKKLLVKDPRARLTAAQALS 318
Cdd:PTZ00036 289 tpTEDQL-KEMNPNYadikfPDVKPKdlkkvfPKGT-PDDAINFISQFLKYEPLKRLNPIEALA 350
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
68-319 3.44e-12

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: 66.98  E-value: 3.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDR-VAVKRL--DKSKMVLPIAVedvKREVQILIALSG--HENVVQFHNA-----FEDDDYVY 137
Cdd:cd07862   9 IGEGAYGKVFKARDLKNGGRfVALKRVrvQTGEEGMPLST---IREVAVLRHLETfeHPNVVRLFDVctvsrTDRETKLT 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 138 IVMELCEGG--ELLDRILSKKGNRYSEKDaavVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAqldSPLKATDFGLSDF 215
Cdd:cd07862  86 LVFEHVDQDltTYLDKVPEPGVPTETIKD---MMFQLLRGLDFLHSHRVVHRDLKPQNILVTSS---GQIKLADFGLARI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 216 IKPGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVItYILLCGRRPFWDRTED-----GIF------------KEVL 277
Cdd:cd07862 160 YSFQMALTSVVVTLWYRAPEVLLQSSyATPVDLWSVGCI-FAEMFRRKPLFRGSSDvdqlgKILdviglpgeedwpRDVA 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 34098881 278 RNKPDFSRKPWATIS-------DSAKDFVKKLLVKDPRARLTAAQALSH 319
Cdd:cd07862 239 LPRQAFHSKSAQPIEkfvtdidELGKDLLLKCLTFNPAKRISAYSALSH 287
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
65-255 4.27e-12

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 66.18  E-value: 4.27e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  65 GKLLGHGQFGYTYVAIHRpngdrvavkrlDKSKMVLPIAVEDVKREVQI-------LIALSGHENVVQFHNAFEDDDYVY 137
Cdd:cd05085   1 GELLGKGNFGEVYKGTLK-----------DKTPVAVKTCKEDLPQELKIkflsearILKQYDHPNIVKLIGVCTQRQPIY 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 138 IVMELCEGGELLDRILSKKGNrysekdaaVVVRQMLK-----VAGECHLHG--LVHRDMKPENFLFKSAQLdspLKATDF 210
Cdd:cd05085  70 IVMELVPGGDFLSFLRKKKDE--------LKTKQLVKfsldaAAGMAYLESknCIHRDLAARNCLVGENNA---LKISDF 138
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 34098881 211 GLS----DFIKPGKRFHDIvgSAYYVAPEVLKR-RSGPESDVWSIGVITY 255
Cdd:cd05085 139 GMSrqedDGVYSSSGLKQI--PIKWTAPEALNYgRYSSESDVWSFGILLW 186
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
369-513 4.80e-12

EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein (ALG-2); The family includes some homologs of mammalian apoptosis-linked gene 2 protein (ALG-2) mainly found in lower eukaryotes, such as a parasitic protist Leishmarua major and a cellular slime mold Dictyostelium discoideum. These homologs contains five EF-hand motifs. Due to the presence of unfavorable residues at the Ca2+-coordinating positions, their non-canonical EF4 and EF5 hands may not bind Ca2+. Two Dictyostelium PEF proteins are the prototypes of this family. They may bind to cytoskeletal proteins and/or signal-transducing proteins localized to detergent-resistant membranes named lipid rafts, and occur as monomers or weak homo- or heterodimers like ALG-2. They can serve as a mediator for Ca2+ signaling-related Dictyostehum programmed cell death (PCD).


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 64.16  E-value: 4.80e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 369 DLRDQFDAIDVDKNGVISLEEMRQALAKDLPwKLKDSRVAEILEAIDSNTDGLVDFTEFvaAALHvhqleehdseKWQLR 448
Cdd:cd16185   1 ELRQWFRAVDRDRSGSIDVNELQKALAGGGL-LFSLATAEKLIRMFDRDGNGTIDFEEF--AALH----------QFLSN 67
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34098881 449 SRAAFEKFDLDKDGYITPEELRMHTGLRG-SIDP-----LLDEADIDRDGKISLHEFRRLlrTASISSQRA 513
Cdd:cd16185  68 MQNGFEQRDTSRSGRLDANEVHEALAASGfQLDPpafqaLFRKFDPDRGGSLGFDDYIEL--CIFLASARN 136
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
58-258 4.88e-12

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: 66.46  E-value: 4.88e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  58 FHDHY-TIGKLLGHGQFG----YTYVAIHRPNGDRVAVKRLDKSKMvlPIAVEDVKREVQILIALSgHENVVQFHNAFED 132
Cdd:cd05080   1 FHKRYlKKIRDLGEGHFGkvslYCYDPTNDGTGEMVAVKALKADCG--PQHRSGWKQEIDILKTLY-HENIVKYKGCCSE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 133 --DDYVYIVMELCEGGELLDrILSKkgNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLdspLKATDF 210
Cdd:cd05080  78 qgGKSLQLIMEYVPLGSLRD-YLPK--HSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRL---VKIGDF 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 34098881 211 GLSDFIKPGKRFH----DIVGSAYYVAPEVLKR-RSGPESDVWSIGVITYILL 258
Cdd:cd05080 152 GLAKAVPEGHEYYrvreDGDSPVFWYAPECLKEyKFYYASDVWSFGVTLYELL 204
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
61-319 5.31e-12

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: 66.55  E-value: 5.31e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRldkskmVLPIAVEDVK---REVQILIALsGHENVV-----QFHNAFED 132
Cdd:cd13986   1 RYRIQRLLGEGGFSFVYLVEDLSTGRLYALKK------ILCHSKEDVKeamREIENYRLF-NHPNILrlldsQIVKEAGG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 133 DDYVYIVMELCEGGELLDRI--LSKKGNRYSEKDaavVVRQMLKV-AGECHLH-----GLVHRDMKPENFLFKSAqlDSP 204
Cdd:cd13986  74 KKEVYLLLPYYKRGSLQDEIerRLVKGTFFPEDR---ILHIFLGIcRGLKAMHepelvPYAHRDIKPGNVLLSED--DEP 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 205 LkATDFG---LSDFIKPGKR----FHDIV---GSAYYVAPEVLKRRSG----PESDVWSIGVITYILLCGRRPFwDRTE- 269
Cdd:cd13986 149 I-LMDLGsmnPARIEIEGRRealaLQDWAaehCTMPYRAPELFDVKSHctidEKTDIWSLGCTLYALMYGESPF-ERIFq 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 34098881 270 --DGIFKEVLRNKPDFSRKPwaTISDSAKDFVKKLLVKDPRARLTAAQALSH 319
Cdd:cd13986 227 kgDSLALAVLSGNYSFPDNS--RYSEELHQLVKSMLVVNPAERPSIDDLLSR 276
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
450-504 5.33e-12

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 61.02  E-value: 5.33e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34098881 450 RAAFEKFDLDKDGYITPEELRMHTGLRGS------IDPLLDEADIDRDGKISLHEFRRLLR 504
Cdd:cd00051   3 REAFRLFDKDGDGTISADELKAALKSLGEglseeeIDEMIREVDKDGDGKIDFEEFLELMA 63
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
68-211 6.11e-12

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: 63.23  E-value: 6.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEdvkREVQILIALSGHE-NVVQFHNAFEDDDYVYIVMELCEGG 146
Cdd:cd13968   1 MGEGASAKVFWAEGECTTIGVAVKIGDDVNNEEGEDLE---SEMDILRRLKGLElNIPKVLVTEDVDGPNILLMELVKGG 77
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34098881 147 ELLDRILskkGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFG 211
Cdd:cd13968  78 TLIAYTQ---EEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSE---DGNVKLIDFG 136
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
61-264 9.46e-12

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: 65.29  E-value: 9.46e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDrVAVKRLDKSKMvlpiAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVM 140
Cdd:cd05113   5 DLTFLKELGTGQFGVVKYGKWRGQYD-VAIKMIKEGSM----SEDEFIEEAKVMMNLS-HEKLVQLYGVCTKQRPIFIIT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCEGGELLDrILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKpGK 220
Cdd:cd05113  79 EYMANGCLLN-YLREMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVND---QGVVKVSDFGLSRYVL-DD 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 34098881 221 RFHDIVGSAYYV---APEVLKR-RSGPESDVWSIGVITY-ILLCGRRPF 264
Cdd:cd05113 154 EYTSSVGSKFPVrwsPPEVLMYsKFSSKSDVWAFGVLMWeVYSLGKMPY 202
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
355-430 1.09e-11

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 62.50  E-value: 1.09e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34098881 355 LRALASTLDEAEISDLRDQFDAIDVDKNGVISLEEMRQALAKdlpWKLKDSRVAEILEAIDSNTDGLVDFTEFVAA 430
Cdd:COG5126  56 VAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTA---LGVSEEEADELFARLDTDGDGKISFEEFVAA 128
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
88-279 1.22e-11

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: 65.10  E-value: 1.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  88 VAVKRLDKSKmvlpIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEGGELLDRILSKKGN-----RYSe 162
Cdd:cd13992  28 VAIKHITFSR----TEKRTILQELNQLKELV-HDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLLNREIKmdwmfKSS- 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 163 kdaavVVRQMLKvaGECHLHG---LVHRDMKPENFLfksaqLDSP--LKATDFGLSDFIKpGKRFHDIVGSA-----YYV 232
Cdd:cd13992 102 -----FIKDIVK--GMNYLHSssiGYHGRLKSSNCL-----VDSRwvVKLTDFGLRNLLE-EQTNHQLDEDAqhkklLWT 168
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 34098881 233 APEVLK-----RRSGPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVLRN 279
Cdd:cd13992 169 APELLRgslleVRGTQKGDVYSFAIILYEILFRSDPFALEREVAIVEKVISG 220
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
66-321 1.29e-11

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: 65.37  E-value: 1.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDRVAVKRLD-KSKMVLPIAVedvKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCE 144
Cdd:cd07870   6 EKLGEGSYATVYKGISRINGQLVALKVISmKTEEGVPFTA---IREASLLKGLK-HANIVLLHDIIHTKETLTFVFEYMH 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 145 GgELLDRILSKKGNRYSEkDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAqldSPLKATDFGLSDFIK-PGKRFH 223
Cdd:cd07870  82 T-DLAQYMIQHPGGLHPY-NVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYL---GELKLADFGLARAKSiPSQTYS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 224 DIVGSAYYVAPEVLKRRS--GPESDVWSIGVITYILLCGRRPF-------------WD----RTED---GIFKeVLRNKP 281
Cdd:cd07870 157 SEVVTLWYRPPDVLLGATdySSALDIWGAGCIFIEMLQGQPAFpgvsdvfeqlekiWTvlgvPTEDtwpGVSK-LPNYKP 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 34098881 282 DFSRKP--------WATISD--SAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd07870 236 EWFLPCkpqqlrvvWKRLSRppKAEDLASQMLMMFPKDRISAQDALLHPY 285
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
60-321 1.35e-11

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: 65.48  E-value: 1.35e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVK--RLDKSKMVLPIAVedvkREVQILIALSgHENVVQFHNAFEDDDYVY 137
Cdd:cd07869   5 DSYEKLEKLGEGSYATVYKGKSKVNGKLVALKviRLQEEEGTPFTAI----REASLLKGLK-HANIVLLHDIIHTKETLT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 138 IVMELCEGGelLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAqldSPLKATDFGLSDFIK 217
Cdd:cd07869  80 LVFEYVHTD--LCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDT---GELKLADFGLARAKS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 218 -PGKRFHDIVGSAYYVAPEVLKRRSGPES--DVWSIGVITYILLCGRRPF--WDRTEDGIFKEVL-------------RN 279
Cdd:cd07869 155 vPSHTYSNEVVTLWYRPPDVLLGSTEYSTclDMWGVGCIFVEMIQGVAAFpgMKDIQDQLERIFLvlgtpnedtwpgvHS 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 34098881 280 KPDFS------------RKPWATIS--DSAKDFVKKLLVKDPRARLTAAQALSHAW 321
Cdd:cd07869 235 LPHFKperftlyspknlRQAWNKLSyvNHAEDLASKLLQCFPKNRLSAQAALSHEY 290
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
67-315 2.17e-11

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: 64.20  E-value: 2.17e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  67 LLGHGQFGYTYVAIHRpnGDRVAVKRLDKSKmvlpiAVEDVKREVQILIALSgHENVVQFHNAFEDDDYvyIVMELCEGG 146
Cdd:cd14068   1 LLGDGGFGSVYRAVYR--GEDVAVKIFNKHT-----SFRLLRQELVVLSHLH-HPSLVALLAAGTAPRM--LVMELAPKG 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 147 ELlDRILskkgnrysEKDAAVVVRQM-----LKVA-GECHLHG--LVHRDMKPENFLFKSAQLDSPL--KATDFGLSDF- 215
Cdd:cd14068  71 SL-DALL--------QQDNASLTRTLqhriaLHVAdGLRYLHSamIIYRDLKPHNVLLFTLYPNCAIiaKIADYGIAQYc 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 216 IKPGKRFHDivGSAYYVAPEVLKRRS--GPESDVWSIGVITY-ILLCGrrpfwDRTEDGI-----FKE--VLRNKPD--- 282
Cdd:cd14068 142 CRMGIKTSE--GTPGFRAPEVARGNViyNQQADVYSFGLLLYdILTCG-----ERIVEGLkfpneFDElaIQGKLPDpvk 214
                       250       260       270
                ....*....|....*....|....*....|....
gi 34098881 283 -FSRKPWATIsdsaKDFVKKLLVKDPRARLTAAQ 315
Cdd:cd14068 215 eYGCAPWPGV----EALIKDCLKENPQCRPTSAQ 244
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
68-259 2.57e-11

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: 64.19  E-value: 2.57e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRL-----DKSKMVLpiavedvkREVQILIALSgHENVVQFHNAFEDDDYVYIVMEL 142
Cdd:cd14222   1 LGKGFFGQAIKVTHKATGKVMVMKELircdeETQKTFL--------TEVKVMRSLD-HPNVLKFIGVLYKDKRLNLLTEF 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 143 CEGGELLDRILSKKGNRYSEKdaavvVRQMLKVA-GECHLHGL--VHRDMKPENFLFKsaqLDSPLKATDFGLSDFI--- 216
Cdd:cd14222  72 IEGGTLKDFLRADDPFPWQQK-----VSFAKGIAsGMAYLHSMsiIHRDLNSHNCLIK---LDKTVVVADFGLSRLIvee 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34098881 217 -------KPG-----------KRFHDIVGSAYYVAPEVLKRRSGPES-DVWSIGvityILLC 259
Cdd:cd14222 144 kkkpppdKPTtkkrtlrkndrKKRYTVVGNPYWMAPEMLNGKSYDEKvDIFSFG----IVLC 201
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
369-430 3.19e-11

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 58.71  E-value: 3.19e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34098881 369 DLRDQFDAIDVDKNGVISLEEMRQALaKDLPWKLKDSRVAEILEAIDSNTDGLVDFTEFVAA 430
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAAL-KSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLEL 61
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
66-304 3.33e-11

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: 63.88  E-value: 3.33e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAihRPNGDrVAVKRLDKSKMVlPIAVEDVKREVQILIAlSGHENVVQFHNAFEDDDYVyIVMELCEG 145
Cdd:cd14150   6 KRIGTGSFGTVFRG--KWHGD-VAVKILKVTEPT-PEQLQAFKNEMQVLRK-TRHVNILLFMGFMTRPNFA-IITQWCEG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLdRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQldsPLKATDFGLSDfIKP----GKR 221
Cdd:cd14150  80 SSLY-RHLHVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGL---TVKIGDFGLAT-VKTrwsgSQQ 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 222 FHDIVGSAYYVAPEVLK-RRSGP---ESDVWSIGVITYILLCGRRPFWD-RTEDGIFKEVLRN--KPDFSRkpwatISDS 294
Cdd:cd14150 155 VEQPSGSILWMAPEVIRmQDTNPysfQSDVYAYGVVLYELMSGTLPYSNiNNRDQIIFMVGRGylSPDLSK-----LSSN 229
                       250
                ....*....|
gi 34098881 295 AKDFVKKLLV 304
Cdd:cd14150 230 CPKAMKRLLI 239
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
66-287 4.06e-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: 4.06e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRpNGDRVAVKRLDKSKMvlpiAVEDVKREVQILIALSgHENVVQFHnAFEDDDYVYIVMELCEG 145
Cdd:cd05067  13 ERLGAGQFGEVWMGYYN-GHTKVAIKSLKQGSM----SPDAFLAEANLMKQLQ-HQRLVRLY-AVVTQEPIYIITEYMEN 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFkSAQLDSplKATDFGLSDFIKP------- 218
Cdd:cd05067  86 GSLVDFLKTPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILV-SDTLSC--KIADFGLARLIEDneytare 162
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34098881 219 GKRFhdivgSAYYVAPEVLKRRS-GPESDVWSIGV-ITYILLCGRRPFWDRTEdgifKEVLRNKPDFSRKP 287
Cdd:cd05067 163 GAKF-----PIKWTAPEAINYGTfTIKSDVWSFGIlLTEIVTHGRIPYPGMTN----PEVIQNLERGYRMP 224
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
67-311 4.26e-11

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: 63.61  E-value: 4.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  67 LLGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMVLPIAVEDVKREVQILIALSGHEN---VVQFHNAFEDDDYVYIVMELC 143
Cdd:cd05606   1 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGGDcpfIVCMTYAFQTPDKLCFILDLM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 144 EGGELlDRILSKKGnRYSEKD----AAVVVrqmlkvAGECHLH--GLVHRDMKPENFLFKSAqldSPLKATDFGLS-DFI 216
Cdd:cd05606  81 NGGDL-HYHLSQHG-VFSEAEmrfyAAEVI------LGLEHMHnrFIVYRDLKPANILLDEH---GHVRISDLGLAcDFS 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 217 KpgKRFHDIVGSAYYVAPEVLKRRSGPES--DVWSIGVITYILLCGRRPF-WDRTEDG--IFKEVLRNKPDFSRkpwaTI 291
Cdd:cd05606 150 K--KKPHASVGTHGYMAPEVLQKGVAYDSsaDWFSLGCMLYKLLKGHSPFrQHKTKDKheIDRMTLTMNVELPD----SF 223
                       250       260
                ....*....|....*....|
gi 34098881 292 SDSAKDFVKKLLVKDPRARL 311
Cdd:cd05606 224 SPELKSLLEGLLQRDVSKRL 243
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
61-264 5.23e-11

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: 62.97  E-value: 5.23e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRpnGDRVAVKRLDkskmvLPIAVEDVKREVQILIALSgHENVVQ-----FHNAfedddy 135
Cdd:cd05083   7 KLTLGEIIGEGEFGAVLQGEYM--GQKVAVKNIK-----CDVTAQAFLEETAVMTKLQ-HKNLVRllgviLHNG------ 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 136 VYIVMELCEGGELLDrILSKKGNrysekdAAVVVRQMLKVA-----GECHLHG--LVHRDMKPENFLFKSaqlDSPLKAT 208
Cdd:cd05083  73 LYIVMELMSKGNLVN-FLRSRGR------ALVPVIQLLQFSldvaeGMEYLESkkLVHRDLAARNILVSE---DGVAKIS 142
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 34098881 209 DFGLSdfiKPGKRFHDIVG-SAYYVAPEVLK-RRSGPESDVWSIGVITY-ILLCGRRPF 264
Cdd:cd05083 143 DFGLA---KVGSMGVDNSRlPVKWTAPEALKnKKFSSKSDVWSYGVLLWeVFSYGRAPY 198
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
65-255 5.43e-11

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: 63.03  E-value: 5.43e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  65 GKLLGHGQFGYTYVAIHRPNGDRVAVKrldKSKMVLPIAVED-VKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELC 143
Cdd:cd05084   1 GERIGRGNFGEVFSGRLRADNTPVAVK---SCRETLPPDLKAkFLQEARILKQYS-HPNIVRLIGVCTQKQPIYIVMELV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 144 EGGELLDrILSKKGNRYSEKDaavVVRQMLKVA-GECHLHG--LVHRDMKPENFLFKSaqlDSPLKATDFGLSdfikpgK 220
Cdd:cd05084  77 QGGDFLT-FLRTEGPRLKVKE---LIRMVENAAaGMEYLESkhCIHRDLAARNCLVTE---KNVLKISDFGMS------R 143
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 34098881 221 RFHDIVGSAY---------YVAPEVLKR-RSGPESDVWSIGVITY 255
Cdd:cd05084 144 EEEDGVYAATggmkqipvkWTAPEALNYgRYSSESDVWSFGILLW 188
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
371-498 5.43e-11

EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 (RCN-3), and similar proteins; The family corresponds to a group of six EF-hand Ca2+-binding proteins, including calumenin (also known as crocalbin or CBP-50), reticulocalbin-1 (RCN-1), reticulocalbin-3 (RCN-3), and similar proteins. Calumenin is an endo/sarcoplasmic reticulum (ER/SR) resident low-affinity Ca2+-binding protein that contains six EF-hand domains and a C-terminal SR retention signal His-Asp-Glu-Phe (HDEF) tetrapeptide. It functions as a novel regulator of SERCA2, and its expressional changes are tightly coupled with Ca2+-cycling of cardiomyocytes. It is also broadly involved in haemostasis and in the pathophysiology of thrombosis. Moreover, the extracellular calumenin acts as a suppressor of cell migration and tumor metastasis. RCN-1 is an endoplasmic reticulum resident Ca2+-binding protein with a carboxyl-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide signal. It acts as a potential negative regulator of B-RAF activation and can negatively modulate cardiomyocyte hypertrophy by inhibition of the mitogen-activated protein kinase signalling cascade. It also plays a key role in the development of doxorubicin-associated resistance. RCN-3 is a putative six EF-hand Ca2+-binding protein that contains five RXXR (X is any amino acid) motifs and a C-terminal ER retrieval signal HDEL tetrapeptide. The RXXR motif represents the target sequence of subtilisin-like proprotein convertases (SPCs). RCN-3 is specifically bound to the paired basic amino-acid-cleaving enzyme-4 (PACE4) precursor protein and plays an important role in the biosynthesis of PACE4.


Pssm-ID: 320024 [Multi-domain]  Cd Length: 264  Bit Score: 62.99  E-value: 5.43e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 371 RDQ--FDAIDVDKNGVISLEEMRQAL-AKDLPwKLKDSRVAEILEAIDSNTDGLVDFTEFVaAALHVHQLEEHDSEkWQL 447
Cdd:cd16226 120 RDErrWKAADQDGDGKLTKEEFTAFLhPEEFP-HMRDIVVQETLEDIDKNKDGFISLEEYI-GDMYRDDDEEEDPD-WVK 196
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 34098881 448 RSRAAFEKF-DLDKDGYITPEELR---MHTG---LRGSIDPLLDEADIDRDGKISLHE 498
Cdd:cd16226 197 SEREQFKEFrDKNKDGKMDREEVKdwiLPEDydhAEAEAKHLIYEADDDKDGKLTKEE 254
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
406-513 7.07e-11

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 60.19  E-value: 7.07e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 406 RVAEILEAIDSNTDGLVDFTEFVAAALHVhqleehdsekWqlrsRAAFEKFDLDKDGYITPEELRMHT------GLRGSI 479
Cdd:COG5126   6 KLDRRFDLLDADGDGVLERDDFEALFRRL----------W----ATLFSEADTDGDGRISREEFVAGMeslfeaTVEPFA 71
                        90       100       110
                ....*....|....*....|....*....|....
gi 34098881 480 DPLLDEADIDRDGKISLHEFRRLLRTASISSQRA 513
Cdd:COG5126  72 RAAFDLLDTDGDGKISADEFRRLLTALGVSEEEA 105
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
68-280 1.04e-10

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: 62.53  E-value: 1.04e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKskmvlpiAVEDVKR----EVQILIALSgHENVVQFHNAFEDDDYVYIVMELC 143
Cdd:cd14154   1 LGKGFFGQAIKVTHRETGEVMVMKELIR-------FDEEAQRnflkEVKVMRSLD-HPNVLKFIGVLYKDKKLNLITEYI 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 144 EGGELLDRILSKKGN-------RYSeKDAAvvvrqmlkvAGECHLH--GLVHRDMKPENFLFKsaqLDSPLKATDFGLSD 214
Cdd:cd14154  73 PGGTLKDVLKDMARPlpwaqrvRFA-KDIA---------SGMAYLHsmNIIHRDLNSHNCLVR---EDKTVVVADFGLAR 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 215 FI-----------KPGKRFH----------DIVGSAYYVAPEVLKRRSGPES-DVWSIGvityILLC---GR---RP-FW 265
Cdd:cd14154 140 LIveerlpsgnmsPSETLRHlkspdrkkryTVVGNPYWMAPEMLNGRSYDEKvDIFSFG----IVLCeiiGRveaDPdYL 215
                       250
                ....*....|....*.
gi 34098881 266 DRTED-GIFKEVLRNK 280
Cdd:cd14154 216 PRTKDfGLNVDSFREK 231
STKc_CK1_fungal cd14127
Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 1; ...
61-220 1.20e-10

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: 62.13  E-value: 1.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKrLDKSKMVLPiAVEDVKREVQILIALSGHENVVQF-----HNAfedddy 135
Cdd:cd14127   1 HYKVGKKIGEGSFGVIFEGTNLLNGQQVAIK-FEPRKSDAP-QLRDEYRTYKLLAGCPGIPNVYYFgqeglHNI------ 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 136 vyIVMELCegGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLF-----KSAQLdspLKATDF 210
Cdd:cd14127  73 --LVIDLL--GPSLEDLFDLCGRKFSVKTVVMVAKQMLTRVQTIHEKNLIYRDIKPDNFLIgrpgtKNANV---IHVVDF 145
                       170
                ....*....|
gi 34098881 211 GLSDFIKPGK 220
Cdd:cd14127 146 GMAKQYRDPK 155
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
65-264 1.28e-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: 62.28  E-value: 1.28e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  65 GKLLGHGQFGYTYVAIHRPNGDRVAVkrldkskmvlPIAVEDVKREV--QILIALSGHenvvqfHNAFEDDDYVYIV--M 140
Cdd:cd05111  12 LKVLGSGVFGTVHKGIWIPEGDSIKI----------PVAIKVIQDRSgrQSFQAVTDH------MLAIGSLDHAYIVrlL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCEG------------GELLDRILSKKGNRysekDAAVVVRQMLKVA-GECHL--HGLVHRDMKPENFLFKSaqlDSPL 205
Cdd:cd05111  76 GICPGaslqlvtqllplGSLLDHVRQHRGSL----GPQLLLNWCVQIAkGMYYLeeHRMVHRNLAARNVLLKS---PSQV 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34098881 206 KATDFGLSDFIKPGKR---FHDIVGSAYYVAPE-VLKRRSGPESDVWSIGVITYILLC-GRRPF 264
Cdd:cd05111 149 QVADFGVADLLYPDDKkyfYSEAKTPIKWMALEsIHFGKYTHQSDVWSYGVTVWEMMTfGAEPY 212
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
67-258 1.63e-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: 61.83  E-value: 1.63e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  67 LLGHGQFGYTYVAIHRPNGDR----VAVKRLDKSKmvlPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDY--VYIVM 140
Cdd:cd05081  11 QLGKGNFGSVELCRYDPLGDNtgalVAVKQLQHSG---PDQQRDFQREIQILKALH-SDFIVKYRGVSYGPGRrsLRLVM 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCEGGELLDrILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKPGK 220
Cdd:cd05081  87 EYLPSGCLRD-FLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVES---EAHVKIADFGLAKLLPLDK 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 34098881 221 RFHDI----VGSAYYVAPEVLKRRS-GPESDVWSIGVITYILL 258
Cdd:cd05081 163 DYYVVrepgQSPIFWYAPESLSDNIfSRQSDVWSFGVVLYELF 205
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
68-259 1.86e-10

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: 61.51  E-value: 1.86e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKmvlpiavEDVKR----EVQILIALSgHENVVQFHNAFEDDDYVYIVMELC 143
Cdd:cd14221   1 LGKGCFGQAIKVTHRETGEVMVMKELIRFD-------EETQRtflkEVKVMRCLE-HPNVLKFIGVLYKDKRLNFITEYI 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 144 EGGELLDRILSKK-----GNRYS-EKDAAvvvrqmlkvAGECHLHGL--VHRDMKPENFLFKSaqlDSPLKATDFGLSDF 215
Cdd:cd14221  73 KGGTLRGIIKSMDshypwSQRVSfAKDIA---------SGMAYLHSMniIHRDLNSHNCLVRE---NKSVVVADFGLARL 140
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 216 I--------------KPGKR-FHDIVGSAYYVAPEVLKRRSGPES-DVWSIGvityILLC 259
Cdd:cd14221 141 MvdektqpeglrslkKPDRKkRYTVVGNPYWMAPEMINGRSYDEKvDVFSFG----IVLC 196
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
68-252 2.01e-10

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: 61.21  E-value: 2.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDR---VAVKRLDKSKMvlPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVyIVMELCE 144
Cdd:cd05060   3 LGHGNFGSVRKGVYLMKSGKeveVAVKTLKQEHE--KAGKKEFLREASVMAQLD-HPCIVRLIGVCKGEPLM-LVMELAP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 145 GGELLDrILSKKGNrYSEKDAAVVVRQM---LKVAGECHLhglVHRDMKPENFLFKSaqlDSPLKATDFGLSDFIKPGkr 221
Cdd:cd05060  79 LGPLLK-YLKKRRE-IPVSDLKELAHQVamgMAYLESKHF---VHRDLAARNVLLVN---RHQAKISDFGMSRALGAG-- 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 34098881 222 fhdivgSAYY------------VAPEVLK-RRSGPESDVWSIGV 252
Cdd:cd05060 149 ------SDYYrattagrwplkwYAPECINyGKFSSKSDVWSYGV 186
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
117-313 2.30e-10

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: 61.74  E-value: 2.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 117 LSGHENVVQFHNAFEDD---------DY------------------VYIVMEL--CEGGELLDRilskkgNRYSEKDAAV 167
Cdd:cd14018  69 LAPHPNIIRVQRAFTDSvpllpgaieDYpdvlparlnpsglghnrtLFLVMKNypCTLRQYLWV------NTPSYRLARV 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 168 VVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSP-LKATDFG--------------LSDFIKPGkrfhdivGSAYYV 232
Cdd:cd14018 143 MILQLLEGVDHLVRHGIAHRDLKSDNILLELDFDGCPwLVIADFGccladdsiglqlpfSSWYVDRG-------GNACLM 215
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 233 APEVLKRRSGP-------ESDVWSIGVITYILLCGRRPFWdrtedGIFKEVLRNKpDFSRKPWATISDS----AKDFVKK 301
Cdd:cd14018 216 APEVSTAVPGPgvvinysKADAWAVGAIAYEIFGLSNPFY-----GLGDTMLESR-SYQESQLPALPSAvppdVRQVVKD 289
                       250
                ....*....|..
gi 34098881 302 LLVKDPRARLTA 313
Cdd:cd14018 290 LLQRDPNKRVSA 301
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
368-498 2.37e-10

EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin/ERC45/calumenin)-EF hand family contains a group of six EF-hand, low-affinity Ca2+-binding proteins, including reticulocalbin (RCN-1), ER Ca2+-binding protein of 55 kDa (ERC-55, also known as TCBP-49 or E6BP), reticulocalbin-3 (RCN-3), Ca2+-binding protein of 45 kDa (Cab45 and its splice variant Cab45b), and calumenin ( also known as crocalbin or CBP-50). The proteins are not only localized in various parts of the secretory pathway, but also found in the cytosolic compartment and at the cell surface. They interact with different ligands or proteins and have been implicated in the secretory process, chaperone activity, signal transduction as well as in a large variety of disease processes.


Pssm-ID: 320021 [Multi-domain]  Cd Length: 267  Bit Score: 61.30  E-value: 2.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 368 SDLRDQFDAIDVDKNGVISLEEMRQALAKDLPWKLKDSRVAEILEAIDSNTDGLVDFTEFVaaALHVHQLEEHDSEKWQL 447
Cdd:cd15899 123 LKDKKRFEAADQDGDLILTLEEFLAFLHPEESPYMLDFVIKETLEDLDKNGDGFISLEEFI--SDPYSADENEEEPEWVK 200
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34098881 448 RSRAAFEKF-DLDKDGYITPEELRMHtglrgsIDP------------LLDEADIDRDGKISLHE 498
Cdd:cd15899 201 VEKERFVELrDKDKDGKLDGEELLSW------VDPsnqeialeeakhLIAESDENKDGKLSPEE 258
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
63-276 2.80e-10

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: 61.04  E-value: 2.80e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  63 TIGKLLGHGQFGYTYVAIHRPNGDR---VAVKRL-----DKSKmvlpiavEDVKREVQILIALSgHENVVQFHNAFEDDD 134
Cdd:cd05066   7 KIEKVIGAGEFGEVCSGRLKLPGKReipVAIKTLkagytEKQR-------RDFLSEASIMGQFD-HPNIIHLEGVVTRSK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 135 YVYIVMELCEGGELlDRILSKKGNRYSEKDAAVVVRQMlkVAGECHLH--GLVHRDMKPENFLFKSAQLdspLKATDFGL 212
Cdd:cd05066  79 PVMIVTEYMENGSL-DAFLRKHDGQFTVIQLVGMLRGI--ASGMKYLSdmGYVHRDLAARNILVNSNLV---CKVSDFGL 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34098881 213 SDFIKpgkrfhDIVGSAY----------YVAPEVLK-RRSGPESDVWSIGVITY-ILLCGRRPFWDRTEDGIFKEV 276
Cdd:cd05066 153 SRVLE------DDPEAAYttrggkipirWTAPEAIAyRKFTSASDVWSYGIVMWeVMSYGERPYWEMSNQDVIKAI 222
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
68-253 3.21e-10

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: 60.90  E-value: 3.21e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVKRLDKSKMvlpiAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEGGE 147
Cdd:cd05052  14 LGGGQYGEVYEGVWKKYNLTVAVKTLKEDTM----EVEEFLKEAAVMKEIK-HPNLVQLLGVCTREPPFYIITEFMPYGN 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 148 LLDRILSKKGnrySEKDAAVVVRQMLKVA-GECHLHG--LVHRDMKPENFLFKSAQLdspLKATDFGLSDFIKpGKRFHD 224
Cdd:cd05052  89 LLDYLRECNR---EELNAVVLLYMATQIAsAMEYLEKknFIHRDLAARNCLVGENHL---VKVADFGLSRLMT-GDTYTA 161
                       170       180       190
                ....*....|....*....|....*....|...
gi 34098881 225 IVGSAY---YVAPEVLK-RRSGPESDVWSIGVI 253
Cdd:cd05052 162 HAGAKFpikWTAPESLAyNKFSIKSDVWAFGVL 194
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
61-315 4.20e-10

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: 60.60  E-value: 4.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  61 HYTIGKL-LGHGQFGYTYVAIHRPNGDRVAVKRldkskmvlpIAVEDVKREVQILIALSGHENVVQFHNAFEDDDYVYIV 139
Cdd:cd13991   6 HWATHQLrIGRGSFGEVHRMEDKQTGFQCAVKK---------VRLEVFRAEELMACAGLTSPRVVPLYGAVREGPWVNIF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELCEGGELLDriLSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLkaTDFGLSDFIKP- 218
Cdd:cd13991  77 MDLKEGGSLGQ--LIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGSDAFL--CDFGHAECLDPd 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 --GK---RFHDIVGSAYYVAPEVLK-RRSGPESDVWSIGVITYILLCGRRPfWDRTEDGIFKEVLRNKPDFSRKPWATIS 292
Cdd:cd13991 153 glGKslfTGDYIPGTETHMAPEVVLgKPCDAKVDVWSSCCMMLHMLNGCHP-WTQYYSGPLCLKIANEPPPLREIPPSCA 231
                       250       260
                ....*....|....*....|...
gi 34098881 293 DSAKDFVKKLLVKDPRARLTAAQ 315
Cdd:cd13991 232 PLTAQAIQAGLRKEPVHRASAAE 254
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
60-315 4.45e-10

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: 60.96  E-value: 4.45e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFG-----YTYVAIHRPNGDRVAVKrldkskMVLPIAVEDVKR----EVQILIALSGHENVVQFHNAF 130
Cdd:cd05055  35 NNLSFGKTLGAGAFGkvveaTAYGLSKSDAVMKVAVK------MLKPTAHSSEREalmsELKIMSHLGNHENIVNLLGAC 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 131 EDDDYVYIVMELCEGGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLdspLKATDF 210
Cdd:cd05055 109 TIGGPILVITEYCCYGDLLNFLRRKRESFLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKI---VKICDF 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 211 GLSDFIKpgkrfHD----IVGSAY----YVAPE-VLKRRSGPESDVWSIGVITY-ILLCGRRPFWDRTEDGIFKEVLRNK 280
Cdd:cd05055 186 GLARDIM-----NDsnyvVKGNARlpvkWMAPEsIFNCVYTFESDVWSYGILLWeIFSLGSNPYPGMPVDSKFYKLIKEG 260
                       250       260       270
                ....*....|....*....|....*....|....*
gi 34098881 281 PDFSRKPWATisDSAKDFVKKLLVKDPRARLTAAQ 315
Cdd:cd05055 261 YRMAQPEHAP--AEIYDIMKTCWDADPLKRPTFKQ 293
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
62-270 5.07e-10

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; 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. Mutations in TTBK2 is associated with the development of spinocerebellar ataxia type 11, belonging to a group of neurodegenerative disorders characterized by progressive incoordination, dysarthria and impairment of eye movements. Brain tissues of SCA11 patients show the presence of neurofibrillary tangles and tau deposition in the brain, similar to Alzheimer's disease (AD) patients. The TTBK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271031 [Multi-domain]  Cd Length: 262  Bit Score: 60.07  E-value: 5.07e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVK--RLDKSKMVLpiavedvKREVQILIALSGHENVVQFHNAFEDDDYVYIV 139
Cdd:cd14129   2 WKVLRKIGGGGFGEIYDALDLLTRENVALKveSAQQPKQVL-------KMEVAVLKKLQGKDHVCRFIGCGRNDRFNYVV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELcEGGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFksAQLDSPLKAT---DFGLS-DF 215
Cdd:cd14129  75 MQL-QGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAM--GRFPSTCRKCymlDFGLArQF 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34098881 216 ------IKPGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPfWDRTED 270
Cdd:cd14129 152 tnscgdVRPPRAVAGFRGTVRYASINAHRNREmGRHDDLWSLFYMLVEFVVGQLP-WRKIKD 212
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
66-264 5.09e-10

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: 59.93  E-value: 5.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHrpNGD-RVAVKRLDKSKMvlpiAVEDVKREVQILIALSgHENVVQFHnAFEDDDYVYIVMELCE 144
Cdd:cd14203   1 VKLGQGCFGEVWMGTW--NGTtKVAIKTLKPGTM----SPEAFLEEAQIMKKLR-HDKLVQLY-AVVSEEPIYIVTEFMS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 145 GGELLDRIlsKKGNRYSEKDAAVVVRQMLKVAGECHLHGL--VHRDMKPENFLFKSAQLdspLKATDFGLSDFIKPGKrF 222
Cdd:cd14203  73 KGSLLDFL--KDGEGKYLKLPQLVDMAAQIASGMAYIERMnyIHRDLRAANILVGDNLV---CKIADFGLARLIEDNE-Y 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 34098881 223 HDIVGSAY---YVAPEV-LKRRSGPESDVWSIGV-ITYILLCGRRPF 264
Cdd:cd14203 147 TARQGAKFpikWTAPEAaLYGRFTIKSDVWSFGIlLTELVTKGRVPY 193
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
63-278 5.41e-10

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: 60.26  E-value: 5.41e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  63 TIGKLLGHGQFGYTYVAIHRPNgDRVAVKRLDKSKMvlpiAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMEL 142
Cdd:cd05114   7 TFMKELGSGLFGVVRLGKWRAQ-YKVAIKAIREGAM----SEEDFIEEAKVMMKLT-HPKLVQLYGVCTQQKPIYIVTEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 143 CEGGELLDRILSKKGNRysEKDAAVVVRQMLKVAGE-CHLHGLVHRDMKPENFLFKSAQLdspLKATDFGLSDFI----- 216
Cdd:cd05114  81 MENGCLLNYLRQRRGKL--SRDMLLSMCQDVCEGMEyLERNNFIHRDLAARNCLVNDTGV---VKVSDFGMTRYVlddqy 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34098881 217 --KPGKRFhdivgSAYYVAPEVLK-RRSGPESDVWSIGVITY-ILLCGRRPFWDRTEDGIFKEVLR 278
Cdd:cd05114 156 tsSSGAKF-----PVKWSPPEVFNySKFSSKSDVWSFGVLMWeVFTEGKMPFESKSNYEVVEMVSR 216
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
62-319 5.57e-10

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: 60.73  E-value: 5.57e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLdKSKmvlPIAVEDVKREVQILIAL------SGHENVVQFHNAFEDDDY 135
Cdd:cd14212   1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVL-KNK---PAYFRQAMLEIAILTLLntkydpEDKHHIVRLLDHFMHHGH 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 136 VYIVMELCeGGELLDRIlskKGNRY---SEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqLDSP-LKATDFG 211
Cdd:cd14212  77 LCIVFELL-GVNLYELL---KQNQFrglSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVN--LDSPeIKLIDFG 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 212 LSDFikPGKRFHDIVGSAYYVAPEVLkrrSG-PES---DVWSIGVIT---------------YILLC------GRRPFW- 265
Cdd:cd14212 151 SACF--ENYTLYTYIQSRFYRSPEVL---LGlPYStaiDMWSLGCIAaelflglplfpgnseYNQLSriiemlGMPPDWm 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 266 -----------DRTEDGIFKEVLRNKP--DFSRK------------PWATISDSAK-----------------------D 297
Cdd:cd14212 226 lekgkntnkffKKVAKSGGRSTYRLKTpeEFEAEnncklepgkryfKYKTLEDIIMnypmkkskkeqidkemetrlafiD 305
                       330       340
                ....*....|....*....|..
gi 34098881 298 FVKKLLVKDPRARLTAAQALSH 319
Cdd:cd14212 306 FLKGLLEYDPKKRWTPDQALNH 327
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
68-253 5.59e-10

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: 59.80  E-value: 5.59e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGDRVAVK----RLDKSKMVlpiavedvkREVQILIALSgHENVVQFHNAFEDDDYVYIVMELC 143
Cdd:cd14155   1 IGSGFFSEVYKVRHRTSGQVMALKmntlSSNRANML---------REVQLMNRLS-HPNILRFMGVCVHQGQLHALTEYI 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 144 EGGELLDRILSKKgnrysEKDAAVVVRQMLKVA-GECHLH--GLVHRDMKPENFLFKSAQLDSPLKATDFGLSDFI---K 217
Cdd:cd14155  71 NGGNLEQLLDSNE-----PLSWTVRVKLALDIArGLSYLHskGIFHRDLTSKNCLIKRDENGYTAVVGDFGLAEKIpdyS 145
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 34098881 218 PGKRFHDIVGSAYYVAPEVLKRRSGPE-SDVWSIGVI 253
Cdd:cd14155 146 DGKEKLAVVGSPYWMAPEVLRGEPYNEkADVFSYGII 182
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
68-280 6.27e-10

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: 60.44  E-value: 6.27e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAI---HRPNGDR--VAVKRLDKSKmvlPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMEL 142
Cdd:cd05093  13 LGEGAFGKVFLAEcynLCPEQDKilVAVKTLKDAS---DNARKDFHREAELLTNLQ-HEHIVKFYGVCVEGDPLIMVFEY 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 143 CEGGEL--------LDRILSKKGNRYSEkdaaVVVRQMLKVA-----GECHL--HGLVHRDMKPENFLFKSAQLdspLKA 207
Cdd:cd05093  89 MKHGDLnkflrahgPDAVLMAEGNRPAE----LTQSQMLHIAqqiaaGMVYLasQHFVHRDLATRNCLVGENLL---VKI 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 208 TDFGLS------DFIKPGKrfHDIVGSAYYVAPEVLKRRSGPESDVWSIGVITY-ILLCGRRPFWDRTEDGIFKEVLRNK 280
Cdd:cd05093 162 GDFGMSrdvystDYYRVGG--HTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWeIFTYGKQPWYQLSNNEVIECITQGR 239
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
68-265 7.08e-10

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: 60.02  E-value: 7.08e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAI---HRPNGDR--VAVKRLDKSKMVlpiAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMEL 142
Cdd:cd05094  13 LGEGAFGKVFLAEcynLSPTKDKmlVAVKTLKDPTLA---ARKDFQREAELLTNLQ-HDHIVKFYGVCGDGDPLIMVFEY 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 143 CEGGELlDRILSKKG--------NRYSEKDAAVVVRQMLKVA-----GECHL--HGLVHRDMKPENFLFKSAQLdspLKA 207
Cdd:cd05094  89 MKHGDL-NKFLRAHGpdamilvdGQPRQAKGELGLSQMLHIAtqiasGMVYLasQHFVHRDLATRNCLVGANLL---VKI 164
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34098881 208 TDFGLSdfikpgkrfHDIVGSAYY------------VAPE-VLKRRSGPESDVWSIGVITY-ILLCGRRPFW 265
Cdd:cd05094 165 GDFGMS---------RDVYSTDYYrvgghtmlpirwMPPEsIMYRKFTTESDVWSFGVILWeIFTYGKQPWF 227
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
66-278 7.46e-10

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: 60.08  E-value: 7.46e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNgDRVAVKRLDKSKMvlpiAVEDVKREVQILIALSgHENVVQFHnAFEDDDYVYIVMELCEG 145
Cdd:cd05070  15 KRLGNGQFGEVWMGTWNGN-TKVAIKTLKPGTM----SPESFLEEAQIMKKLK-HDKLVQLY-AVVSEEPIYIVTEYMSK 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 146 GELLDRILSKKGNRYSEKDAAVVVRQMlkVAGECHLHGL--VHRDMKPENFLFKSAQLdspLKATDFGLSDFI------- 216
Cdd:cd05070  88 GSLLDFLKDGEGRALKLPNLVDMAAQV--AAGMAYIERMnyIHRDLRSANILVGNGLI---CKIADFGLARLIedneyta 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34098881 217 KPGKRFhdivgSAYYVAPEV-LKRRSGPESDVWSIGV-ITYILLCGRRPFWDRTEDGIFKEVLR 278
Cdd:cd05070 163 RQGAKF-----PIKWTAPEAaLYGRFTIKSDVWSFGIlLTELVTKGRVPYPGMNNREVLEQVER 221
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
68-285 8.19e-10

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: 59.33  E-value: 8.19e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAihRPNGDrVAVKRLDKSKMVlPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVyIVMELCEGGE 147
Cdd:cd14062   1 IGSGSFGTVYKG--RWHGD-VAVKKLNVTDPT-PSQLQAFKNEVAVLRKTR-HVNILLFMGYMTKPQLA-IVTQWCEGSS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 148 LLdRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPEN-FLfksaQLDSPLKATDFGLSDfIKP----GKRF 222
Cdd:cd14062  75 LY-KHLHVLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNiFL----HEDLTVKIGDFGLAT-VKTrwsgSQQF 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 223 HDIVGSAYYVAPEVLKRRSG----PESDVWSIGVITYILLCGRRPFWD-RTEDGIFKEVLRN--KPDFSR 285
Cdd:cd14062 149 EQPTGSILWMAPEVIRMQDEnpysFQSDVYAFGIVLYELLTGQLPYSHiNNRDQILFMVGRGylRPDLSK 218
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
64-268 8.39e-10

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: 59.50  E-value: 8.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  64 IGKLLGHGQFGYTYVAIHRPNGDR---VAVKRLDKSkmvlpiAVEDVKREVQILIALSG---HENVVQFHNAFEDDDYVY 137
Cdd:cd05065   8 IEEVIGAGEFGEVCRGRLKLPGKReifVAIKTLKSG------YTEKQRRDFLSEASIMGqfdHPNIIHLEGVVTKSRPVM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 138 IVMELCEGGELlDRILSKKGNRYSEKDAAVVVRQMlkVAGECHLHGL--VHRDMKPENFLFKSAQLdspLKATDFGLSDF 215
Cdd:cd05065  82 IITEFMENGAL-DSFLRQNDGQFTVIQLVGMLRGI--AAGMKYLSEMnyVHRDLAARNILVNSNLV---CKVSDFGLSRF 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34098881 216 IKPGKRFHDIVGS------AYYVAPEVLK-RRSGPESDVWSIGVITY-ILLCGRRPFWDRT 268
Cdd:cd05065 156 LEDDTSDPTYTSSlggkipIRWTAPEAIAyRKFTSASDVWSYGIVMWeVMSYGERPYWDMS 216
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
67-318 8.98e-10

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: 59.55  E-value: 8.98e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  67 LLGHGQFGYTYVAihRPNGDRVAVKRLDKSK-----------MVLPIAVED-------VKREVQILIALSgHENVVQFHN 128
Cdd:cd14000   1 LLGDGGFGSVYRA--SYKGEPVAVKIFNKHTssnfanvpadtMLRHLRATDamknfrlLRQELTVLSHLH-HPSIVYLLG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 129 AFEDDdyVYIVMELCEGGELlDRILSKKGNRYSEKDAAVVVRQMLKVA-GECHLHG--LVHRDMKPENFLFKSaqLDSP- 204
Cdd:cd14000  78 IGIHP--LMLVLELAPLGSL-DHLLQQDSRSFASLGRTLQQRIALQVAdGLRYLHSamIIYRDLKSHNVLVWT--LYPNs 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 205 ---LKATDFGLSDFIKP--GKRFHdivGSAYYVAPEVLKRRS--GPESDVWSIGVITYILLCGRRPFWDRTEDGIFKEVL 277
Cdd:cd14000 153 aiiIKIADYGISRQCCRmgAKGSE---GTPGFRAPEIARGNViyNEKVDVFSFGMLLYEILSGGAPMVGHLKFPNEFDIH 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 34098881 278 RNKPDFSRKPWATISDSAKDFVKKLLVKDPRARLTAAQALS 318
Cdd:cd14000 230 GGLRPPLKQYECAPWPEVEVLMKKCWKENPQQRPTAVTVVS 270
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
67-313 9.31e-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: 59.76  E-value: 9.31e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  67 LLGHGQFGYTYVAihRPNGDRVAVKrldkskmVLPIAVEDV-KREVQIL-IALSGHENVVQFHNAFEDDDY----VYIVM 140
Cdd:cd13998   2 VIGKGRFGEVWKA--SLKNEPVAVK-------IFSSRDKQSwFREKEIYrTPMLKHENILQFIAADERDTAlrteLWLVT 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCEGGELLDRIlskkgNRYSekdaaVVVRQMLKVA-----GECHLH-----------GLVHRDMKPENFLFKSaqlDSP 204
Cdd:cd13998  73 AFHPNGSL*DYL-----SLHT-----IDWVSLCRLAlsvarGLAHLHseipgctqgkpAIAHRDLKSKNILVKN---DGT 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 205 LKATDFGLSDFIKPGKRFHDI-----VGSAYYVAPEVLKRR-------SGPESDVWSIGVITYILLcgRR---------- 262
Cdd:cd13998 140 CCIADFGLAVRLSPSTGEEDNanngqVGTKRYMAPEVLEGAinlrdfeSFKRVDIYAMGLVLWEMA--SRctdlfgivee 217
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34098881 263 ---PFWDRT-EDGIFKE----VLRNK--PDFsrkPWATISDSAKDFVKKLLVK----DPRARLTA 313
Cdd:cd13998 218 ykpPFYSEVpNHPSFEDmqevVVRDKqrPNI---PNRWLSHPGLQSLAETIEEcwdhDAEARLTA 279
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
56-264 1.27e-09

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: 58.84  E-value: 1.27e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  56 KDFHDHYTIGKllghGQFGYTYVAIHRpnGDRVAVK--RLDKSKMVLpIAVEDVKREVQilialsgHENVVQFHNAF-ED 132
Cdd:cd05082   6 KELKLLQTIGK----GEFGDVMLGDYR--GNKVAVKciKNDATAQAF-LAEASVMTQLR-------HSNLVQLLGVIvEE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 133 DDYVYIVMELCEGGELLDRILSKKgnrysekdaavvvRQMLkvAGECHLH---------------GLVHRDMKPENFLFK 197
Cdd:cd05082  72 KGGLYIVTEYMAKGSLVDYLRSRG-------------RSVL--GGDCLLKfsldvceameylegnNFVHRDLAARNVLVS 136
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 198 SaqlDSPLKATDFGLSdfiKPGKRFHDIVG-SAYYVAPEVLK-RRSGPESDVWSIGVITY-ILLCGRRPF 264
Cdd:cd05082 137 E---DNVAKVSDFGLT---KEASSTQDTGKlPVKWTAPEALReKKFSTKSDVWSFGILLWeIYSFGRVPY 200
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
60-277 1.41e-09

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: 58.94  E-value: 1.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRP-NGD----RVAVKRLdkSKMVLPIAVEDVKREVQILIALSgHENVVQFHNAFEDDD 134
Cdd:cd05036   6 KNLTLIRALGQGAFGEVYEGTVSGmPGDpsplQVAVKTL--PELCSEQDEMDFLMEALIMSKFN-HPNIVRCIGVCFQRL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 135 YVYIVMELCEGGEL-----LDRILSKKGNRYSEKDAAVVVRQmlkVAGECHL---HGLVHRDMKPENFLFKSAQLDSPLK 206
Cdd:cd05036  83 PRFILLELMAGGDLksflrENRPRPEQPSSLTMLDLLQLAQD---VAKGCRYleeNHFIHRDIAARNCLLTCKGPGRVAK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 207 ATDFGLSdfikpgkrfHDIVGSAYYvapevlkRRSG----------PE----------SDVWSIGVITY-ILLCGRRPFW 265
Cdd:cd05036 160 IGDFGMA---------RDIYRADYY-------RKGGkamlpvkwmpPEafldgiftskTDVWSFGVLLWeIFSLGYMPYP 223
                       250
                ....*....|..
gi 34098881 266 DRTEdgifKEVL 277
Cdd:cd05036 224 GKSN----QEVM 231
EF-hand_7 pfam13499
EF-hand domain pair;
367-432 1.50e-09

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 54.18  E-value: 1.50e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34098881   367 ISDLRDQFDAIDVDKNGVISLEEMRQALAK-DLPWKLKDSRVAEILEAIDSNTDGLVDFTEFVAAAL 432
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKlEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
68-285 1.67e-09

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: 58.89  E-value: 1.67e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAihRPNGDrVAVKRLdKSKMVLPIAVEDVKREVQILIAlSGHENVVQFHNAFEDDDyVYIVMELCEGGE 147
Cdd:cd14149  20 IGSGSFGTVYKG--KWHGD-VAVKIL-KVVDPTPEQFQAFRNEVAVLRK-TRHVNILLFMGYMTKDN-LAIVTQWCEGSS 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 148 LLDR--ILSKKGNRYSEKDAAvvvRQMLKVAGECHLHGLVHRDMKPENFLFKSAQldsPLKATDFGLSDfIKP----GKR 221
Cdd:cd14149  94 LYKHlhVQETKFQMFQLIDIA---RQTAQGMDYLHAKNIIHRDMKSNNIFLHEGL---TVKIGDFGLAT-VKSrwsgSQQ 166
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34098881 222 FHDIVGSAYYVAPEVLKRR-SGP---ESDVWSIGVITYILLCGRRPFWD-RTEDGIFKEVLRN--KPDFSR 285
Cdd:cd14149 167 VEQPTGSILWMAPEVIRMQdNNPfsfQSDVYSYGIVLYELMTGELPYSHiNNRDQIIFMVGRGyaSPDLSK 237
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
62-275 2.10e-09

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; 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. Genetic variations in TTBK1 are linked to Alzheimer's disease (AD). Hyperphosphorylated tau is a major component of paired helical filaments that accumulate in the brain of AD patients. Studies in transgenic mice show that TTBK1 is involved in the phosphorylation-dependent pathogenic aggregation of tau. The TTBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271032 [Multi-domain]  Cd Length: 262  Bit Score: 58.50  E-value: 2.10e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVK--RLDKSKMVLpiavedvKREVQILIALSGHENVVQFHNAFEDDDYVYIV 139
Cdd:cd14130   2 WKVLKKIGGGGFGEIYEAMDLLTRENVALKveSAQQPKQVL-------KMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 140 MELcEGGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFksAQLDSPLKAT---DFGLS--- 213
Cdd:cd14130  75 MQL-QGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAM--GRLPSTYRKCymlDFGLArqy 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34098881 214 ----DFIKPGKRFHDIVGSAYYVAPEVLKRRS-GPESDVWSIGVITYILLCGRRPfWDRTED----GIFKE 275
Cdd:cd14130 152 tnttGEVRPPRNVAGFRGTVRYASVNAHKNREmGRHDDLWSLFYMLVEFAVGQLP-WRKIKDkeqvGMIKE 221
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
68-263 2.35e-09

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: 58.30  E-value: 2.35e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRPNGdRVAVKRLDKSKmvlpIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVMELCEGGe 147
Cdd:cd14156   1 IGSGFFSKVYKVTHGATG-KVMVVKIYKND----VDQHKIVREISLLQKLS-HPNIVRYLGICVKDEKLHPILEYVSGG- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 148 LLDRILSKKGNRYSEKD----AAVVVRQMLKVagecHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLSDFI-----KP 218
Cdd:cd14156  74 CLEELLAREELPLSWREkvelACDISRGMVYL----HSKNIYHRDLNSKNCLIRVTPRGREAVVTDFGLAREVgempaND 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 34098881 219 GKRFHDIVGSAYYVAPEVLkrRSGP---ESDVWSIGvityILLC---GRRP 263
Cdd:cd14156 150 PERKLSLVGSAFWMAPEML--RGEPydrKVDVFSFG----IVLCeilARIP 194
STKc_CK1_alpha cd14128
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze ...
62-224 2.65e-09

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; 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. CK1alpha plays a role in cell cycle progression, spindle dynamics, and chromosome segregation. It is also involved in regulating apoptosis mediated by Fas or the retinoid X receptor (RXR), and is a positive regulator of Wnt signaling. CK1alpha phosphorylates the NS5A protein of flaviviruses such as the Hepatitis C virus (HCV) and yellow fever virus (YFV), and influences flaviviral replication. The CK1 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: 271030 [Multi-domain]  Cd Length: 266  Bit Score: 58.29  E-value: 2.65e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKrLDKSKMVLPiaveDVKREVQILIALSGHENVVQFHNAFEDDDYVYIVME 141
Cdd:cd14128   2 YRLVRKIGSGSFGDIYLGINITNGEEVAVK-LESQKARHP----QLLYESKLYKILQGGVGIPHIRWYGQEKDYNVLVMD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCegGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLSdfikpgKR 221
Cdd:cd14128  77 LL--GPSLEDLFNFCSRRFTMKTVLMLADQMIGRIEYVHNKNFIHRDIKPDNFLMGIGRHCNKLFLIDFGLA------KK 148

                ...
gi 34098881 222 FHD 224
Cdd:cd14128 149 YRD 151
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
109-317 3.19e-09

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: 58.02  E-value: 3.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 109 REVQILIALSGHENVVQFHNAFEDDdYVYIVMELCEGGELLDRILSKKGNRYSEKDAAV-----VVRQMLKVAGECHLHG 183
Cdd:cd14020  52 KERAALEQLQGHRNIVTLYGVFTNH-YSANVPSRCLLLELLDVSVSELLLRSSNQGCSMwmiqhCARDVLEALAFLHHEG 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 184 LVHRDMKPENFLFkSAQlDSPLKATDFGLSdfIKPGKRFHDIVGSAYYVAPEVLKRRS----GPES--------DVWSIG 251
Cdd:cd14020 131 YVHADLKPRNILW-SAE-DECFKLIDFGLS--FKEGNQDVKYIQTDGYRAPEAELQNClaqaGLQSetectsavDLWSLG 206
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34098881 252 VITYILLCG-------RRPFWDRTE----DGIF-KEVLRNKpdfsrkpwATISDSAKDFVKKLLVKDPRARLTAAQAL 317
Cdd:cd14020 207 IVLLEMFSGmklkhtvRSQEWKDNSsaiiDHIFaSNAVVNP--------AIPAYHLRDLIKSMLHNDPGKRATAEAAL 276
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
60-274 3.35e-09

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: 58.10  E-value: 3.35e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVA------IHRPNG-DRVAVKRL--DKSKMVLpiavEDVKREVQILIALSGHENVVQFHNAF 130
Cdd:cd05098  13 DRLVLGKPLGEGCFGQVVLAeaigldKDKPNRvTKVAVKMLksDATEKDL----SDLISEMEMMKMIGKHKNIINLLGAC 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 131 EDDDYVYIVMELCEGGELLDRILSKK--GNRY------------SEKD----AAVVVRQMLKVAG-EChlhglVHRDMKP 191
Cdd:cd05098  89 TQDGPLYVIVEYASKGNLREYLQARRppGMEYcynpshnpeeqlSSKDlvscAYQVARGMEYLASkKC-----IHRDLAA 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 192 ENFLFKSaqlDSPLKATDFGLSDFIKPGKRFHDIVGS---AYYVAPEVL-KRRSGPESDVWSIGVITY-ILLCGRRPFWD 266
Cdd:cd05098 164 RNVLVTE---DNVMKIADFGLARDIHHIDYYKKTTNGrlpVKWMAPEALfDRIYTHQSDVWSFGVLLWeIFTLGGSPYPG 240

                ....*...
gi 34098881 267 RTEDGIFK 274
Cdd:cd05098 241 VPVEELFK 248
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
66-291 3.58e-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: 58.11  E-value: 3.58e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDR----VAVKRLDKSKMvlPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDyVYIVME 141
Cdd:cd05108  13 KVLGSGAFGTVYKGLWIPEGEKvkipVAIKELREATS--PKANKEILDEAYVMASVD-NPHVCRLLGICLTST-VQLITQ 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELLDRILSKKGNRYSEKDAAVVVrQMLKVAGECHLHGLVHRDMKPENFLFKSAQldsPLKATDFGLSDFIKPGKR 221
Cdd:cd05108  89 LMPFGCLLDYVREHKDNIGSQYLLNWCV-QIAKGMNYLEDRRLVHRDLAARNVLVKTPQ---HVKITDFGLAKLLGAEEK 164
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34098881 222 FHDIVGSAY---YVAPE-VLKRRSGPESDVWSIGVITYILLC-GRRPFwdrteDGI----FKEVLRNKPDFSRKPWATI 291
Cdd:cd05108 165 EYHAEGGKVpikWMALEsILHRIYTHQSDVWSYGVTVWELMTfGSKPY-----DGIpaseISSILEKGERLPQPPICTI 238
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
120-264 3.93e-09

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: 57.67  E-value: 3.93e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 120 HENVVQFHNAFEDDDYVYIVMELCEGGELLDRILSKKGNRYSEKDAAVVvRQMLKVAGECHLHGLVHRDMKPENFLFKSA 199
Cdd:cd14152  55 HENVVLFMGACMHPPHLAIITSFCKGRTLYSFVRDPKTSLDINKTRQIA-QEIIKGMGYLHAKGIVHKDLKSKNVFYDNG 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 200 QldspLKATDFGL---SDFIKPGKRFHDIV---GSAYYVAPEVLkRRSGP-----------ESDVWSIGVITYILLCGRR 262
Cdd:cd14152 134 K----VVITDFGLfgiSGVVQEGRRENELKlphDWLCYLAPEIV-REMTPgkdedclpfskAADVYAFGTIWYELQARDW 208

                ..
gi 34098881 263 PF 264
Cdd:cd14152 209 PL 210
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
66-253 4.89e-09

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: 57.67  E-value: 4.89e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRpnGDRVAVKRLDKSKMvlpiavEDVKREVQIL-IALSGHENVVQFHNAfedDDY-------VY 137
Cdd:cd14056   1 KTIGKGRYGEVWLGKYR--GEKVAVKIFSSRDE------DSWFRETEIYqTVMLRHENILGFIAA---DIKstgswtqLW 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 138 IVMELCEGGELLDRIlskkgnRYSEKDAAVVVRQMLKVA-GECHLH----------GLVHRDMKPENFLFKSaqlDSPLK 206
Cdd:cd14056  70 LITEYHEHGSLYDYL------QRNTLDTEEALRLAYSAAsGLAHLHteivgtqgkpAIAHRDLKSKNILVKR---DGTCC 140
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34098881 207 ATDFGL-------SDFIKPGkrFHDIVGSAYYVAPEVLKRRSGPES-------DVWSIGVI 253
Cdd:cd14056 141 IADLGLavrydsdTNTIDIP--PNPRVGTKRYMAPEVLDDSINPKSfesfkmaDIYSFGLV 199
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
66-264 4.98e-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: 4.98e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDR----VAVKRLDKSKMvlPIAVEDVKREVQILIALsGHENVVQFHNAFEDDDyVYIVME 141
Cdd:cd05109  13 KVLGSGAFGTVYKGIWIPDGENvkipVAIKVLRENTS--PKANKEILDEAYVMAGV-GSPYVCRLLGICLTST-VQLVTQ 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELLDRILSKKGnRYSEKDAAVVVRQMLKvaGECHLHG--LVHRDMKPENFLFKSAqldSPLKATDFGLSDFIK-P 218
Cdd:cd05109  89 LMPYGCLLDYVRENKD-RIGSQDLLNWCVQIAK--GMSYLEEvrLVHRDLAARNVLVKSP---NHVKITDFGLARLLDiD 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 GKRFHDIVGSA---YYVAPEVLKRRSGPESDVWSIGVITYILLC-GRRPF 264
Cdd:cd05109 163 ETEYHADGGKVpikWMALESILHRRFTHQSDVWSYGVTVWELMTfGAKPY 212
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
60-264 5.15e-09

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: 57.67  E-value: 5.15e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVA----IHRPNGDR---VAVKRLDKSKMVLPIAveDVKREVQILIALSGHENVVQFHNAFED 132
Cdd:cd05099  12 DRLVLGKPLGEGCFGQVVRAeaygIDKSRPDQtvtVAVKMLKDNATDKDLA--DLISEMELMKLIGKHKNIINLLGVCTQ 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 133 DDYVYIVMELCEGGELLDRILSKK---------GNRYSE-----KDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKS 198
Cdd:cd05099  90 EGPLYVIVEYAAKGNLREFLRARRppgpdytfdITKVPEeqlsfKDLVSCAYQVARGMEYLESRRCIHRDLAARNVLVTE 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 199 aqlDSPLKATDFGLSdfikpgKRFHDIvgsAYY------------VAPEVL-KRRSGPESDVWSIGVITY-ILLCGRRPF 264
Cdd:cd05099 170 ---DNVMKIADFGLA------RGVHDI---DYYkktsngrlpvkwMAPEALfDRVYTHQSDVWSFGILMWeIFTLGGSPY 237
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
64-264 6.39e-09

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: 57.28  E-value: 6.39e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  64 IGKLLGHGQFGYTY--VAIH---RPNGDRVAVKRLDKSKMvlPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYI 138
Cdd:cd05045   4 LGKTLGEGEFGKVVkaTAFRlkgRAGYTTVAVKMLKENAS--SSELRDLLSEFNLLKQVN-HPHVIKLYGACSQDGPLLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 139 VMELCEGGELLDRI-LSKK---------GNRYSEKD-----AAVVVRQMLKVA-----GECHLH--GLVHRDMKPENFLF 196
Cdd:cd05045  81 IVEYAKYGSLRSFLrESRKvgpsylgsdGNRNSSYLdnpdeRALTMGDLISFAwqisrGMQYLAemKLVHRDLAARNVLV 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34098881 197 KSAQLdspLKATDFGLSDFIKPG----KRFHDIVgSAYYVAPEVL-KRRSGPESDVWSIGVITY-ILLCGRRPF 264
Cdd:cd05045 161 AEGRK---MKISDFGLSRDVYEEdsyvKRSKGRI-PVKWMAIESLfDHIYTTQSDVWSFGVLLWeIVTLGGNPY 230
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
62-260 7.57e-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: 57.46  E-value: 7.57e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKskmvLPIAVEDVKREVQILIALSGHE----NVVQFHNAFEDDDYVY 137
Cdd:cd14211   1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKN----HPSYARQGQIEVSILSRLSQENadefNFVRAYECFQHKNHTC 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 138 IVMELCEGgELLDRIlskKGNRYSE---KDAAVVVRQMLKVAGECHLHGLVHRDMKPEN-FLFKSAQLDSPLKATDFG-L 212
Cdd:cd14211  77 LVFEMLEQ-NLYDFL---KQNKFSPlplKYIRPILQQVLTALLKLKSLGLIHADLKPENiMLVDPVRQPYRVKVIDFGsA 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 34098881 213 SDFIKPGKRFHdiVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCG 260
Cdd:cd14211 153 SHVSKAVCSTY--LQSRYYRAPEIILGLPFCEAiDMWSLGCVIAELFLG 199
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
62-260 7.75e-09

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


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 57.35  E-value: 7.75e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSkmvlPIAVEDVKREVQILIALSGHE----NVVQFHNAFEDDDYVY 137
Cdd:cd14229   2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNH----PSYARQGQIEVGILARLSNENadefNFVRAYECFQHRNHTC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 138 IVMELCEGgELLDRIlskKGNRYSEKDAAVV---VRQMLKVAGECHLHGLVHRDMKPEN-FLFKSAQLDSPLKATDFGLS 213
Cdd:cd14229  78 LVFEMLEQ-NLYDFL---KQNKFSPLPLKVIrpiLQQVATALKKLKSLGLIHADLKPENiMLVDPVRQPYRVKVIDFGSA 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 34098881 214 DFIKPGKrFHDIVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCG 260
Cdd:cd14229 154 SHVSKTV-CSTYLQSRYYRAPEIILGLPFCEAiDMWSLGCVIAELFLG 200
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
62-224 9.86e-09

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: 56.61  E-value: 9.86e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKrldkskmvlpiaVEDVK-REVQILIA------LSGHENVVQFHNAFEDDD 134
Cdd:cd14125   2 YRLGRKIGSGSFGDIYLGTNIQTGEEVAIK------------LESVKtKHPQLLYEsklykiLQGGVGIPNVRWYGVEGD 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 135 YVYIVMELCegGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSPLKATDFGLSd 214
Cdd:cd14125  70 YNVMVMDLL--GPSLEDLFNFCSRKFSLKTVLMLADQMISRIEYVHSKNFIHRDIKPDNFLMGLGKKGNLVYIIDFGLA- 146
                       170
                ....*....|
gi 34098881 215 fikpgKRFHD 224
Cdd:cd14125 147 -----KKYRD 151
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
66-237 1.15e-08

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


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 56.57  E-value: 1.15e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAihRPNGDRVAVKrldkskmVLPIAVED---VKREVQILIALSgHENVVQFHNA-----FEDDDYvY 137
Cdd:cd14053   1 EIKARGRFGAVWKA--QYLNRLVAVK-------IFPLQEKQswlTEREIYSLPGMK-HENILQFIGAekhgeSLEAEY-W 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 138 IVMELCEGGELLDRIlskKGNRYSEKdaavvvrQMLKVA-----GECHLH------------GLVHRDMKPENFLFKSaq 200
Cdd:cd14053  70 LITEFHERGSLCDYL---KGNVISWN-------ELCKIAesmarGLAYLHedipatngghkpSIAHRDFKSKNVLLKS-- 137
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 34098881 201 lDSPLKATDFGLSDFIKPGKRF---HDIVGSAYYVAPEVL 237
Cdd:cd14053 138 -DLTACIADFGLALKFEPGKSCgdtHGQVGTRRYMAPEVL 176
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
369-499 1.19e-08

Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+.


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 54.46  E-value: 1.19e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 369 DLRDQFDAIDVDKNGVISLEEMRQALAKDLPWKLKDSRVAEILEAIDSNTDGLVDFTEFVaaALHvHQLEEhdsekWqlr 448
Cdd:cd16180   1 ELRRIFQAVDRDRSGRISAKELQRALSNGDWTPFSIETVRLMINMFDRDRSGTINFDEFV--GLW-KYIQD-----W--- 69
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 34098881 449 sRAAFEKFDLDKDGYITPEELR---MHTGLRGS---IDPLLDEADIDRDGKISLHEF 499
Cdd:cd16180  70 -RRLFRRFDRDRSGSIDFNELQnalSSFGYRLSpqfVQLLVRKFDRRRRGSISFDDF 125
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
71-258 1.47e-08

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


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 56.19  E-value: 1.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  71 GQFGYTYVAihRPNGDRVAVKrldkskmVLPIAVEDVKREVQILIALSG--HENVVQFHNAFED----DDYVYIVMELCE 144
Cdd:cd14140   6 GRFGCVWKA--QLMNEYVAVK-------IFPIQDKQSWQSEREIFSTPGmkHENLLQFIAAEKRgsnlEMELWLITAFHD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 145 GGELLDRIlskKGNRYSEKDAAVVVRQMLK-----------VAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFGLS 213
Cdd:cd14140  77 KGSLTDYL---KGNIVSWNELCHIAETMARglsylhedvprCKGEGHKPAIAHRDFKSKNVLLKN---DLTAVLADFGLA 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 34098881 214 DFIKPGK---RFHDIVGSAYYVAPEVL------KRRSGPESDVWSIGVITYILL 258
Cdd:cd14140 151 VRFEPGKppgDTHGQVGTRRYMAPEVLegainfQRDSFLRIDMYAMGLVLWELV 204
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
66-270 1.51e-08

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: 55.93  E-value: 1.51e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVA----IHRPNGDR-VAVKRLDKSKMvlPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDYVYIVM 140
Cdd:cd05046  11 TTLGRGEFGEVFLAkakgIEEEGGETlVLVKALQKTKD--ENLQSEFRRELDMFRKLS-HKNVVRLLGLCREAEPHYMIL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCEGGELLDRILSKKGNRYSEKDAAVVVRQMLKVA-----GECHL--HGLVHRDMKPENFLFkSAQLDspLKATDFGLS 213
Cdd:cd05046  88 EYTDLGDLKQFLRATKSKDEKLKPPPLSTKQKVALCtqialGMDHLsnARFVHRDLAARNCLV-SSQRE--VKVSLLSLS 164
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 214 dfikpgkrfHDIVGSAYY-----------VAPE-VLKRRSGPESDVWSIGVITY-ILLCGRRPFWDRTED 270
Cdd:cd05046 165 ---------KDVYNSEYYklrnaliplrwLAPEaVQEDDFSTKSDVWSFGVLMWeVFTQGELPFYGLSDE 225
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
370-470 1.52e-08

EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 53.44  E-value: 1.52e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 370 LRDQFDAIDVDKNGVISLEEMRQALAKDLPwKLKDSRVAEILEAIDSNTDGLVDFTEFVAAalhVHQLEEHDSekwqLRS 449
Cdd:cd15898   2 LRRQWIKADKDGDGKLSLKEIKKLLKRLNI-RVSEKELKKLFKEVDTNGDGTLTFDEFEEL---YKSLTERPE----LEP 73
                        90       100
                ....*....|....*....|.
gi 34098881 450 raAFEKFDLDKDGYITPEELR 470
Cdd:cd15898  74 --IFKKYAGTNRDYMTLEEFI 92
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
60-264 2.44e-08

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: 55.79  E-value: 2.44e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAihrpngDRVAVKRlDKSKMVLPIAVE------------DVKREVQILIALSGHENVVQFH 127
Cdd:cd05101  24 DKLTLGKPLGEGCFGQVVMA------EAVGIDK-DKPKEAVTVAVKmlkddatekdlsDLVSEMEMMKMIGKHKNIINLL 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 128 NAFEDDDYVYIVMELCEGGELLDRILSKK--GNRYSEKDAAVVVRQM-LKVAGECHLH---GL--------VHRDMKPEN 193
Cdd:cd05101  97 GACTQDGPLYVIVEYASKGNLREYLRARRppGMEYSYDINRVPEEQMtFKDLVSCTYQlarGMeylasqkcIHRDLAARN 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 194 FLFKSAQLdspLKATDFGLSdfikpgkrfHDIVGSAYY------------VAPEVL-KRRSGPESDVWSIGVITY-ILLC 259
Cdd:cd05101 177 VLVTENNV---MKIADFGLA---------RDINNIDYYkkttngrlpvkwMAPEALfDRVYTHQSDVWSFGVLMWeIFTL 244

                ....*
gi 34098881 260 GRRPF 264
Cdd:cd05101 245 GGSPY 249
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
62-260 4.75e-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: 55.10  E-value: 4.75e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSkmvlPIAVEDVKREVQILIALSGHE----NVVQFHNAFEDDDYVY 137
Cdd:cd14227  17 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNH----PSYARQGQIEVSILARLSTESaddyNFVRAYECFQHKNHTC 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 138 IVMELCEGgELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPEN-FLFKSAQLDSPLKATDFGLSDFI 216
Cdd:cd14227  93 LVFEMLEQ-NLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENiMLVDPSRQPYRVKVIDFGSASHV 171
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 34098881 217 KPGKrFHDIVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCG 260
Cdd:cd14227 172 SKAV-CSTYLQSRYYRAPEIILGLPFCEAiDMWSLGCVIAELFLG 215
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
68-264 4.76e-08

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: 54.31  E-value: 4.76e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHrpNGD-RVAVKRLDKSKMvlpiAVEDVKREVQILIALSgHENVVQFHnAFEDDDYVYIVMELCEGG 146
Cdd:cd05071  17 LGQGCFGEVWMGTW--NGTtRVAIKTLKPGTM----SPEAFLQEAQVMKKLR-HEKLVQLY-AVVSEEPIYIVTEYMSKG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 147 ELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLdspLKATDFGLSDFI-------KPG 219
Cdd:cd05071  89 SLLDFLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLV---CKVADFGLARLIedneytaRQG 165
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 34098881 220 KRFhdivgSAYYVAPEV-LKRRSGPESDVWSIGV-ITYILLCGRRPF 264
Cdd:cd05071 166 AKF-----PIKWTAPEAaLYGRFTIKSDVWSFGIlLTELTTKGRVPY 207
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
153-258 4.99e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 54.88  E-value: 4.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  153 LSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAqldSPLKATDFGLSDFIKPGKRFHDIVGSAYYV 232
Cdd:PHA03209 147 LTKRSRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDV---DQVCIGDLGAAQFPVVAPAFLGLAGTVETN 223
                         90       100
                 ....*....|....*....|....*..
gi 34098881  233 APEVLKR-RSGPESDVWSIGVITYILL 258
Cdd:PHA03209 224 APEVLARdKYNSKADIWSAGIVLFEML 250
EFh_CREC_RCN3 cd16230
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ...
371-498 5.24e-08

EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand calcium-binding protein RLP49, is a putative six EF-hand Ca2+-binding protein that contains five RXXR (X is any amino acid) motifs and a C-terminal ER retrieval signal His-Asp-Glu-Leu (HDEL) tetrapeptide. The RXXR motif represents the target sequence of subtilisin-like proprotein convertases (SPCs). RCN-3 is specifically bound to the paired basic amino-acid-cleaving enzyme-4 (PACE4) precursor protein and plays an important role in the biosynthesis of PACE4.


Pssm-ID: 320028 [Multi-domain]  Cd Length: 268  Bit Score: 54.21  E-value: 5.24e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 371 RDQ--FDAIDVDKNGVISLEEMRQAL-AKDLPwKLKDSRVAEILEAIDSNTDGLVDFTEFVAAALHVHQLEEHdsEKWQL 447
Cdd:cd16230 124 RDErrFRVADQDGDSMATREELTAFLhPEEFP-HMRDIVVAETLEDLDKNKDGYVQVEEYIADLYSGEPGEEE--PAWVQ 200
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 34098881 448 RSRAAFEKF-DLDKDGYITPEELRmHTGLRGSID-------PLLDEADIDRDGKISLHE 498
Cdd:cd16230 201 TERQQFRQFrDLNKDGRLDGSEVG-HWVLPPSQDqplveanHLLHESDTDKDGRLSKAE 258
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
67-292 6.45e-08

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: 53.89  E-value: 6.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  67 LLGHGQFGYTYVAIHRPNGDRV--AVKRLDKskmvlpIAVEDVKR----EVQILIALSGHENVVQFHNAFEDDDYVYIVM 140
Cdd:cd05047   2 VIGEGNFGQVLKARIKKDGLRMdaAIKRMKE------YASKDDHRdfagELEVLCKLGHHPNIINLLGACEHRGYLYLAI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCEGGELLDRIlskKGNRYSEKDAAVVV----------RQMLKVAGECH--LHGL-----VHRDMKPENFLFKSAQLds 203
Cdd:cd05047  76 EYAPHGNLLDFL---RKSRVLETDPAFAIanstastlssQQLLHFAADVArgMDYLsqkqfIHRDLAARNILVGENYV-- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 204 pLKATDFGLSD----FIKP--GK---RFHDIVGSAYYVAPEvlkrrsgpESDVWSIGVITY-ILLCGRRPFWDRT----- 268
Cdd:cd05047 151 -AKIADFGLSRgqevYVKKtmGRlpvRWMAIESLNYSVYTT--------NSDVWSYGVLLWeIVSLGGTPYCGMTcaely 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 34098881 269 ---------------EDGIF---KEVLRNKPdFSRKPWATIS 292
Cdd:cd05047 222 eklpqgyrlekplncDDEVYdlmRQCWREKP-YERPSFAQIL 262
EF-hand_7 pfam13499
EF-hand domain pair;
450-504 6.50e-08

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 49.56  E-value: 6.50e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34098881   450 RAAFEKFDLDKDGYITPEELR-MHTGLRGSIDP-------LLDEADIDRDGKISLHEFRRLLR 504
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKkLLRKLEEGEPLsdeeveeLFKEFDLDKDGRISFEEFLELYS 67
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
62-261 7.31e-08

Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 and BubR1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Bub1 (Budding uninhibited by benzimidazoles 1), BubR1, and similar proteins. They contain an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. Bub1 and BubR1 are involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Impaired SAC leads to genomic instabilities and tumor development. Bub1 and BubR1 facilitate the localization of SAC proteins to kinetochores and regulate kinetochore-microtubule (K-MT) attachments. Repression studies of Bub1 and BubR1 show that they exert an additive effect in misalignment phenotypes and may function cooperatively or in parallel pathways in regulating K-MT attachments. The Bub1/BubR1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 53.90  E-value: 7.31e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHrpnGDRVAVKRLDKSKMVLPIAVEDVKREVQI---LIALSGHENVVQFHNAFEDDDYVYI 138
Cdd:cd13981   2 YVISKELGEGGYASVYLAKD---DDEQSDGSLVALKVEKPPSIWEFYICDQLhsrLKNSRLRESISGAHSAHLFQDESIL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 139 VMELCEGGELLDRILSKKGNRYSEKDAAVV---VRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLDSP----------- 204
Cdd:cd13981  79 VMDYSSQGTLLDVVNKMKNKTGGGMDEPLAmffTIELLKVVEALHEVGIIHGDIKPDNFLLRLEICADWpgegengwlsk 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34098881 205 -LKATDFGLS-DF--IKPGKRFHDIVGSAYYVAPEVLKRRSGP-ESDVWSIGVITYILLCGR 261
Cdd:cd13981 159 gLKLIDFGRSiDMslFPKNQSFKADWHTDSFDCIEMREGRPWTyQIDYFGIAATIHVMLFGK 220
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
60-318 7.37e-08

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: 53.89  E-value: 7.37e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTY--VAIHRPNGD---RVAVKRL-DKSKMVLPIAVedvKREVQILIALSGHeNVVQFHNAFEDD 133
Cdd:cd05032   6 EKITLIRELGQGSFGMVYegLAKGVVKGEpetRVAIKTVnENASMRERIEF---LNEASVMKEFNCH-HVVRLLGVVSTG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 134 DYVYIVMELCEGGELLDRILSKK-GNRYSEKDAAVVVRQMLKVAGE-----CHLHGL--VHRDMKPENFLFKSaqlDSPL 205
Cdd:cd05032  82 QPTLVVMELMAKGDLKSYLRSRRpEAENNPGLGPPTLQKFIQMAAEiadgmAYLAAKkfVHRDLAARNCMVAE---DLTV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 206 KATDFGLSdfikpgkrfHDIVGSAYY------------VAPEVLKrrSG---PESDVWSIGVITY-ILLCGRRPFWDRTE 269
Cdd:cd05032 159 KIGDFGMT---------RDIYETDYYrkggkgllpvrwMAPESLK--DGvftTKSDVWSFGVVLWeMATLAEQPYQGLSN 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 34098881 270 DGIFKEVLR----NKPDFSRKPWAtisdsakDFVKKLLVKDPRARLTAAQALS 318
Cdd:cd05032 228 EEVLKFVIDgghlDLPENCPDKLL-------ELMRMCWQYNPKMRPTFLEIVS 273
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
66-314 7.40e-08

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


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 53.92  E-value: 7.40e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDR----VAVK--RLDKSKmvlpiaveDVKREVQILIALS-GHENVVQFHNAFE-----DD 133
Cdd:cd14055   1 KLVGKGRFAEVWKAKLKQNASGqyetVAVKifPYEEYA--------SWKNEKDIFTDASlKHENILQFLTAEErgvglDR 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 134 DYvYIVMELCEGGELLDRIlskKGNRYSEKDAAVVVRQMlkVAGECHLHG-----------LVHRDMKPENFLFKSaqlD 202
Cdd:cd14055  73 QY-WLITAYHENGSLQDYL---TRHILSWEDLCKMAGSL--ARGLAHLHSdrtpcgrpkipIAHRDLKSSNILVKN---D 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 203 SPLKATDFGLSDFIKPGKRFHDI-----VGSAYYVAPEVLKRR-------SGPESDVWSIGVITYILL--C--------- 259
Cdd:cd14055 144 GTCVLADFGLALRLDPSLSVDELansgqVGTARYMAPEALESRvnledleSFKQIDVYSMALVLWEMAsrCeasgevkpy 223
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34098881 260 --------GRRPFWDRTEDGIFKEvlRNKPDFSRKpWATisDSAKDFVKKLLVK----DPRARLTAA 314
Cdd:cd14055 224 elpfgskvRERPCVESMKDLVLRD--RGRPEIPDS-WLT--HQGMCVLCDTITEcwdhDPEARLTAS 285
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
19-253 8.38e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 54.70  E-value: 8.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881   19 SSQTKSKAAPTpiDTKASTKRRTGSIPCGKrTDFGYSKDFHDHYTIGKLLGHGQFGYTYV-AIHRPNGDRVAVKRLD--- 94
Cdd:PHA03210 110 SGAEDSDASHL--DFDEAPPDAAGPVPLAQ-AKLKHDDEFLAHFRVIDDLPAGAFGKIFIcALRASTEEAEARRGVNstn 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881   95 ----KSKMVLPIAVEDVKR-----EVQIL-IALSGHENVVQFHNAFEDDDYVYIVMELCE---GGELLDRILSKKgNRYS 161
Cdd:PHA03210 187 qgkpKCERLIAKRVKAGSRaaiqlENEILaLGRLNHENILKIEEILRSEANTYMITQKYDfdlYSFMYDEAFDWK-DRPL 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  162 EKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSaqlDSPLKATDFG-LSDFIKPGKRF-HDIVGSAYYVAPEVLKR 239
Cdd:PHA03210 266 LKQTRAIMKQLLCAVEYIHDKKLIHRDIKLENIFLNC---DGKIVLGDFGtAMPFEKEREAFdYGWVGTVATNSPEILAG 342
                        250
                 ....*....|....*
gi 34098881  240 RSGPE-SDVWSIGVI 253
Cdd:PHA03210 343 DGYCEiTDIWSCGLI 357
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
60-260 8.76e-08

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


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 54.32  E-value: 8.76e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRPNGDRVAVKRLDKSkmvlPIAVEDVKREVQILIALSGHE----NVVQFHNAFEDDDY 135
Cdd:cd14228  15 NSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNH----PSYARQGQIEVSILSRLSSENadeyNFVRSYECFQHKNH 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 136 VYIVMELCEGgELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPEN-FLFKSAQLDSPLKATDFGLSD 214
Cdd:cd14228  91 TCLVFEMLEQ-NLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENiMLVDPVRQPYRVKVIDFGSAS 169
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 34098881 215 FIKPGKrFHDIVGSAYYVAPEVLKRRSGPES-DVWSIGVITYILLCG 260
Cdd:cd14228 170 HVSKAV-CSTYLQSRYYRAPEIILGLPFCEAiDMWSLGCVIAELFLG 215
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
166-322 1.05e-07

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


Pssm-ID: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 53.60  E-value: 1.05e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 166 AVVVRQMLKVAGECHLHGLVHRDMKPENFLFksAQLDSPLKATDFGLSDFIKPGKRF--HDIVGSAYYVAPE-------- 235
Cdd:cd14013 123 KSIMRQILVALRKLHSTGIVHRDVKPQNIIV--SEGDGQFKIIDLGAAADLRIGINYipKEFLLDPRYAPPEqyimstqt 200
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 236 --------------VLKRRSGPES-DVWSIGVItYILLC--------GRRPF--------WD------RTEDGIFKEVlr 278
Cdd:cd14013 201 psappapvaaalspVLWQMNLPDRfDMYSAGVI-LLQMAfpnlrsdsNLIAFnrqlkqcdYDlnawrmLVEPRASADL-- 277
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 34098881 279 nKPDFS------RKPWatisdsakDFVKKLLVKDPRARLTAAQALSHAWV 322
Cdd:cd14013 278 -REGFEildlddGAGW--------DLVTKLIRYKPRGRLSASAALAHPYF 318
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
363-498 1.13e-07

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This family corresponds to a group of uncharacterized RCN2-like proteins, which are mainly found in protostomes. Although their biological function remains unclear, they show high sequence similarity with RCN2 (also known as E6BP or TCBP-49), which is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. Members in this family contain six copies of the EF-hand Ca2+-binding motif, but may lack a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320025 [Multi-domain]  Cd Length: 263  Bit Score: 53.09  E-value: 1.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 363 DEAEISDLRDQFDAIDVDKNGVISLEEMRQALAkdlPWKLKDSRVAEI---LEAIDSNTDGLVDFTEFVAAALHvhqleE 439
Cdd:cd16227 117 DLKLLEDDKEMFEAADLNKDGKLDKTEFSAFQH---PEEYPHMHPVLIeqtLRDKDKDNDGFISFQEFLGDRAG-----H 188
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34098881 440 HDSEkWQLRSRAAFEK-FDLDKDGYITPEELR------MHTGLRGSIDPLLDEADIDRDGKISLHE 498
Cdd:cd16227 189 EDKE-WLLVEKDRFDEdYDKDGDGKLDGEEILswlvpdNEEIAEEEVDHLFASADDDHDDRLSFDE 253
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
58-255 1.21e-07

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: 53.48  E-value: 1.21e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  58 FHDHYTIGKLLGHGQFGYTYVAI-HRPNGDRVA---VKRLDKSKmvlpiavEDVKREVQIL--IALSGHEN---VVQFHN 128
Cdd:cd14215  10 LQERYEIVSTLGEGTFGRVVQCIdHRRGGARVAlkiIKNVEKYK-------EAARLEINVLekINEKDPENknlCVQMFD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 129 AFEDDDYVYIVMELCeGGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLD------ 202
Cdd:cd14215  83 WFDYHGHMCISFELL-GLSTFDFLKENNYLPYPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVNSDYEltynle 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34098881 203 ----------SPLKATDFGLSDFikPGKRFHDIVGSAYYVAPEVLKRRSGPES-DVWSIGVITY 255
Cdd:cd14215 162 kkrdersvksTAIRVVDFGSATF--DHEHHSTIVSTRHYRAPEVILELGWSQPcDVWSIGCIIF 223
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
68-312 1.49e-07

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: 53.15  E-value: 1.49e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHrpNGD-RVAVKRLDKSKMvLPiavEDVKREVQILIALSgHENVVQFHnAFEDDDYVYIVMELCEGG 146
Cdd:cd05069  20 LGQGCFGEVWMGTW--NGTtKVAIKTLKPGTM-MP---EAFLQEAQIMKKLR-HDKLVPLY-AVVSEEPIYIVTEFMGKG 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 147 ELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAQLdspLKATDFGLSDFIKPGKrFHDIV 226
Cdd:cd05069  92 SLLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLV---CKIADFGLARLIEDNE-YTARQ 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 227 GSAY---YVAPEV-LKRRSGPESDVWSIGVI-TYILLCGRRPFWDRTEDGIFKEVLRNkpdfSRKPWAT-ISDSAKDFVK 300
Cdd:cd05069 168 GAKFpikWTAPEAaLYGRFTIKSDVWSFGILlTELVTKGRVPYPGMVNREVLEQVERG----YRMPCPQgCPESLHELMK 243
                       250
                ....*....|..
gi 34098881 301 KLLVKDPRARLT 312
Cdd:cd05069 244 LCWKKDPDERPT 255
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
60-264 2.40e-07

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: 52.42  E-value: 2.40e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGY----TYVAI--HRPNGDRVAVKRLDKSKMVLPIAveDVKREVQILIALSGHENVVQFHNAFEDD 133
Cdd:cd05053  12 DRLTLGKPLGEGAFGQvvkaEAVGLdnKPNEVVTVAVKMLKDDATEKDLS--DLVSEMEMMKMIGKHKNIINLLGACTQD 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 134 DYVYIVMELCEGGELLDRILSKKG-NRYSEKDAAVVVRQMLK----------VA-GECHLHG--LVHRDMKPENFLFKSa 199
Cdd:cd05053  90 GPLYVVVEYASKGNLREFLRARRPpGEEASPDDPRVPEEQLTqkdlvsfayqVArGMEYLASkkCIHRDLAARNVLVTE- 168
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34098881 200 qlDSPLKATDFGLSDFIkpgkrfHDIvgsAYY------------VAPEVL-KRRSGPESDVWSIGVITY-ILLCGRRPF 264
Cdd:cd05053 169 --DNVMKIADFGLARDI------HHI---DYYrkttngrlpvkwMAPEALfDRVYTHQSDVWSFGVLLWeIFTLGGSPY 236
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
60-277 2.51e-07

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 52.28  E-value: 2.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  60 DHYTIGKLLGHGQFGYTYVAIHRP--NGD---RVAVKRLDKSKMvLPIAVEDVKrEVQILIALSGHeNVVQFHNAFEDDD 134
Cdd:cd05061   6 EKITLLRELGQGSFGMVYEGNARDiiKGEaetRVAVKTVNESAS-LRERIEFLN-EASVMKGFTCH-HVVRLLGVVSKGQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 135 YVYIVMELCEGGELLDRILSKKGNrySEKDA---AVVVRQMLKVAGE-----CHLHG--LVHRDMKPENFLFKSaqlDSP 204
Cdd:cd05061  83 PTLVVMELMAHGDLKSYLRSLRPE--AENNPgrpPPTLQEMIQMAAEiadgmAYLNAkkFVHRDLAARNCMVAH---DFT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 205 LKATDFGLSdfikpgkrfHDIVGSAYY------------VAPEVLKRRS-GPESDVWSIGVITY-ILLCGRRPFWDRTED 270
Cdd:cd05061 158 VKIGDFGMT---------RDIYETDYYrkggkgllpvrwMAPESLKDGVfTTSSDMWSFGVVLWeITSLAEQPYQGLSNE 228

                ....*..
gi 34098881 271 GIFKEVL 277
Cdd:cd05061 229 QVLKFVM 235
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
64-260 2.81e-07

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: 52.11  E-value: 2.81e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  64 IGKLLGHGQFGYTYV----AIHRPNGDRVAVKRLDKSkmvlpiaVEDVKREVQILIALSGHENVVQFHNAFEDDDY---- 135
Cdd:cd13975   4 LGRELGRGQYGVVYAcdswGGHFPCALKSVVPPDDKH-------WNDLALEFHYTRSLPKHERIVSLHGSVIDYSYgggs 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 136 ---VYIVMELceggelLDRILskkgnrYSEKDAAVVVRQMLKVA-----GECHLH--GLVHRDMKPENFLfksaqLDSPL 205
Cdd:cd13975  77 siaVLLIMER------LHRDL------YTGIKAGLSLEERLQIAldvveGIRFLHsqGLVHRDIKLKNVL-----LDKKN 139
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 34098881 206 KA--TDFGlsdFIKPGKRFH-DIVGSAYYVAPEVLKRRSGPESDVWSIGVITYILLCG 260
Cdd:cd13975 140 RAkiTDLG---FCKPEAMMSgSIVGTPIHMAPELFSGKYDNSVDVYAFGILFWYLCAG 194
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
66-286 3.01e-07

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


Pssm-ID: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 52.38  E-value: 3.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  66 KLLGHGQFGYTYVAIHRPNGDR----VAVKRLDKSKMvlPIAVEDVKREVQILIALSgHENVVQFHNAFEDDDyVYIVME 141
Cdd:cd05110  13 KVLGSGAFGTVYKGIWVPEGETvkipVAIKILNETTG--PKANVEFMDEALIMASMD-HPHLVRLLGVCLSPT-IQLVTQ 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCEGGELLDRILSKKGNRYSEkdaaVVVRQMLKVA-GECHLHG--LVHRDMKPENFLFKSAqldSPLKATDFGLSDFIKP 218
Cdd:cd05110  89 LMPHGCLLDYVHEHKDNIGSQ----LLLNWCVQIAkGMMYLEErrLVHRDLAARNVLVKSP---NHVKITDFGLARLLEG 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34098881 219 GKRFHDIVGSAY---YVAPEVLK-RRSGPESDVWSIGVITYILLC-GRRPFwdrteDGIfkeVLRNKPDFSRK 286
Cdd:cd05110 162 DEKEYNADGGKMpikWMALECIHyRKFTHQSDVWSYGVTIWELMTfGGKPY-----DGI---PTREIPDLLEK 226
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
370-506 3.05e-07

EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin/ERC45/calumenin)-EF hand family contains a group of six EF-hand, low-affinity Ca2+-binding proteins, including reticulocalbin (RCN-1), ER Ca2+-binding protein of 55 kDa (ERC-55, also known as TCBP-49 or E6BP), reticulocalbin-3 (RCN-3), Ca2+-binding protein of 45 kDa (Cab45 and its splice variant Cab45b), and calumenin ( also known as crocalbin or CBP-50). The proteins are not only localized in various parts of the secretory pathway, but also found in the cytosolic compartment and at the cell surface. They interact with different ligands or proteins and have been implicated in the secretory process, chaperone activity, signal transduction as well as in a large variety of disease processes.


Pssm-ID: 320021 [Multi-domain]  Cd Length: 267  Bit Score: 52.06  E-value: 3.05e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 370 LRDQFDAIDVDKNGVISLEEMRQALAKDLPWKLKDSrVAEILEAIDSNTDGLVDFTEFVAAAL--HVHQLEEHDSE---- 443
Cdd:cd15899  37 LGVIVSKMDVDKDGFISAKELHSWILESFKRHAMEE-SKEQFRAVDPDEDGHVSWDEYKNDTYgsVGDDEENVADNiked 115
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34098881 444 ----KWQLRSRAAFEKFDLDKDGYITPEELRM--------HTgLRGSIDPLLDEADIDRDGKISLHEFRRLLRTA 506
Cdd:cd15899 116 eeykKLLLKDKKRFEAADQDGDLILTLEEFLAflhpeespYM-LDFVIKETLEDLDKNGDGFISLEEFISDPYSA 189
EFh_CREC_RCN1 cd16229
EF-hand, calcium binding motif, found in reticulocalbin-1 (RCN-1); RCN-1 is an endoplasmic ...
371-498 3.76e-07

EF-hand, calcium binding motif, found in reticulocalbin-1 (RCN-1); RCN-1 is an endoplasmic reticulum resident low-affinity Ca2+-binding protein with six EF-hand motifs and a carboxyl-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide signal. It is expressed at the cell surface. RCN-1 acts as a potential negative regulator of B-RAF activation and can negatively modulate cardiomyocyte hypertrophy by inhibition of the mitogen-activated protein kinase signaling cascade. It also plays a key role in the development of doxorubicin-associated resistance.


Pssm-ID: 320027 [Multi-domain]  Cd Length: 267  Bit Score: 51.42  E-value: 3.76e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 371 RDQ--FDAIDVDKNGVISLEEMRQALAKDLPWKLKDSRVAEILEAIDSNTDGLVDFTEFVaAALHVHqlEEHDSE-KWQL 447
Cdd:cd16229 123 RDErrFKAADLDGDLAATREEFTAFLHPEEFEHMKDIVVLETLEDIDKNGDGFVDEDEYI-ADMFSH--EEGGPEpDWVK 199
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 34098881 448 RSRAAFEKF-DLDKDGYITPEELRmHTGLRGSID-------PLLDEADIDRDGKISLHE 498
Cdd:cd16229 200 TEREQFSDFrDLNKDGKMDKEEIR-HWILPQDYDhaqaearHLVYESDKDKDQKLTKEE 257
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
78-266 4.49e-07

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


Pssm-ID: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 51.87  E-value: 4.49e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  78 VAIHRPNGDRVAVKRLDkskmvLPIAVEDVKREVQILIALS---GHENVVQFHNAFEDDDYVYIVMELCEGGELLDRILS 154
Cdd:cd08227  18 LARYKPTGEYVTVRRIN-----LEACTNEMVTFLQGELHVSklfNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICT 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 155 KKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLFkSAQLDSPLKATDFGLSdFIKPGKR---FHDI----VG 227
Cdd:cd08227  93 HFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILI-SVDGKVYLSGLRSNLS-MINHGQRlrvVHDFpkysVK 170
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 34098881 228 SAYYVAPEVLKRR---SGPESDVWSIGVITYILLCGRRPFWD 266
Cdd:cd08227 171 VLPWLSPEVLQQNlqgYDAKSDIYSVGITACELANGHVPFKD 212
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
63-264 4.97e-07

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: 51.56  E-value: 4.97e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  63 TIGKLLGHGQFGYTYVAihrpngDRVAVKRlDKSKMVLPIAVE------------DVKREVQILIALSGHENVVQFHNAF 130
Cdd:cd05100  15 TLGKPLGEGCFGQVVMA------EAIGIDK-DKPNKPVTVAVKmlkddatdkdlsDLVSEMEMMKMIGKHKNIINLLGAC 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 131 EDDDYVYIVMELCEGGELLDRILSKK--GNRYSE------------KD----AAVVVRQMLKVAGEchlhGLVHRDMKPE 192
Cdd:cd05100  88 TQDGPLYVLVEYASKGNLREYLRARRppGMDYSFdtcklpeeqltfKDlvscAYQVARGMEYLASQ----KCIHRDLAAR 163
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34098881 193 NFLFKSaqlDSPLKATDFGLSDFIKPGKRFHDIVGS---AYYVAPEVL-KRRSGPESDVWSIGVITY-ILLCGRRPF 264
Cdd:cd05100 164 NVLVTE---DNVMKIADFGLARDVHNIDYYKKTTNGrlpVKWMAPEALfDRVYTHQSDVWSFGVLLWeIFTLGGSPY 237
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
67-292 5.24e-07

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: 51.54  E-value: 5.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  67 LLGHGQFGYTYVAIHRPNGDRVAVKrldkSKMVLPIAVEDVKR----EVQILIALSGHENVVQFHNAFEDDDYVYIVMEL 142
Cdd:cd05089   9 VIGEGNFGQVIKAMIKKDGLKMNAA----IKMLKEFASENDHRdfagELEVLCKLGHHPNIINLLGACENRGYLYIAIEY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 143 CEGGELLDRIlskKGNRYSEKDAA----------VVVRQMLKVAGECH--LHGL-----VHRDMKPENFLFKSAQLDspl 205
Cdd:cd05089  85 APYGNLLDFL---RKSRVLETDPAfakehgtastLTSQQLLQFASDVAkgMQYLsekqfIHRDLAARNVLVGENLVS--- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 206 KATDFGLSD----FIKP--GK---RFHDIVGSAYYVAPEvlkrrsgpESDVWSIGVITY-ILLCGRRPFWDRT------- 268
Cdd:cd05089 159 KIADFGLSRgeevYVKKtmGRlpvRWMAIESLNYSVYTT--------KSDVWSFGVLLWeIVSLGGTPYCGMTcaelyek 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 34098881 269 -------------EDGIF---KEVLRNKPdFSRKPWATIS 292
Cdd:cd05089 231 lpqgyrmekprncDDEVYelmRQCWRDRP-YERPPFSQIS 269
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
363-498 5.74e-07

EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN.


Pssm-ID: 320023 [Multi-domain]  Cd Length: 278  Bit Score: 51.15  E-value: 5.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 363 DEAEISDLRDQFDAIDVDKNGVISLEE------------MRQALAKDlpwklkdsrvaeILEAIDSNTDGLVDFTEFVAA 430
Cdd:cd16225 126 DKEVLDRYKDRWSQADEPEDGLLDVEEflsfrhpehsrgMLKNMVKE------------ILHDLDQDGDEKLTLDEFVSL 193
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 431 AL-HVHQLEEHDSEKWQLRSRAAFEK-FDLDKDGYITPEELRMHtglrgsIDP------------LLDEADIDRDGKISL 496
Cdd:cd16225 194 PPgTVEEQQAEDDDEWKKERKKEFEEvIDLNHDGKVTKEELEEY------MDPrnerhalneakqLIAVADENKDGKLSL 267

                ..
gi 34098881 497 HE 498
Cdd:cd16225 268 EE 269
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
372-503 5.75e-07

EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand proteins family, also named the calbindin sub-family, contains a group of six EF-hand Ca2+-binding proteins, including calretinin (CR, also termed 29 kDa calbindin), calbindin D28K (CB, also termed vitamin D-dependent calcium-binding protein, avian-type), and secretagogin (SCGN). CR is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t-specific neurons of the central and peripheral nervous system. It is a multifunctional protein implicated in many biological processes, including cell proliferation, differentiation, and cell death. CB is highly expressed in brain tissue. It is a strong calcium-binding and buffering protein responsible for preventing a neuronal death as well as maintaining and controlling calcium homeostasis. SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a Ca2+ sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. Although the family members share a significant amount of secondary sequence homology, they display altered structural and biochemical characteristics, and operate in distinct fashions. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. They harbor two and four EF-hand motifs, respectively. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. Human SCGN simultaneously binds four calcium ions through its EF-hands 3, 4, 5 and 6 in one high affinity and three low affinity calcium-binding sites. In contrast, SCGNs in other lower eukaryotes, such as D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, are fully competent in terms of six calcium-binding.


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 50.81  E-value: 5.75e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 372 DQFDAIDVDKNGVISLEEMR---QALAKDLPWKLKD-----SRVAEILEAIDSNTDGLVDFTEFVaaalHVHQLEEH--- 440
Cdd:cd15902   3 EVWMHFDADGNGYIEGKELDsflRELLKALNGKDKTddevaEKKKEFMEKYDENEDGKIEIRELA----NILPTEENfll 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 441 -----DSEKWQLRSRAAFEKFDLDKDGYITPEELR--------------MHTGLRGSIDPLLDEADIDRDGKISLHEFRR 501
Cdd:cd15902  79 lfrreQPLISSVEFMKIWRKYDTDGSGFIEAKELKgflkdlllknkkhvSPPKLDEYTKLILKEFDANKDGKLELDEMAK 158

                ..
gi 34098881 502 LL 503
Cdd:cd15902 159 LL 160
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
68-263 5.88e-07

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 51.36  E-value: 5.88e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  68 LGHGQFGYTYVAIHRpnGDRVAVKRL-DKSKMVLPIAVEDVKREVQILIALSgHENVVQFHN-AFEDDDY--VYIVMElc 143
Cdd:cd14159   1 IGEGGFGCVYQAVMR--NTEYAVKRLkEDSELDWSVVKNSFLTEVEKLSRFR-HPNIVDLAGySAQQGNYclIYVYLP-- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 144 eGGELLDRIlskkgnRYSEKDAAVVVRQMLKVA-----GECHLH----GLVHRDMKPENFLfksaqLDSPL--KATDFGL 212
Cdd:cd14159  76 -NGSLEDRL------HCQVSCPCLSWSQRLHVLlgtarAIQYLHsdspSLIHGDVKSSNIL-----LDAALnpKLGDFGL 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34098881 213 SDFIK----PGK-----RFHDIVGSAYYVAPEVLKR-RSGPESDVWSIGVITYILLCGRRP 263
Cdd:cd14159 144 ARFSRrpkqPGMsstlaRTQTVRGTLAYLPEEYVKTgTLSVEIDVYSFGVVLLELLTGRRA 204
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
65-321 6.53e-07

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: 51.22  E-value: 6.53e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  65 GKLLGHGQFGYTYVAIHRPNGDR--VAVKRLDKSKMVLPIAvedvkREVQILIALSgHENVVQFHNAF--EDDDYVYIVM 140
Cdd:cd07867   7 GCKVGRGTYGHVYKAKRKDGKDEkeYALKQIEGTGISMSAC-----REIALLRELK-HPNVIALQKVFlsHSDRKVWLLF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCEGG--ELLDRILSKKGNRYSEKDAAVVVRQMLK--VAGECHLHG--LVHRDMKPENFLFKSAQLD-SPLKATDFGLS 213
Cdd:cd07867  81 DYAEHDlwHIIKFHRASKANKKPMQLPRSMVKSLLYqiLDGIHYLHAnwVLHRDLKPANILVMGEGPErGRVKIADMGFA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 214 DF----IKPGKRFHDIVGSAYYVAPEVL--KRRSGPESDVWSIGVITYILLCGRRPFWDRTED-------------GIFK 274
Cdd:cd07867 161 RLfnspLKPLADLDPVVVTFWYRAPELLlgARHYTKAIDIWAIGCIFAELLTSEPIFHCRQEDiktsnpfhhdqldRIFS 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34098881 275 ----------EVLRNKP-------DFSRKPWAT-----------ISDSAKDFV--KKLLVKDPRARLTAAQALSHAW 321
Cdd:cd07867 241 vmgfpadkdwEDIRKMPeyptlqkDFRRTTYANsslikymekhkVKPDSKVFLllQKLLTMDPTKRITSEQALQDPY 317
STKc_CK1_gamma cd14126
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; STKs catalyze ...
62-233 9.72e-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: 50.50  E-value: 9.72e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHRPNGDRVAVKrLDKSKMVLPiaveDVKREVQILIALSGHENVVQFHNAFEDDDYVYIVME 141
Cdd:cd14126   2 FRVGKKIGCGNFGELRLGKNLYNNEHVAIK-LEPMKSRAP----QLHLEYRFYKLLGQAEGLPQVYYFGPCGKYNAMVLE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 142 LCegGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLF--KSAQLDSPLKATDFGLS-DFIKP 218
Cdd:cd14126  77 LL--GPSLEDLFDLCDRTFSLKTVLMIAIQLISRIEYVHSKHLIYRDVKPENFLIgrQSTKKQHVIHIIDFGLAkEYIDP 154
                       170       180
                ....*....|....*....|..
gi 34098881 219 GKRFH-------DIVGSAYYVA 233
Cdd:cd14126 155 ETNKHipyrehkSLTGTARYMS 176
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
62-317 9.84e-07

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: 50.33  E-value: 9.84e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAIHrPNGDRVaVKRLDKSKMVLPIavEDVKREVQ-ILIALSGHENVVQFHNAFEDDDYVYIVM 140
Cdd:cd13980   2 YLYDKSLGSTRFLKVARARH-DEGLVV-VKVFVKPDPALPL--RSYKQRLEeIRDRLLELPNVLPFQKVIETDKAAYLIR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 141 ELCeGGELLDRILSKKGNRYSEKdaAVVVRQMLKVAGECHLHGLVHRDMKPENFLFKSAqlDSPLkatdfgLSDF--IKP 218
Cdd:cd13980  78 QYV-KYNLYDRISTRPFLNLIEK--KWIAFQLLHALNQCHKRGVCHGDIKTENVLVTSW--NWVY------LTDFasFKP 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 219 G----------KRFHDIVGS-AYYVAPE----------VLKRRSG---PESDVWSIG-VITYILLCGRRPFwdrTEDGIF 273
Cdd:cd13980 147 TylpednpadfSYFFDTSRRrTCYIAPErfvdaltldaESERRDGeltPAMDIFSLGcVIAELFTEGRPLF---DLSQLL 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 34098881 274 KevLRNKPDFSRKPWATISD-SAKDFVKKLLVKDPRARLTAAQAL 317
Cdd:cd13980 224 A--YRKGEFSPEQVLEKIEDpNIRELILHMIQRDPSKRLSAEDYL 266
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
62-253 1.03e-06

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: 50.62  E-value: 1.03e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881  62 YTIGKLLGHGQFGYTYVAI-HRPNGDRVAVK---RLDKSKmvlpiavEDVKREVQILIALSGHE-----NVVQFHNAFED 132
Cdd:cd14213  14 YEIVDTLGEGAFGKVVECIdHKMGGMHVAVKivkNVDRYR-------EAARSEIQVLEHLNTTDpnstfRCVQMLEWFDH 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 133 DDYVYIVMELCeGGELLDRILSKKGNRYSEKDAAVVVRQMLKVAGECHLHGLVHRDMKPENFLF-----------KSAQL 201
Cdd:cd14213  87 HGHVCIVFELL-GLSTYDFIKENSFLPFPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFvqsdyvvkynpKMKRD 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 34098881 202 DSPLKATDFGLSDFikpGKRFHD------IVGSAYYVAPEV-LKRRSGPESDVWSIGVI 253
Cdd:cd14213 166 ERTLKNPDIKVVDF---GSATYDdehhstLVSTRHYRAPEViLALGWSQPCDVWSIGCI 221
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
374-499 8.12e-06

EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 (RCN-3), and similar proteins; The family corresponds to a group of six EF-hand Ca2+-binding proteins, including calumenin (also known as crocalbin or CBP-50), reticulocalbin-1 (RCN-1), reticulocalbin-3 (RCN-3), and similar proteins. Calumenin is an endo/sarcoplasmic reticulum (ER/SR) resident low-affinity Ca2+-binding protein that contains six EF-hand domains and a C-terminal SR retention signal His-Asp-Glu-Phe (HDEF) tetrapeptide. It functions as a novel regulator of SERCA2, and its expressional changes are tightly coupled with Ca2+-cycling of cardiomyocytes. It is also broadly involved in haemostasis and in the pathophysiology of thrombosis. Moreover, the extracellular calumenin acts as a suppressor of cell migration and tumor metastasis. RCN-1 is an endoplasmic reticulum resident Ca2+-binding protein with a carboxyl-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide signal. It acts as a potential negative regulator of B-RAF activation and can negatively modulate cardiomyocyte hypertrophy by inhibition of the mitogen-activated protein kinase signalling cascade. It also plays a key role in the development of doxorubicin-associated resistance. RCN-3 is a putative six EF-hand Ca2+-binding protein that contains five RXXR (X is any amino acid) motifs and a C-terminal ER retrieval signal HDEL tetrapeptide. The RXXR motif represents the target sequence of subtilisin-like proprotein convertases (SPCs). RCN-3 is specifically bound to the paired basic amino-acid-cleaving enzyme-4 (PACE4) precursor protein and plays an important role in the biosynthesis of PACE4.


Pssm-ID: 320024 [Multi-domain]  Cd Length: 264  Bit Score: 47.58  E-value: 8.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 374 FDAIDVDKNGVISLEEM--------RQALAKD---------------LPWKLKDSRVAEILEAIDSNTDGLVDFTEFVaa 430
Cdd:cd16226  41 VDKIDKNGDGFVTEEELkdwikyvqKKYIREDvdrqwkeydpnkdgkLSWEEYKKATYGFLDDEEEDDDLHESYKKMI-- 118
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34098881 431 alhvhqleEHDSEKWqlrsRAAfekfDLDKDGYITPEEL----------RMHTGLrgsIDPLLDEADIDRDGKISLHEF 499
Cdd:cd16226 119 --------RRDERRW----KAA----DQDGDGKLTKEEFtaflhpeefpHMRDIV---VQETLEDIDKNKDGFISLEEY 178
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
344-465 2.31e-05

EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein (ALG-2); The family includes some homologs of mammalian apoptosis-linked gene 2 protein (ALG-2) mainly found in lower eukaryotes, such as a parasitic protist Leishmarua major and a cellular slime mold Dictyostelium discoideum. These homologs contains five EF-hand motifs. Due to the presence of unfavorable residues at the Ca2+-coordinating positions, their non-canonical EF4 and EF5 hands may not bind Ca2+. Two Dictyostelium PEF proteins are the prototypes of this family. They may bind to cytoskeletal proteins and/or signal-transducing proteins localized to detergent-resistant membranes named lipid rafts, and occur as monomers or weak homo- or heterodimers like ALG-2. They can serve as a mediator for Ca2+ signaling-related Dictyostehum programmed cell death (PCD).


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 44.90  E-value: 2.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 344 FVRYSRLKQFalralastldeaeISDLRDQFDAIDVDKNGVISLEEMRQALAKdLPWKLKDSRVAEILEAIDSNTDGLVD 423
Cdd:cd16185  55 FEEFAALHQF-------------LSNMQNGFEQRDTSRSGRLDANEVHEALAA-SGFQLDPPAFQALFRKFDPDRGGSLG 120
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 34098881 424 FTEFVAAALHVHQleehdsekwqlrSRAAFEKFDLDKDGYIT 465
Cdd:cd16185 121 FDDYIELCIFLAS------------ARNLFQAFDRQRTGRVT 150
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
363-499 5.91e-05

EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN.


Pssm-ID: 320023 [Multi-domain]  Cd Length: 278  Bit Score: 44.98  E-value: 5.91e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 363 DEAEISDLRDQFDAIDVDKNGVISLEEMRQALAKDLPWKLKDSRV--AEILEAIDSNTDGLVDFTEF------------V 428
Cdd:cd16225  29 EPKKRKKLKEIFKKVDVNTDGFLSAEELEDWIMEKTQEHFQEAVEenEQIFKAVDTDKDGNVSWEEYrvhfllskgyseE 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 429 AAALHVHQLEE---HDSEKWQL-RSRAAFEKFDLDKDGYITPEEL-------RMHTGLRGSIDPLLDEADIDRDGKISLH 497
Cdd:cd16225 109 EAEEKIKNNEElklDEDDKEVLdRYKDRWSQADEPEDGLLDVEEFlsfrhpeHSRGMLKNMVKEILHDLDQDGDEKLTLD 188

                ..
gi 34098881 498 EF 499
Cdd:cd16225 189 EF 190
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
396-499 7.26e-05

EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN.


Pssm-ID: 320023 [Multi-domain]  Cd Length: 278  Bit Score: 44.60  E-value: 7.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 396 KDLPWKLKDSRVAEILEAIDSNTDGLVDFTEFvaAALHVHQLEEHDSEKWQlRSRAAFEKFDLDKDGYITPEELRMH--- 472
Cdd:cd16225  25 EEDSEPKKRKKLKEIFKKVDVNTDGFLSAEEL--EDWIMEKTQEHFQEAVE-ENEQIFKAVDTDKDGNVSWEEYRVHfll 101
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 34098881 473 ----------------------TGLRGSIDPLLD---EADIDRDGKISLHEF 499
Cdd:cd16225 102 skgyseeeaeekiknneelkldEDDKEVLDRYKDrwsQADEPEDGLLDVEEF 153
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
344-499 8.37e-05

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This family corresponds to a group of uncharacterized RCN2-like proteins, which are mainly found in protostomes. Although their biological function remains unclear, they show high sequence similarity with RCN2 (also known as E6BP or TCBP-49), which is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. Members in this family contain six copies of the EF-hand Ca2+-binding motif, but may lack a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320025 [Multi-domain]  Cd Length: 263  Bit Score: 44.23  E-value: 8.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 344 FVRYSRLKQFALRALAStLDEAEISDlrdQFDAIDVDKNGVIS---------------LEEMRQALAKDLPWKLKDSRva 408
Cdd:cd16227  52 FIDRKELKAWILRSFKM-LDEEEANE---RFEEADEDGDGKVTweeyladsfgyddedNEEMIKDSTEDDLKLLEDDK-- 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 409 EILEAIDSNTDGLVDFTEFVAaalhvhqleehdsekwqlrsraafekfdldkdgYITPEEL-RMHTGLrgsIDPLLDEAD 487
Cdd:cd16227 126 EMFEAADLNKDGKLDKTEFSA---------------------------------FQHPEEYpHMHPVL---IEQTLRDKD 169
                       170
                ....*....|..
gi 34098881 488 IDRDGKISLHEF 499
Cdd:cd16227 170 KDNDGFISFQEF 181
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
366-465 3.02e-04

Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+.


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 41.36  E-value: 3.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 366 EISDLRDQFDAIDVDKNGVISLEEMRQALaKDLPWKLKDSRVAEILEAIDSNTDGLVDFTEFVAAALHVHQLEEhdsekw 445
Cdd:cd16180  65 YIQDWRRLFRRFDRDRSGSIDFNELQNAL-SSFGYRLSPQFVQLLVRKFDRRRRGSISFDDFVEACVTLKRLTD------ 137
                        90       100
                ....*....|....*....|
gi 34098881 446 qlrsraAFEKFDLDKDGYIT 465
Cdd:cd16180 138 ------AFRKYDTNRTGYAT 151
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
339-506 3.03e-04

EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand proteins family, also named the calbindin sub-family, contains a group of six EF-hand Ca2+-binding proteins, including calretinin (CR, also termed 29 kDa calbindin), calbindin D28K (CB, also termed vitamin D-dependent calcium-binding protein, avian-type), and secretagogin (SCGN). CR is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t-specific neurons of the central and peripheral nervous system. It is a multifunctional protein implicated in many biological processes, including cell proliferation, differentiation, and cell death. CB is highly expressed in brain tissue. It is a strong calcium-binding and buffering protein responsible for preventing a neuronal death as well as maintaining and controlling calcium homeostasis. SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a Ca2+ sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. Although the family members share a significant amount of secondary sequence homology, they display altered structural and biochemical characteristics, and operate in distinct fashions. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. They harbor two and four EF-hand motifs, respectively. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. Human SCGN simultaneously binds four calcium ions through its EF-hands 3, 4, 5 and 6 in one high affinity and three low affinity calcium-binding sites. In contrast, SCGNs in other lower eukaryotes, such as D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, are fully competent in terms of six calcium-binding.


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 42.73  E-value: 3.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 339 NNLRQFVRYSRLKqfalralaSTLDEAEIsdlrdqFDAIDVDKNGVISLEEMRQALaKDLPWKLK----DSRVAE----I 410
Cdd:cd15902  75 NFLLLFRREQPLI--------SSVEFMKI------WRKYDTDGSGFIEAKELKGFL-KDLLLKNKkhvsPPKLDEytklI 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 411 LEAIDSNTDGLVDFTEFvAAALHVhqlEEHDSEKWQLRSR---------AAFEKFDLDKDGYITPEEL------------ 469
Cdd:cd15902 140 LKEFDANKDGKLELDEM-AKLLPV---QENFLLKFQILGAmdltkedfeKVFEHYDKDNNGVIEGNELdallkdlleknk 215
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 34098881 470 --RMHTGLRGSIDPLLDEADIDRDGKISLHEFRRLLRTA 506
Cdd:cd15902 216 adIDKPDLENFRDAILRACDKNKDGKIQKTELALFLSAK 254
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
354-395 2.70e-03

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 36.37  E-value: 2.70e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 34098881 354 ALRALASTLDEAEISDLrdqFDAIDVDKNGVISLEEMRQALA 395
Cdd:cd00051  25 ALKSLGEGLSEEEIDEM---IREVDKDGDGKIDFEEFLELMA 63
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
406-499 3.00e-03

EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 (RCN-3), and similar proteins; The family corresponds to a group of six EF-hand Ca2+-binding proteins, including calumenin (also known as crocalbin or CBP-50), reticulocalbin-1 (RCN-1), reticulocalbin-3 (RCN-3), and similar proteins. Calumenin is an endo/sarcoplasmic reticulum (ER/SR) resident low-affinity Ca2+-binding protein that contains six EF-hand domains and a C-terminal SR retention signal His-Asp-Glu-Phe (HDEF) tetrapeptide. It functions as a novel regulator of SERCA2, and its expressional changes are tightly coupled with Ca2+-cycling of cardiomyocytes. It is also broadly involved in haemostasis and in the pathophysiology of thrombosis. Moreover, the extracellular calumenin acts as a suppressor of cell migration and tumor metastasis. RCN-1 is an endoplasmic reticulum resident Ca2+-binding protein with a carboxyl-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide signal. It acts as a potential negative regulator of B-RAF activation and can negatively modulate cardiomyocyte hypertrophy by inhibition of the mitogen-activated protein kinase signalling cascade. It also plays a key role in the development of doxorubicin-associated resistance. RCN-3 is a putative six EF-hand Ca2+-binding protein that contains five RXXR (X is any amino acid) motifs and a C-terminal ER retrieval signal HDEL tetrapeptide. The RXXR motif represents the target sequence of subtilisin-like proprotein convertases (SPCs). RCN-3 is specifically bound to the paired basic amino-acid-cleaving enzyme-4 (PACE4) precursor protein and plays an important role in the biosynthesis of PACE4.


Pssm-ID: 320024 [Multi-domain]  Cd Length: 264  Bit Score: 39.49  E-value: 3.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34098881 406 RVAEILEAIDSNTDGLVDFTEFVAAALHVHQ--LEEHDSEKWQLrsraafekFDLDKDGYITPEELRMHT-GLRGSIDPL 482
Cdd:cd16226  36 RLGIIVDKIDKNGDGFVTEEELKDWIKYVQKkyIREDVDRQWKE--------YDPNKDGKLSWEEYKKATyGFLDDEEED 107
                        90       100       110
                ....*....|....*....|....*....|....
gi 34098881 483 LDE-----------------ADIDRDGKISLHEF 499
Cdd:cd16226 108 DDLhesykkmirrderrwkaADQDGDGKLTKEEF 141
 
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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