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Conserved domains on  [gi|115430241|ref|NP_065731|]
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N-terminal kinase-like protein isoform A [Homo sapiens]

Protein Classification

SCY1-like family protein( domain architecture ID 10195806)

SCY1-like family protein belonging to the protein kinase superfamily is a catalytically inactive protein with similarity to yeast Scy1, and may be involved in membrane trafficking

CATH:  1.10.510.10
Gene Ontology:  GO:0005524
PubMed:  26981075|16244704

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
20-296 7.42e-87

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


:

Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 276.90  E-value: 7.42e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  20 PPEGGLPGPWALHRGRKKATGSPVSIFVYDVKPGA-------EEQTQVAKAAFKRFKTLRHPNILAYIDGLETEK-CLHV 91
Cdd:cd14011    1 VASAGPGLPWKIYNGSKKSTKQEVSVFVFEKKQLEeyskrdrEQILELLKRGVKQLTRLRHPRILTVQHPLEESReSLAF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  92 VTEAVT-PLGIYLKARVE---------AGGLKELEISWGLHQIVKALSFLVNDCSLIHNNVCMAAVFVDRAGEWKLGGLD 161
Cdd:cd14011   81 ATEPVFaSLANVLGERDNmpspppelqDYKLYDVEIKYGLLQISEALSFLHNDVKLVHGNICPESVVINSNGEWKLAGFD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 162 YMYSAQGNGGGPP-----RKGIPELEQYDPPELADSSGRVVREKWSADMWRLGCLIWEVFngplpraaalrNPGKIPKTl 236
Cdd:cd14011  161 FCISSEQATDQFPyfreyDPNLPPLAQPNLNYLAPEYILSKTCDPASDMFSLGVLIYAIY-----------NKGKPLFD- 228
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115430241 237 vphyCELVGANPKVRPNPARFLQ-NCRAPGGFMSNRFVETNLFL-EEIQIK-EPAEKQKFFQE 296
Cdd:cd14011  229 ----CVNNLLSYKKNSNQLRQLSlSLLEKVPEELRDHVKTLLNVtPEVRPDaEQLSKIPFFDD 287
 
Name Accession Description Interval E-value
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
20-296 7.42e-87

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


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 276.90  E-value: 7.42e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  20 PPEGGLPGPWALHRGRKKATGSPVSIFVYDVKPGA-------EEQTQVAKAAFKRFKTLRHPNILAYIDGLETEK-CLHV 91
Cdd:cd14011    1 VASAGPGLPWKIYNGSKKSTKQEVSVFVFEKKQLEeyskrdrEQILELLKRGVKQLTRLRHPRILTVQHPLEESReSLAF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  92 VTEAVT-PLGIYLKARVE---------AGGLKELEISWGLHQIVKALSFLVNDCSLIHNNVCMAAVFVDRAGEWKLGGLD 161
Cdd:cd14011   81 ATEPVFaSLANVLGERDNmpspppelqDYKLYDVEIKYGLLQISEALSFLHNDVKLVHGNICPESVVINSNGEWKLAGFD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 162 YMYSAQGNGGGPP-----RKGIPELEQYDPPELADSSGRVVREKWSADMWRLGCLIWEVFngplpraaalrNPGKIPKTl 236
Cdd:cd14011  161 FCISSEQATDQFPyfreyDPNLPPLAQPNLNYLAPEYILSKTCDPASDMFSLGVLIYAIY-----------NKGKPLFD- 228
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115430241 237 vphyCELVGANPKVRPNPARFLQ-NCRAPGGFMSNRFVETNLFL-EEIQIK-EPAEKQKFFQE 296
Cdd:cd14011  229 ----CVNNLLSYKKNSNQLRQLSlSLLEKVPEELRDHVKTLLNVtPEVRPDaEQLSKIPFFDD 287
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
69-259 1.74e-09

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 59.08  E-value: 1.74e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241    69 KTLRHPNILAYIDGLETEKCLHVVTEAVT--PLGIYLKARveaGGLKELEISWGLHQIVKALSFLvNDCSLIH-----NN 141
Cdd:smart00220  52 KKLKHPNIVRLYDVFEDEDKLYLVMEYCEggDLFDLLKKR---GRLSEDEARFYLRQILSALEYL-HSKGIVHrdlkpEN 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241   142 vcmaaVFVDRAGEWKLG--GLdymySAQGNGGGPPRK--GIPEleqYDPPELadssgrVVREKWS--ADMWRLGCLIWEV 215
Cdd:smart00220 128 -----ILLDEDGHVKLAdfGL----ARQLDPGEKLTTfvGTPE---YMAPEV------LLGKGYGkaVDIWSLGVILYEL 189
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115430241   216 ------FNGPLPRAAALRNPGKIPKTLVPHY-------CELVGA----NPKVRPNPARFLQ 259
Cdd:smart00220 190 ltgkppFPGDDQLLELFKKIGKPKPPFPPPEwdispeaKDLIRKllvkDPEKRLTAEEALQ 250
Pkinase pfam00069
Protein kinase domain;
33-221 1.24e-06

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 49.93  E-value: 1.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241   33 RGRKKATGSPVSIFVYDVKPGAEEQTQVAKAAFKRFKTLRHPNILAYIDGLETEKCLHVVTEAVtPLGIYLKARVEAGGL 112
Cdd:pfam00069  17 KAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV-EGGSLFDLLSEKGAF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  113 KELEISWGLHQIVKALsflvndcsliHNNVCMaAVFVdragewklGGLDYMysAqgngggpprkgiPEL---EQYDPPel 189
Cdd:pfam00069  96 SEREAKFIMKQILEGL----------ESGSSL-TTFV--------GTPWYM--A------------PEVlggNPYGPK-- 140
                         170       180       190
                  ....*....|....*....|....*....|..
gi 115430241  190 adssgrvvrekwsADMWRLGCLIWEVFNGPLP 221
Cdd:pfam00069 141 -------------VDVWSLGCILYELLTGKPP 159
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
55-305 3.86e-06

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 50.40  E-value: 3.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  55 EEQTQVAKAAFKRFKTLRHPNILAYIDGLETEKCLHVVTEAVT--PLGIYLKARV-EAGGLKELEISWGLHQIVKALSFL 131
Cdd:PTZ00267 106 ERQAAYARSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSggDLNKQIKQRLkEHLPFQEYEVGLLFYQIVLALDEV 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 132 VNDCsLIHNNVCMAAVFVDRAGEWKLGglDYMYSAQGNGG-----GPPRKGIPeleQYDPPELADssgrvvREKWS--AD 204
Cdd:PTZ00267 186 HSRK-MMHRDLKSANIFLMPTGIIKLG--DFGFSKQYSDSvsldvASSFCGTP---YYLAPELWE------RKRYSkkAD 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 205 MWRLGCLIWEV------FNGPLPRAAALR--------NPGKIPKTLVPHYCELVGANPKVRPNPARFLQNcrapgGFMsn 270
Cdd:PTZ00267 254 MWSLGVILYELltlhrpFKGPSQREIMQQvlygkydpFPCPVSSGMKALLDPLLSKNPALRPTTQQLLHT-----EFL-- 326
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 115430241 271 RFVeTNLFlEEI----QIKEPAEKQKFFQELSKSLDAFP 305
Cdd:PTZ00267 327 KYV-ANLF-QDIvrhsETISPHDREEILRQLQESGERAP 363
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
61-221 8.70e-03

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 39.61  E-value: 8.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  61 AKAAFKR----FKTLRHPNILAYIDGLETEKCLHVVTEAVTplGIYLKARVEAGG-LKELEISWGLHQIVKALSFLvNDC 135
Cdd:COG0515   50 ARERFRRearaLARLNHPNIVRVYDVGEEDGRPYLVMEYVE--GESLADLLRRRGpLPPAEALRILAQLAEALAAA-HAA 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 136 SLIHNNVCMAAVFVDRAGEWKLG--GLDYMYSAQGNGGGPPRKGIPeleQYDPPELAdsSGRVVREkwSADMWRLGCLIW 213
Cdd:COG0515  127 GIVHRDIKPANILLTPDGRVKLIdfGIARALGGATLTQTGTVVGTP---GYMAPEQA--RGEPVDP--RSDVYSLGVTLY 199

                 ....*...
gi 115430241 214 EVFNGPLP 221
Cdd:COG0515  200 ELLTGRPP 207
 
Name Accession Description Interval E-value
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
20-296 7.42e-87

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


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 276.90  E-value: 7.42e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  20 PPEGGLPGPWALHRGRKKATGSPVSIFVYDVKPGA-------EEQTQVAKAAFKRFKTLRHPNILAYIDGLETEK-CLHV 91
Cdd:cd14011    1 VASAGPGLPWKIYNGSKKSTKQEVSVFVFEKKQLEeyskrdrEQILELLKRGVKQLTRLRHPRILTVQHPLEESReSLAF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  92 VTEAVT-PLGIYLKARVE---------AGGLKELEISWGLHQIVKALSFLVNDCSLIHNNVCMAAVFVDRAGEWKLGGLD 161
Cdd:cd14011   81 ATEPVFaSLANVLGERDNmpspppelqDYKLYDVEIKYGLLQISEALSFLHNDVKLVHGNICPESVVINSNGEWKLAGFD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 162 YMYSAQGNGGGPP-----RKGIPELEQYDPPELADSSGRVVREKWSADMWRLGCLIWEVFngplpraaalrNPGKIPKTl 236
Cdd:cd14011  161 FCISSEQATDQFPyfreyDPNLPPLAQPNLNYLAPEYILSKTCDPASDMFSLGVLIYAIY-----------NKGKPLFD- 228
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115430241 237 vphyCELVGANPKVRPNPARFLQ-NCRAPGGFMSNRFVETNLFL-EEIQIK-EPAEKQKFFQE 296
Cdd:cd14011  229 ----CVNNLLSYKKNSNQLRQLSlSLLEKVPEELRDHVKTLLNVtPEVRPDaEQLSKIPFFDD 287
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
32-260 6.85e-16

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: 77.31  E-value: 6.85e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  32 HRGRKKATGSPVSIFVYDvKPGAEEQTQVAKAAFKRFKTLRHPNILAYIDGLETEKCLHVVTEAVTPLGIYLKARVEAGG 111
Cdd:cd00180   10 YKARDKETGKKVAVKVIP-KEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLKDLLKENKGP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 112 LKELEISWGLHQIVKALSFLvNDCSLIHNNVCMAAVFVDRAGEWKLGGLDYMYSAQGNGGGPPRKGIPELEQYDPPELAd 191
Cdd:cd00180   89 LSEEEALSILRQLLSALEYL-HSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGGTTPPYYAPPELL- 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115430241 192 ssGRVVREKwSADMWRLGCLIWEvfngpLPRAAALrnpgkIPKTLVPhycelvgaNPKVRPNPARFLQN 260
Cdd:cd00180  167 --GGRYYGP-KVDIWSLGVILYE-----LEELKDL-----IRRMLQY--------DPKKRPSAKELLEH 214
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
69-259 1.74e-09

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 59.08  E-value: 1.74e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241    69 KTLRHPNILAYIDGLETEKCLHVVTEAVT--PLGIYLKARveaGGLKELEISWGLHQIVKALSFLvNDCSLIH-----NN 141
Cdd:smart00220  52 KKLKHPNIVRLYDVFEDEDKLYLVMEYCEggDLFDLLKKR---GRLSEDEARFYLRQILSALEYL-HSKGIVHrdlkpEN 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241   142 vcmaaVFVDRAGEWKLG--GLdymySAQGNGGGPPRK--GIPEleqYDPPELadssgrVVREKWS--ADMWRLGCLIWEV 215
Cdd:smart00220 128 -----ILLDEDGHVKLAdfGL----ARQLDPGEKLTTfvGTPE---YMAPEV------LLGKGYGkaVDIWSLGVILYEL 189
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115430241   216 ------FNGPLPRAAALRNPGKIPKTLVPHY-------CELVGA----NPKVRPNPARFLQ 259
Cdd:smart00220 190 ltgkppFPGDDQLLELFKKIGKPKPPFPPPEwdispeaKDLIRKllvkDPEKRLTAEEALQ 250
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
56-261 4.17e-09

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: 58.14  E-value: 4.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  56 EQTQVAKAAFKRFKTLRHPNILAYIDGLETEKclhvvtEAVTPLGIY-LKARVEAGGLKE-LEI----------SWGLhQ 123
Cdd:cd14012   40 KQIQLLEKELESLKKLRHPNLVSYLAFSIERR------GRSDGWKVYlLTEYAPGGSLSElLDSvgsvpldtarRWTL-Q 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 124 IVKALSFLVNDcSLIHNNVCMAAVFVDRA---GEWKLGGLDYMYSAQgNGGGPPRKGIPELEQYDPPELADSSGRVVREk 200
Cdd:cd14012  113 LLEALEYLHRN-GVVHKSLHAGNVLLDRDagtGIVKLTDYSLGKTLL-DMCSRGSLDEFKQTYWLPPELAQGSKSPTRK- 189
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 201 wsADMWRLGCL---------IWEVFNGPLPraaaLRNPGKIPKTLVPHYCELVGANPKVRPNPARFLQNC 261
Cdd:cd14012  190 --TDVWDLGLLflqmlfgldVLEKYTSPNP----VLVSLDLSASLQDFLSKCLSLDPKKRPTALELLPHE 253
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
71-258 1.61e-08

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: 56.26  E-value: 1.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  71 LRHPNILAYIDGLETEKCLHVVTEAVtPLGIYLKARVEAGGLKELEISWGLHQIVKALSFLvNDCSLIHNNVCMAAVFVD 150
Cdd:cd06632   59 LRHPNIVQYYGTEREEDNLYIFLEYV-PGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYL-HSRNTVHRDIKGANILVD 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 151 RAGEWKLGglDYMYSAQGNGGGPPR--KGIPeleQYDPPEladssgrVVREKWS-----ADMWRLGCLIWEVFNGPLP-- 221
Cdd:cd06632  137 TNGVVKLA--DFGMAKHVEAFSFAKsfKGSP---YWMAPE-------VIMQKNSgyglaVDIWSLGCTVLEMATGKPPws 204
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 115430241 222 ---RAAALRNPGK------IPKTLVPHYCELVG----ANPKVRPNPARFL 258
Cdd:cd06632  205 qyeGVAAIFKIGNsgelppIPDHLSPDAKDFIRlclqRDPEDRPTASQLL 254
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
35-233 2.22e-08

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: 55.99  E-value: 2.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  35 RKKATGSPVSIFVYDVKPGAEEQTQVAKAAFKRFKTLRHPNILAYIDGLETEKCLHVVTEAVTPlGIYLKARVEAGGLKE 114
Cdd:cd14072   20 RHVLTGREVAIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYASG-GEVFDYLVAHGRMKE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 115 LEISWGLHQIVKALSFLvNDCSLIHNNVCMAAVFVDRAGEWKLGglDYMYSAQGNGG-------GPPRKGIPELEQ---Y 184
Cdd:cd14072   99 KEARAKFRQIVSAVQYC-HQKRIVHRDLKAENLLLDADMNIKIA--DFGFSNEFTPGnkldtfcGSPPYAAPELFQgkkY 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 115430241 185 DPPELadssgrvvrekwsaDMWRLGCLIWEVFNGPLP---------RAAALRNPGKIP 233
Cdd:cd14072  176 DGPEV--------------DVWSLGVILYTLVSGSLPfdgqnlkelRERVLRGKYRIP 219
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
35-220 3.00e-08

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: 55.79  E-value: 3.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  35 RKKATGSPVSIFVYDVKPGAEEQTQVAKAAFKRFKTLRHPNILAYIDGLETEKCLHVVTEAV--TPLGiYLKARveAGGL 112
Cdd:cd07833   21 RNKATGEIVAIKKFKESEDDEDVKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYLVFEYVerTLLE-LLEAS--PGGL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 113 KELEISWGLHQIVKALSFL-VNDCslIHNNVCMAAVFVDRAGEWKLGGLDYMYSAQGNGGGPPRKGI-------PEL--- 181
Cdd:cd07833   98 PPDAVRSYIWQLLQAIAYChSHNI--IHRDIKPENILVSESGVLKLCDFGFARALTARPASPLTDYVatrwyraPELlvg 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 115430241 182 -EQYDPPeladssgrvvrekwsADMWRLGCLIWEVFNG-PL 220
Cdd:cd07833  176 dTNYGKP---------------VDVWAIGCIMAELLDGePL 201
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
33-238 1.59e-07

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: 53.41  E-value: 1.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  33 RGRKKATGSPVSI-FVydVKPG-AEEQTQVAKAAFKRFKTLRHPNILAYIDGLETEKCLHVVTE-AVTPLGIYLKarvEA 109
Cdd:cd14002   19 KGRRKYTGQVVALkFI--PKRGkSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEyAQGELFQILE---DD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 110 GGLKELEISWGLHQIVKALSFLvNDCSLIHNNVCMAAVFVDRAGEWKLggLDYmysaqgnggGPPR------------KG 177
Cdd:cd14002   94 GTLPEEEVRSIAKQLVSALHYL-HSNRIIHRDMKPQNILIGKGGVVKL--CDF---------GFARamscntlvltsiKG 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115430241 178 IPeleQYDPPELadssgrvVREK---WSADMWRLGCLIWEVFNGPLPRAAA---------LRNPGKIPKTLVP 238
Cdd:cd14002  162 TP---LYMAPEL-------VQEQpydHTADLWSLGCILYELFVGQPPFYTNsiyqlvqmiVKDPVKWPSNMSP 224
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
69-229 1.90e-07

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: 53.04  E-value: 1.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  69 KTLRHPNILAYIDGLETEKCLHVVTE--AVTPLGIYLKARVEAGGLKELEISWGL-HQIVKALSFLvNDCSLIHNNVCMA 145
Cdd:cd08224   55 QQLNHPNIIKYLASFIENNELNIVLElaDAGDLSRLIKHFKKQKRLIPERTIWKYfVQLCSALEHM-HSKRIMHRDIKPA 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 146 AVFVDRAGEWKLG--GLDYMYSAQGNGG----GPPrkgipeleQYDPPEladssgrVVREK---WSADMWRLGCLIWEVf 216
Cdd:cd08224  134 NVFITANGVVKLGdlGLGRFFSSKTTAAhslvGTP--------YYMSPE-------RIREQgydFKSDIWSLGCLLYEM- 197
                        170
                 ....*....|...
gi 115430241 217 ngplpraAALRNP 229
Cdd:cd08224  198 -------AALQSP 203
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
35-260 3.37e-07

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: 52.47  E-value: 3.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  35 RKKATGSPVSIFVYDVKPGAEEQTQVAKAAFKRFKTLRHPNILAYIDGLETEKCLHVVTE--AVTPLGIYLKARVEAGG- 111
Cdd:cd08215   20 RRKSDGKLYVLKEIDLSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEyaDGGDLAQKIKKQKKKGQp 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 112 LKELEI-SWgLHQIVKALSFLvNDCSLIHNNVCMAAVFVDRAGEWKLG--GLDYMYS-----AQGNGGGPprkgipeleQ 183
Cdd:cd08215  100 FPEEQIlDW-FVQICLALKYL-HSRKILHRDLKTQNIFLTKDGVVKLGdfGISKVLEsttdlAKTVVGTP---------Y 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 184 YDPPELadssgrvVREK---WSADMWRLGCLIWEV------FNGP-LPraaALRNpgKI----PKTLVPHYC----ELVG 245
Cdd:cd08215  169 YLSPEL-------CENKpynYKSDIWALGCVLYELctlkhpFEANnLP---ALVY--KIvkgqYPPIPSQYSselrDLVN 236
                        250
                 ....*....|....*....
gi 115430241 246 A----NPKVRPNPARFLQN 260
Cdd:cd08215  237 SmlqkDPEKRPSANEILSS 255
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
69-260 5.11e-07

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: 51.94  E-value: 5.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  69 KTLRHPNILAYIDGLETEKCLHVVTEAVT--PLGIYLKARveaGGLKELEISWGLHQIVKALSFLvNDCSLIHNNVCMAA 146
Cdd:cd14188   56 RILHHKHVVQFYHYFEDKENIYILLEYCSrrSMAHILKAR---KVLTEPEVRYYLRQIVSGLKYL-HEQEILHRDLKLGN 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 147 VFVDRAGEWKLGglDYMYSAQGNGGGPPRKGIPELEQYDPPELADSSGrvvrEKWSADMWRLGCLIWEVFNGPLP----- 221
Cdd:cd14188  132 FFINENMELKVG--DFGLAARLEPLEHRRRTICGTPNYLSPEVLNKQG----HGCESDIWALGCVMYTMLLGRPPfettn 205
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 115430241 222 --------RAAALRNPGKIPKTLVPHYCELVGANPKVRPNPARFLQN 260
Cdd:cd14188  206 lketyrciREARYSLPSSLLAPAKHLIASMLSKNPEDRPSLDEIIRH 252
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
69-218 5.88e-07

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: 51.46  E-value: 5.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  69 KTLRHPNILAYIDGLETEKCLHVVTEAVtpLGIYLKARVEA-GGLKELEISWGLHQIVKALSFLvNDCSLIHNNVCMAAV 147
Cdd:cd06627   54 KKLNHPNIVKYIGSVKTKDSLYIILEYV--ENGSLASIIKKfGKFPESLVAVYIYQVLEGLAYL-HEQGVIHRDIKGANI 130
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115430241 148 FVDRAGEWKLGglDYMYSAQGNGGGPPRKGIPELEQYDPPELADSSGRVVrekwSADMWRLGCLIWEVFNG 218
Cdd:cd06627  131 LTTKDGLVKLA--DFGVATKLNEVEKDENSVVGTPYWMAPEVIEMSGVTT----ASDIWSVGCTVIELLTG 195
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
69-212 6.00e-07

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: 51.79  E-value: 6.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  69 KTLRHPNILAYIDGLETEKCLHVVTEAVT--PLGIYLKARveaGGLKELEISWGLHQIVKALSFLvNDCSLIHNNVCMAA 146
Cdd:cd14099   56 RSLKHPNIVKFHDCFEDEENVYILLELCSngSLMELLKRR---KALTEPEVRYFMRQILSGVKYL-HSNRIIHRDLKLGN 131
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 147 VFVDRAGEWKLGglDYMYSAQGNGGGPPRK---GIPeleQYDPPE-LADSSGrvvrEKWSADMWRLGCLI 212
Cdd:cd14099  132 LFLDENMNVKIG--DFGLAARLEYDGERKKtlcGTP---NYIAPEvLEKKKG----HSFEVDIWSLGVIL 192
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
35-248 8.66e-07

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: 51.27  E-value: 8.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  35 RKKATGSPVSIFVYdvkPGAEEQTQVAKAAF---KRFKTLRHPNILAYIDGLETEKCLHVVTEAV--TPLGIYLKArveA 109
Cdd:cd07846   21 RHKETGQIVAIKKF---LESEDDKMVKKIAMreiKMLKQLRHENLVNLIEVFRRKKRWYLVFEFVdhTVLDDLEKY---P 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 110 GGLKELEISWGLHQIVKALSFLVNDcSLIHNNVCMAAVFVDRAGEWKLggLDYMYSAQGNGGGPPRKGIPELEQYDPPEL 189
Cdd:cd07846   95 NGLDESRVRKYLFQILRGIDFCHSH-NIIHRDIKPENILVSQSGVVKL--CDFGFARTLAAPGEVYTDYVATRWYRAPEL 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115430241 190 --ADSS-GRVVrekwsaDMWRLGCLIWEVFNG-PL-PRAAALRNPGKIPK---TLVPHYCELVGANP 248
Cdd:cd07846  172 lvGDTKyGKAV------DVWAVGCLVTEMLTGePLfPGDSDIDQLYHIIKclgNLIPRHQELFQKNP 232
Pkinase pfam00069
Protein kinase domain;
33-221 1.24e-06

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 49.93  E-value: 1.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241   33 RGRKKATGSPVSIFVYDVKPGAEEQTQVAKAAFKRFKTLRHPNILAYIDGLETEKCLHVVTEAVtPLGIYLKARVEAGGL 112
Cdd:pfam00069  17 KAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV-EGGSLFDLLSEKGAF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  113 KELEISWGLHQIVKALsflvndcsliHNNVCMaAVFVdragewklGGLDYMysAqgngggpprkgiPEL---EQYDPPel 189
Cdd:pfam00069  96 SEREAKFIMKQILEGL----------ESGSSL-TTFV--------GTPWYM--A------------PEVlggNPYGPK-- 140
                         170       180       190
                  ....*....|....*....|....*....|..
gi 115430241  190 adssgrvvrekwsADMWRLGCLIWEVFNGPLP 221
Cdd:pfam00069 141 -------------VDVWSLGCILYELLTGKPP 159
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
55-305 3.86e-06

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 50.40  E-value: 3.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  55 EEQTQVAKAAFKRFKTLRHPNILAYIDGLETEKCLHVVTEAVT--PLGIYLKARV-EAGGLKELEISWGLHQIVKALSFL 131
Cdd:PTZ00267 106 ERQAAYARSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSggDLNKQIKQRLkEHLPFQEYEVGLLFYQIVLALDEV 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 132 VNDCsLIHNNVCMAAVFVDRAGEWKLGglDYMYSAQGNGG-----GPPRKGIPeleQYDPPELADssgrvvREKWS--AD 204
Cdd:PTZ00267 186 HSRK-MMHRDLKSANIFLMPTGIIKLG--DFGFSKQYSDSvsldvASSFCGTP---YYLAPELWE------RKRYSkkAD 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 205 MWRLGCLIWEV------FNGPLPRAAALR--------NPGKIPKTLVPHYCELVGANPKVRPNPARFLQNcrapgGFMsn 270
Cdd:PTZ00267 254 MWSLGVILYELltlhrpFKGPSQREIMQQvlygkydpFPCPVSSGMKALLDPLLSKNPALRPTTQQLLHT-----EFL-- 326
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 115430241 271 RFVeTNLFlEEI----QIKEPAEKQKFFQELSKSLDAFP 305
Cdd:PTZ00267 327 KYV-ANLF-QDIvrhsETISPHDREEILRQLQESGERAP 363
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
50-221 4.70e-06

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: 49.03  E-value: 4.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241   50 VKPGAEEQTQvakAAFKR----FKTLRHPNILAYIdGLetekCLH-----VVTEAVT--PLGIYLKARVEAGGLKELeIS 118
Cdd:pfam07714  36 LKEGADEEER---EDFLEeasiMKKLDHPNIVKLL-GV----CTQgeplyIVTEYMPggDLLDFLRKHKRKLTLKDL-LS 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  119 WGlHQIVKALSFLvNDCSLIHNNVCMAAVFVDRAGEWKLG--GL------DYMYSAQGNGGGPPRkgipeleqYDPPE-L 189
Cdd:pfam07714 107 MA-LQIAKGMEYL-ESKNFVHRDLAARNCLVSENLVVKISdfGLsrdiydDDYYRKRGGGKLPIK--------WMAPEsL 176
                         170       180       190
                  ....*....|....*....|....*....|...
gi 115430241  190 ADssgRVVREKwsADMWRLGCLIWEVF-NGPLP 221
Cdd:pfam07714 177 KD---GKFTSK--SDVWSFGVLLWEIFtLGEQP 204
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
59-239 6.51e-06

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: 48.35  E-value: 6.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  59 QVAKAAFKR----FKTLRHPNILAYIDGLETEKCLHVVTEAVTplGIYLKARVEAGG---LKE-LEIswgLHQIVKALSF 130
Cdd:cd14014   41 EEFRERFLRearaLARLSHPNIVRVYDVGEDDGRPYIVMEYVE--GGSLADLLRERGplpPREaLRI---LAQIADALAA 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 131 LvNDCSLIHNNVCMAAVFVDRAGEWKLG--GLDYMYSAQGNGGGPPRKGIPeleQYDPPELAdsSGRVVREKwsADMWRL 208
Cdd:cd14014  116 A-HRAGIVHRDIKPANILLTEDGRVKLTdfGIARALGDSGLTQTGSVLGTP---AYMAPEQA--RGGPVDPR--SDIYSL 187
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 115430241 209 GCLIWEVFNGPLPRAAA---------LRNPGKIPKTLVPH 239
Cdd:cd14014  188 GVVLYELLTGRPPFDGDspaavlakhLQEAPPPPSPLNPD 227
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
71-215 6.76e-06

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: 48.58  E-value: 6.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  71 LRHPNILAYIDGLETEKCLHVVTEAVTPLGIYLKARVEAGGL-KELEISWGLHQIVKALSFlVNDCSLIHNNVCMAAVFV 149
Cdd:cd08221   56 LNHDNIITYYNHFLDGESLFIEMEYCNGGNLHDKIAQQKNQLfPEEVVLWYLYQIVSAVSH-IHKAGILHRDIKTLNIFL 134
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115430241 150 DRAGEWKLGglDYMYSAQGNGGGPPRKGIPELEQYDPPELAdssgRVVREKWSADMWRLGCLIWEV 215
Cdd:cd08221  135 TKADLVKLG--DFGISKVLDSESSMAESIVGTPYYMSPELV----QGVKYNFKSDIWAVGCVLYEL 194
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
69-222 7.52e-06

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: 48.36  E-value: 7.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  69 KTLRHPNILAYIDGLETEKCLHVVTE-----AVTPLGIYLKARveaggLKELEISWGLHQIVKALSFL-VNDCslIHNNV 142
Cdd:cd06614   51 KECKHPNIVDYYDSYLVGDELWVVMEymdggSLTDIITQNPVR-----MNESQIAYVCREVLQGLEYLhSQNV--IHRDI 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 143 CMAAVFVDRAGEWKLGglDYMYSAQGNGGGPPRKGI--------PEL---EQYDPpeladssgrvvrekwSADMWRLGCL 211
Cdd:cd06614  124 KSDNILLSKDGSVKLA--DFGFAAQLTKEKSKRNSVvgtpywmaPEVikrKDYGP---------------KVDIWSLGIM 186
                        170
                 ....*....|.
gi 115430241 212 IWEVFNGPLPR 222
Cdd:cd06614  187 CIEMAEGEPPY 197
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
68-218 9.21e-06

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 47.90  E-value: 9.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  68 FKTLRHPNILAYIDGLETEKCLHVVTEAVTplGIYLKARVEA-GGLKELEISWGLHQIVKALSFLvNDCSLIHNNVCMAA 146
Cdd:cd06606   53 LSSLKHPNIVRYLGTERTENTLNIFLEYVP--GGSLASLLKKfGKLPEPVVRKYTRQILEGLEYL-HSNGIVHRDIKGAN 129
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115430241 147 VFVDRAGEWKLGglD-----YMYSAQGNGGGPPRKGIPeleQYDPPELADSSGrvvrEKWSADMWRLGCLIWEVFNG 218
Cdd:cd06606  130 ILVDSDGVVKLA--DfgcakRLAEIATGEGTKSLRGTP---YWMAPEVIRGEG----YGRAADIWSLGCTVIEMATG 197
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
31-220 1.40e-05

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: 47.86  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  31 LHRGRKKATGSPVSIfvYDVKPGAEEQT-QVAKAAFKRFKTLRHPNILAYIDGLETEKCLHVVTEAV-TPLGIYLKARVE 108
Cdd:cd07836   16 VYKGRNRTTGEIVAL--KEIHLDAEEGTpSTAIREISLMKELKHENIVRLHDVIHTENKLMLVFEYMdKDLKKYMDTHGV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 109 AGGLKELEISWGLHQIVKALSFlVNDCSLIHNNVCMAAVFVDRAGEWKLGglDYmysaqgnggGPPRK-GIP------EL 181
Cdd:cd07836   94 RGALDPNTVKSFTYQLLKGIAF-CHENRVLHRDLKPQNLLINKRGELKLA--DF---------GLARAfGIPvntfsnEV 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 115430241 182 EQ--YDPPELADSSgRVVREkwSADMWRLGCLIWEVFNG-PL 220
Cdd:cd07836  162 VTlwYRAPDVLLGS-RTYST--SIDIWSVGCIMAEMITGrPL 200
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
33-131 1.62e-05

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: 47.09  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  33 RGRKKATGSPVSIFVYDVKPGAEEQTQVAKAAFKRFKTLRHPNILAYIDGLETEKCLHVVTEAVTplGIYLKAR-VEAGG 111
Cdd:cd05117   18 LAVHKKTGEEYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMELCT--GGELFDRiVKKGS 95
                         90       100
                 ....*....|....*....|
gi 115430241 112 LKELEISWGLHQIVKALSFL 131
Cdd:cd05117   96 FSEREAAKIMKQILSAVAYL 115
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
69-260 1.80e-05

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: 47.24  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  69 KTLRHPNILAYIDGLETEKCLHVVTEAVTPLGIY-LKARVEAggLKELEISWGLHQIVKALSFLVNDcSLIHNNVCMAAV 147
Cdd:cd14187   62 RSLAHQHVVGFHGFFEDNDFVYVVLELCRRRSLLeLHKRRKA--LTEPEARYYLRQIILGCQYLHRN-RVIHRDLKLGNL 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 148 FVDRAGEWKLGglDYMYSAQGNGGGPPRKGIPELEQYDPPELADSSGrvvrEKWSADMWRLGCLIWEVFNGPLPRAAAL- 226
Cdd:cd14187  139 FLNDDMEVKIG--DFGLATKVEYDGERKKTLCGTPNYIAPEVLSKKG----HSFEVDIWSIGCIMYTLLVGKPPFETSCl 212
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 115430241 227 --------RNPGKIPKTLVPHYCELVG----ANPKVRPNPARFLQN 260
Cdd:cd14187  213 ketylrikKNEYSIPKHINPVAASLIQkmlqTDPTARPTINELLND 258
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
69-229 2.38e-05

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: 46.77  E-value: 2.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  69 KTLRHPNILAYIDG--LETEKCLHVVTE--AVTPLGIYLKARVEAGGLKELEISWG-LHQIVKALsflvNDC-------- 135
Cdd:cd08217   54 RELKHPNIVRYYDRivDRANTTLYIVMEycEGGDLAQLIKKCKKENQYIPEEFIWKiFTQLLLAL----YEChnrsvggg 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 136 SLIHNNVCMAAVFVDRAGEWKLG--GLDYMYS-----AQGNGGGPPrkgipeleqYDPPELAdsSGRVVREKwsADMWRL 208
Cdd:cd08217  130 KILHRDLKPANIFLDSDNNVKLGdfGLARVLShdssfAKTYVGTPY---------YMSPELL--NEQSYDEK--SDIWSL 196
                        170       180
                 ....*....|....*....|.
gi 115430241 209 GCLIWEvfngplprAAALRNP 229
Cdd:cd08217  197 GCLIYE--------LCALHPP 209
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
39-221 2.81e-05

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: 46.73  E-value: 2.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  39 TGSPVSIFVYDvKPGAEEQTQVAKAaFKR----FKTLRHPNILAYIDGLETEKCLHVVTEaVTPLGIYLKARVEAGGLKE 114
Cdd:cd14070   26 TGEKVAIKVID-KKKAKKDSYVTKN-LRRegriQQMIRHPNITQLLDILETENSYYLVME-LCPGGNLMHRIYDKKRLEE 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 115 LEISWGLHQIVKALSFLvNDCSLIHNNVCMAAVFVDRAGEWKLGGLDYMYSAQGNGGGPP---RKGIPeleQYDPPELad 191
Cdd:cd14070  103 REARRYIRQLVSAVEHL-HRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCAGILGYSDPfstQCGSP---AYAAPEL-- 176
                        170       180       190
                 ....*....|....*....|....*....|..
gi 115430241 192 ssgrVVREKW--SADMWRLGCLIWEVFNGPLP 221
Cdd:cd14070  177 ----LARKKYgpKVDVWSIGVNMYAMLTGTLP 204
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
73-259 3.38e-05

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: 46.23  E-value: 3.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  73 HPNILAYIDGLETEKCLHVVTEaVTPLGIYLKARVEAGGLKEL---EISWG-LHQIVKALSFLvNDCSLIHNNVCMAAVF 148
Cdd:cd08530   58 HPNIIRYKEAFLDGNRLCIVME-YAPFGDLSKLISKRKKKRRLfpeDDIWRiFIQMLRGLKAL-HDQKILHRDLKSANIL 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 149 VDRAGEWKLGGLDYMYSAQGNGG----GPPRKGIPELEQ---YDppeladssgrvvrekWSADMWRLGCLIWEVFNGPLP 221
Cdd:cd08530  136 LSAGDLVKIGDLGISKVLKKNLAktqiGTPLYAAPEVWKgrpYD---------------YKSDIWSLGCLLYEMATFRPP 200
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 115430241 222 ----RAAALRNP---GKIPKtLVPHYC--------ELVGANPKVRPNPARFLQ 259
Cdd:cd08530  201 fearTMQELRYKvcrGKFPP-IPPVYSqdlqqiirSLLQVNPKKRPSCDKLLQ 252
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
33-221 3.72e-05

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: 46.17  E-value: 3.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  33 RGRKKATGSPVSIFVYDVKPGAEEQtQVAKAAFKRFKTLRHPNILAYIDGLETEKCLHVVTEAVTPLGIYlKARVEAGGL 112
Cdd:cd14088   19 RAKDKTTGKLYTCKKFLKRDGRKVR-KAAKNEINILKMVKHPNILQLVDVFETRKEYFIFLELATGREVF-DWILDQGYY 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 113 KELEISWGLHQIVKALSFLVNDCsLIHNNVCMA-AVFVDRAGEWKLGGLDYMYSAQGNGGGPPRKGIPEleqYDPPELad 191
Cdd:cd14088   97 SERDTSNVIRQVLEAVAYLHSLK-IVHRNLKLEnLVYYNRLKNSKIVISDFHLAKLENGLIKEPCGTPE---YLAPEV-- 170
                        170       180       190
                 ....*....|....*....|....*....|..
gi 115430241 192 ssgrVVREKWS--ADMWRLGCLIWEVFNGPLP 221
Cdd:cd14088  171 ----VGRQRYGrpVDCWAIGVIMYILLSGNPP 198
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
68-229 4.41e-05

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: 46.17  E-value: 4.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  68 FKTLRHPNILAYIDGLETEKCLHVVTEA-----VTPLGIYLKARVEAggLKELEISWGLHQIVKALSFLvNDCSLIHNNV 142
Cdd:cd08228   56 LKQLNHPNVIKYLDSFIEDNELNIVLELadagdLSQMIKYFKKQKRL--IPERTVWKYFVQLCSAVEHM-HSRRVMHRDI 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 143 CMAAVFVDRAGEWKLG--GLDYMYSAQGNGG----GPPrkgipeleQYDPPELADSSGRvvreKWSADMWRLGCLIWEVf 216
Cdd:cd08228  133 KPANVFITATGVVKLGdlGLGRFFSSKTTAAhslvGTP--------YYMSPERIHENGY----NFKSDIWSLGCLLYEM- 199
                        170
                 ....*....|...
gi 115430241 217 ngplpraAALRNP 229
Cdd:cd08228  200 -------AALQSP 205
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
34-221 8.65e-05

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: 44.89  E-value: 8.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  34 GRKKATGSPVSIFVYDVKPGAEEQTQVAKAAFkrFKTLRHPNILAYIDGLETEKCLHVVTE-----AVTPLgiyLKARVe 108
Cdd:cd05122   19 ARHKKTGQIVAIKKINLESKEKKESILNEIAI--LKKCKHPNIVKYYGSYLKKDELWIVMEfcsggSLKDL---LKNTN- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 109 aGGLKELEISWGLHQIVKALSFLVNDcSLIHNNVCMAAVFVDRAGEWKLGglDYMYSAQGNGGGPPRK--GIPeleQYDP 186
Cdd:cd05122   93 -KTLTEQQIAYVCKEVLKGLEYLHSH-GIIHRDIKAANILLTSDGEVKLI--DFGLSAQLSDGKTRNTfvGTP---YWMA 165
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 115430241 187 PEladssgRVVREKWS--ADMWRLGCLIWEVFNGPLP 221
Cdd:cd05122  166 PE------VIQGKPYGfkADIWSLGITAIEMAEGKPP 196
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
55-185 1.53e-04

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 44.22  E-value: 1.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  55 EEQTQ-VAKAAFKRF-------KTLRHPNILAYIDG----LETEKCLHVVTEAVTP--LGIYLKaRVEAGGLKELEiSWG 120
Cdd:cd14033   33 ELQTRkLSKGERQRFseevemlKGLQHPNIVRFYDSwkstVRGHKCIILVTELMTSgtLKTYLK-RFREMKLKLLQ-RWS 110
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115430241 121 lHQIVKALSFLVNDC-SLIHNNVCMAAVFVD-RAGEWKLG--GLDYMYSAQGNGG--GPPRKGIPEL--EQYD 185
Cdd:cd14033  111 -RQILKGLHFLHSRCpPILHRDLKCDNIFITgPTGSVKIGdlGLATLKRASFAKSviGTPEFMAPEMyeEKYD 182
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
49-260 1.59e-04

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: 44.35  E-value: 1.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  49 DVKPGAEEQTQVAKAAFKRFKTLRHPNILAYIDGLETEKC-LHVVTEAVTPLGIYLKARVEAGGLKELE--ISWGLhQIV 125
Cdd:cd08223   34 NLKNASKRERKAAEQEAKLLSKLKHPNIVSYKESFEGEDGfLYIVMGFCEGGDLYTRLKEQKGVLLEERqvVEWFV-QIA 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 126 KALSFLvNDCSLIHNNVCMAAVFVDRAGEWKLGGLDYMYSAQG-NGGGPPRKGIPeleQYDPPELAdsSGRVVREKwsAD 204
Cdd:cd08223  113 MALQYM-HERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESsSDMATTLIGTP---YYMSPELF--SNKPYNHK--SD 184
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 205 MWRLGCLIWEV------FNGPLPRAAALRN-PGKI---PKTLVPHYCELVGA----NPKVRPNPARFLQN 260
Cdd:cd08223  185 VWALGCCVYEMatlkhaFNAKDMNSLVYKIlEGKLppmPKQYSPELGELIKAmlhqDPEKRPSVKRILRQ 254
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
59-160 2.08e-04

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: 43.75  E-value: 2.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  59 QVAKAAFKRF-------KTLRHPNILAYIDGLETE--KCLHVVTEAVTP--LGIYLKaRVEAGGLKELEiSWGLhQIVKA 127
Cdd:cd13983   38 KLPKAERQRFkqeieilKSLKHPNIIKFYDSWESKskKEVIFITELMTSgtLKQYLK-RFKRLKLKVIK-SWCR-QILEG 114
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 115430241 128 LSFLVN-DCSLIHNNVCMAAVFVDRA-GEWKLGGL 160
Cdd:cd13983  115 LNYLHTrDPPIIHRDLKCDNIFINGNtGEVKIGDL 149
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
91-221 2.11e-04

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


Pssm-ID: 270633 [Multi-domain]  Cd Length: 259  Bit Score: 44.01  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  91 VVTEAVT--PLGIYLKARveaGGLkeLEISWGL---HQIVKALSFLvNDCSLIHNNVCMAAVFVDRAGEwKLGGLDYMYS 165
Cdd:cd05037   78 MVQEYVRygPLDKYLRRM---GNN--VPLSWKLqvaKQLASALHYL-EDKKLIHGNVRGRNILLAREGL-DGYPPFIKLS 150
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 115430241 166 AQGNGGGPPRKGIPELeqyDPPELADSSGRVVREKWS--ADMWRLGCLIWEVF-NGPLP 221
Cdd:cd05037  151 DPGVPITVLSREERVD---RIPWIAPECLRNLQANLTiaADKWSFGTTLWEICsGGEEP 206
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
30-211 3.34e-04

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: 43.03  E-value: 3.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  30 ALHRGRKKATGSPVSIFVYDVKPGAEEQtqvAKAAFKRFKTLRHPNILAYIDGLETEKCLHVVTEAVTplGIYLKARV-E 108
Cdd:cd14006    8 VVKRCIEKATGREFAAKFIPKRDKKKEA---VLREISILNQLQHPRIIQLHEAYESPTELVLILELCS--GGELLDRLaE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 109 AGGLKELEISWGLHQIVKALSFLvNDCSLIH-----NNVCMAAVfvdRAGEWKLggLDYMYSAQGNGGGPPR--KGIPEl 181
Cdd:cd14006   83 RGSLSEEEVRTYMRQLLEGLQYL-HNHHILHldlkpENILLADR---PSPQIKI--IDFGLARKLNPGEELKeiFGTPE- 155
                        170       180       190
                 ....*....|....*....|....*....|
gi 115430241 182 eqYDPPELADSSGRVVrekwSADMWRLGCL 211
Cdd:cd14006  156 --FVAPEIVNGEPVSL----ATDMWSIGVL 179
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
33-221 6.45e-04

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: 42.37  E-value: 6.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  33 RGRKKATGSPVSIFVYDVKPGAEEQTQVaKAAFKRFKTLRHPNILAYIDGLETEKCLHVVTEAVtPLGIYLKARVEAGGL 112
Cdd:cd14078   21 LATHILTGEKVAIKIMDKKALGDDLPRV-KTEIEALKNLSHQHICRLYHVIETDNKIFMVLEYC-PGGELFDYIVAKDRL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 113 KELEISWGLHQIVKALSFlVNDCSLIHNNVCMAAVFVDRAGEWKLggLDYMYSAQGNGG---------GPPRKGIPEL-- 181
Cdd:cd14078   99 SEDEARVFFRQIVSAVAY-VHSQGYAHRDLKPENLLLDEDQNLKL--IDFGLCAKPKGGmdhhletccGSPAYAAPELiq 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 115430241 182 -EQYDPPEladssgrvvrekwsADMWRLGCLIWEVFNGPLP 221
Cdd:cd14078  176 gKPYIGSE--------------ADVWSMGVLLYALLCGFLP 202
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
98-252 7.33e-04

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; 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 cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. Jaks 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 Jak3 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: 271110 [Multi-domain]  Cd Length: 260  Bit Score: 42.20  E-value: 7.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  98 PLGIYLKARVEAGglkELEISWGLhQIVKALSFLVN---DCSLIHNNVCMAAVFVDRagewklggldymysaQGNGGGPP 174
Cdd:cd14208   87 ALDLYLKKQQQKG---PVAISWKL-QVVKQLAYALNyleDKQLVHGNVSAKKVLLSR---------------EGDKGSPP 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 175 RkgipeLEQYDP---PELADSSGRVVREKW--------------SADMWRLGCLIWEVFNGPLPRAAALRNPGKIP---- 233
Cdd:cd14208  148 F-----IKLSDPgvsIKVLDEELLAERIPWvapeclsdpqnlalEADKWGFGATLWEIFSGGHMPLSALDPSKKLQfynd 222
                        170       180
                 ....*....|....*....|....*...
gi 115430241 234 -KTL-VPHYCEL-------VGANPKVRP 252
Cdd:cd14208  223 rKQLpAPHWIELasliqqcMSYNPLLRP 250
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
71-223 7.46e-04

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: 41.94  E-value: 7.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  71 LRHPNILAYIDGLETEKCLHVVTEAVTPLGIYLKARVEaGGLKELEISWGLHQIVKALSFLvNDCSLIHNNVCMAAVFVD 150
Cdd:cd14075   58 LHHPNIIRLYEVVETLSKLHLVMEYASGGELYTKISTE-GKLSESEAKPLFAQIVSAVKHM-HENNIIHRDLKAENVFYA 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 151 RAGEWKLGglDYMYSAQGNG--------GGPPrkgipeleqYDPPEL-ADSS--GRVVrekwsaDMWRLGCLIWEVFNGP 219
Cdd:cd14075  136 SNNCVKVG--DFGFSTHAKRgetlntfcGSPP---------YAAPELfKDEHyiGIYV------DIWALGVLLYFMVTGV 198

                 ....*
gi 115430241 220 LP-RA 223
Cdd:cd14075  199 MPfRA 203
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
99-218 7.93e-04

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely expressed in many tissues. It 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 cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Despite this, the presumed pseudokinase (repeat 1) domain of Jak2 exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Inactivation of the repeat 1 domain increased Jak2 basal activity, suggesting that it modulates the kinase activity of the C-terminal catalytic (repeat 2) domain. The Jak2 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: 270663 [Multi-domain]  Cd Length: 262  Bit Score: 42.24  E-value: 7.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  99 LGIYLKARVEAgglkeLEISWGLH---QIVKALSFLvNDCSLIHNNVCMAAVFVDRAGEWKLGGLDYMYSAQgngggP-- 173
Cdd:cd05078   90 LDTYLKKNKNC-----INILWKLEvakQLAWAMHFL-EEKTLVHGNVCAKNILLIREEDRKTGNPPFIKLSD-----Pgi 158
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 115430241 174 -----PRKGIPELEQYDPPELADSSGRVvreKWSADMWRLGCLIWEVFNG 218
Cdd:cd05078  159 sitvlPKDILLERIPWVPPECIENPKNL---SLATDKWSFGTTLWEICSG 205
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
69-215 1.00e-03

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: 41.72  E-value: 1.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  69 KTLRHPNILAYIDGLETEKCLHVVTEAVTPLGIYLKARVEAGGL-KELEI-SWGLhQIVKALSFlVNDCSLIHNNVCMAA 146
Cdd:cd08218   54 SKMKHPNIVQYQESFEENGNLYIVMDYCDGGDLYKRINAQRGVLfPEDQIlDWFV-QLCLALKH-VHDRKILHRDIKSQN 131
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115430241 147 VFVDRAGEWKLGglDYMYSAQGNGGGPPRKGIPELEQYDPPELADSsgRVVREKwsADMWRLGCLIWEV 215
Cdd:cd08218  132 IFLTKDGIIKLG--DFGIARVLNSTVELARTCIGTPYYLSPEICEN--KPYNNK--SDIWALGCVLYEM 194
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
35-261 1.17e-03

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: 41.59  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  35 RKKATGSPVSI--FVydvkpGAEEQTQVAKAAF---KRFKTLRHPNILAYIDGLETEKCLHVVTEAV--TPLGiYLKARV 107
Cdd:cd07847   21 RNRETGQIVAIkkFV-----ESEDDPVIKKIALreiRMLKQLKHPNLVNLIEVFRRKRKLHLVFEYCdhTVLN-ELEKNP 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 108 EagGLKELEISWGLHQIVKALSFL-VNDCslIHNNVCMAAVFVDRAGEWKLGglDYMYSAQGNGGGPP----------RK 176
Cdd:cd07847   95 R--GVPEHLIKKIIWQTLQAVNFChKHNC--IHRDVKPENILITKQGQIKLC--DFGFARILTGPGDDytdyvatrwyRA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 177 giPEL----EQYDPPeladssgrvvrekwsADMWRLGCLIWEVFNG-PL-PRAAALRNPGKIPKT---LVPHYCELVGAN 247
Cdd:cd07847  169 --PELlvgdTQYGPP---------------VDVWAIGCVFAELLTGqPLwPGKSDVDQLYLIRKTlgdLIPRHQQIFSTN 231
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 115430241 248 ---------------------PKVRPNPARFLQNC 261
Cdd:cd07847  232 qffkglsipepetrepleskfPNISSPALSFLKGC 266
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
34-221 2.08e-03

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: 40.85  E-value: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  34 GRKKATGSPVSIFVYD----VKPGAEEQTQVAKAAFKRfktLRHPNILAYIDGLETEKCLHVVTEAVTplGIYLKARVEA 109
Cdd:cd14663   19 ARNTKTGESVAIKIIDkeqvAREGMVEQIKREIAIMKL---LRHPNIVELHEVMATKTKIFFVMELVT--GGELFSKIAK 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 110 GG-LKELEISWGLHQIVKALSFlvndC---SLIHNNVCMAAVFVDRAGEWKLG--GLDYMYSA-QGNGGGPPRKGIPele 182
Cdd:cd14663   94 NGrLKEDKARKYFQQLIDAVDY----ChsrGVFHRDLKPENLLLDEDGNLKISdfGLSALSEQfRQDGLLHTTCGTP--- 166
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 115430241 183 QYDPPELADSSGrvvREKWSADMWRLGCLIWEVFNGPLP 221
Cdd:cd14663  167 NYVAPEVLARRG---YDGAKADIWSCGVILFVLLAGYLP 202
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
69-221 2.28e-03

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: 40.83  E-value: 2.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  69 KTLRHPNILAYIDGLETEKCLHVVTEAVtPLGIYLKARVEAGGLKELEISWGLHQIVKALSFLvNDCSLIHNNVCMAAVF 148
Cdd:cd06629   63 KDLDHPNIVQYLGFEETEDYFSIFLEYV-PGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYL-HSKGILHRDLKADNIL 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 149 VDRAGEWKLGglDYMYS-----AQGNGGGPPRKG-IPELeqydPPELADSSGRvvreKWSA--DMWRLGCLIWEVFNGPL 220
Cdd:cd06629  141 VDLEGICKIS--DFGISkksddIYGNNGATSMQGsVFWM----APEVIHSQGQ----GYSAkvDIWSLGCVVLEMLAGRR 210

                 .
gi 115430241 221 P 221
Cdd:cd06629  211 P 211
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
69-221 2.44e-03

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: 40.68  E-value: 2.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  69 KTLRHPNILAYIDGLETEKCLHVVTEAVT--PLGIYLKARveaGGLKELEISWGLHQIVKALSFLVNDcSLIHNNVCMAA 146
Cdd:cd14189   56 RDLHHKHVVKFSHHFEDAENIYIFLELCSrkSLAHIWKAR---HTLLEPEVRYYLKQIISGLKYLHLK-GILHRDLKLGN 131
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115430241 147 VFVDRAGEWKLGglDYMYSAQGNGGGPPRKGIPELEQYDPPELADSSGRVVRekwsADMWRLGCLIWEVFNGPLP 221
Cdd:cd14189  132 FFINENMELKVG--DFGLAARLEPPEQRKKTICGTPNYLAPEVLLRQGHGPE----SDVWSLGCVMYTLLCGNPP 200
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
71-260 2.56e-03

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: 40.47  E-value: 2.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  71 LRHPNILAYIDGLETEKCLHVVTE--AVTPLGIYLKARVeAGGLKELEIsWGLH-QIVKALSFLVNDcSLIHNNVCMAAV 147
Cdd:cd08529   56 LNSPYVIKYYDSFVDKGKLNIVMEyaENGDLHSLIKSQR-GRPLPEDQI-WKFFiQTLLGLSHLHSK-KILHRDIKSMNI 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 148 FVDRAGEWKLG--GLDYMYSAQGNGG----GPPrkgipeleQYDPPELADssGRVVREKwsADMWRLGCLIWEVFNGPLP 221
Cdd:cd08529  133 FLDKGDNVKIGdlGVAKILSDTTNFAqtivGTP--------YYLSPELCE--DKPYNEK--SDVWALGCVLYELCTGKHP 200
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 115430241 222 RAAA---------LR---NPgkIPKTLVPHYCELVGA----NPKVRPNPARFLQN 260
Cdd:cd08529  201 FEAQnqgalilkiVRgkyPP--ISASYSQDLSQLIDScltkDYRQRPDTTELLRN 253
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
37-139 3.29e-03

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: 40.05  E-value: 3.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  37 KATGSPVSIFVYDVKP--GAEEQTQVAKAAFKRfktLRHPNILAYIDGLETEKCLHVVTEAVTplGIYLKAR-VEAGGLK 113
Cdd:cd14083   25 KATGKLVAIKCIDKKAlkGKEDSLENEIAVLRK---IKHPNIVQLLDIYESKSHLYLVMELVT--GGELFDRiVEKGSYT 99
                         90       100
                 ....*....|....*....|....*.
gi 115430241 114 ELEISWGLHQIVKALSFLvNDCSLIH 139
Cdd:cd14083  100 EKDASHLIRQVLEAVDYL-HSLGIVH 124
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
32-214 4.73e-03

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: 39.86  E-value: 4.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  32 HRGRKKATGSPVSIfvYDVKPGAEEQTQ--VAKAAFKRFKTLR---HPNILAYIDGLETEKCLHVVTE-AVTPLGIYLKA 105
Cdd:cd07841   17 YKARDKETGRIVAI--KKIKLGERKEAKdgINFTALREIKLLQelkHPNIIGLLDVFGHKSNINLVFEfMETDLEKVIKD 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 106 RveAGGLKELEI-SWGLhQIVKALSFLvNDCSLIH-----NNvcmaaVFVDRAGEWKLG--GLDYMYsaqgngGGPPRKG 177
Cdd:cd07841   95 K--SIVLTPADIkSYML-MTLRGLEYL-HSNWILHrdlkpNN-----LLIASDGVLKLAdfGLARSF------GSPNRKM 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 115430241 178 IPEL--EQYDPPEL---ADSSGRvvrekwSADMWRLGCLIWE 214
Cdd:cd07841  160 THQVvtRWYRAPELlfgARHYGV------GVDMWSVGCIFAE 195
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
31-218 4.84e-03

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: 40.06  E-value: 4.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  31 LHRGRKKATGSPVSIFVYDVKpgaEEQ----TQVAKAAFkrFKTLRHPNILAYIDGLETEKCLHVVTEAV-TPLGIYLKA 105
Cdd:cd07869   21 VYKGKSKVNGKLVALKVIRLQ---EEEgtpfTAIREASL--LKGLKHANIVLLHDIIHTKETLTLVFEYVhTDLCQYMDK 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 106 rvEAGGLKELEISWGLHQIVKALSFlVNDCSLIHNNVCMAAVFVDRAGEWKLGGLdymysaqgngGGPPRKGIPELEQ-- 183
Cdd:cd07869   96 --HPGGLHPENVKLFLFQLLRGLSY-IHQRYILHRDLKPQNLLISDTGELKLADF----------GLARAKSVPSHTYsn 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 115430241 184 ------YDPPELADSSgrvVREKWSADMWRLGCLIWEVFNG 218
Cdd:cd07869  163 evvtlwYRPPDVLLGS---TEYSTCLDMWGVGCIFVEMIQG 200
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
31-165 6.27e-03

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: 39.59  E-value: 6.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  31 LHRGRKKATGSPVSIFVYDVKPGAEEQTQVAKAAFKRFKTLRHPNILAYIDGLETEKCLHVvteaVTPLGIY-----LKA 105
Cdd:cd08216   16 VHLAKHKPTNTLVAVKKINLESDSKEDLKFLQQEILTSRQLQHPNILPYVTSFVVDNDLYV----VTPLMAYgscrdLLK 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115430241 106 RVEAGGLKELEISWGLHQIVKALSFL-VNDCslIHNNVCMAAVFVDRAGEWKLGGLDYMYS 165
Cdd:cd08216   92 THFPEGLPELAIAFILRDVLNALEYIhSKGY--IHRSVKASHILISGDGKVVLSGLRYAYS 150
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
69-221 6.48e-03

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: 39.16  E-value: 6.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  69 KTLRHPNILAYIDGLETEKCLHVVTEAVT--PLGIYLkarVEAGGLKELEISWGLHQIVKALSFlvndCsliHN-NVC-- 143
Cdd:cd14081   56 KLIEHPNVLKLYDVYENKKYLYLVLEYVSggELFDYL---VKKGRLTEKEARKFFRQIISALDY----C---HShSIChr 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 144 ---MAAVFVDRAGEWKLGglDY-MYSAQGNGG------GPPRKGIPEL---EQYDppeladssGRvvrekwSADMWRLGC 210
Cdd:cd14081  126 dlkPENLLLDEKNNIKIA--DFgMASLQPEGSlletscGSPHYACPEVikgEKYD--------GR------KADIWSCGV 189
                        170
                 ....*....|.
gi 115430241 211 LIWEVFNGPLP 221
Cdd:cd14081  190 ILYALLVGALP 200
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
31-253 7.75e-03

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: 39.06  E-value: 7.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  31 LHRGRKKatGSPVSIFVYDVKPGAEEQTQvakaAFKR----FKTLRHPNILAYIDGLETEKCLHVVTEavtplgiYLkar 106
Cdd:cd13999    9 VYKGKWR--GTDVAIKKLKVEDDNDELLK----EFRRevsiLSKLRHPNIVQFIGACLSPPPLCIVTE-------YM--- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 107 vEAGGL------KELEISWGL-----HQIVKALSFLvNDCSLIH-----NNvcmaaVFVDRAGEWKLG--GLdymySAQG 168
Cdd:cd13999   73 -PGGSLydllhkKKIPLSWSLrlkiaLDIARGMNYL-HSPPIIHrdlksLN-----ILLDENFTVKIAdfGL----SRIK 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 169 NGGGPPRKGIPELEQYDPPELAdsSGRVVREKwsADMWRLGCLIWEVFNGPLP----------RAAALRN-PGKIPKTLV 237
Cdd:cd13999  142 NSTTEKMTGVVGTPRWMAPEVL--RGEPYTEK--ADVYSFGIVLWELLTGEVPfkelspiqiaAAVVQKGlRPPIPPDCP 217
                        250       260
                 ....*....|....*....|
gi 115430241 238 PHYCELV----GANPKVRPN 253
Cdd:cd13999  218 PELSKLIkrcwNEDPEKRPS 237
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
31-170 7.99e-03

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


Pssm-ID: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 39.08  E-value: 7.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  31 LHRGRKKATGSPVSIFVYDVKPGAEEQTQVAKAAFKRFKTLRHPNILAYIDGLETEKCLHVvteaVTPLGIYLKAR---- 106
Cdd:cd08226   16 VYLARHTPTGTLVTVKITNLDNCSEEHLKALQNEVVLSHFFRHPNIMTHWTVFTEGSWLWV----ISPFMAYGSARgllk 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115430241 107 -VEAGGLKELEISWGLHQIVKALSFL-VNDCslIHNNVCMAAVFVDRAGEWKLGGLDYMYSAQGNG 170
Cdd:cd08226   92 tYFPEGMNEALIGNILYGAIKALNYLhQNGC--IHRSVKASHILISGDGLVSLSGLSHLYSMVTNG 155
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
61-221 8.70e-03

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 39.61  E-value: 8.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  61 AKAAFKR----FKTLRHPNILAYIDGLETEKCLHVVTEAVTplGIYLKARVEAGG-LKELEISWGLHQIVKALSFLvNDC 135
Cdd:COG0515   50 ARERFRRearaLARLNHPNIVRVYDVGEEDGRPYLVMEYVE--GESLADLLRRRGpLPPAEALRILAQLAEALAAA-HAA 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 136 SLIHNNVCMAAVFVDRAGEWKLG--GLDYMYSAQGNGGGPPRKGIPeleQYDPPELAdsSGRVVREkwSADMWRLGCLIW 213
Cdd:COG0515  127 GIVHRDIKPANILLTPDGRVKLIdfGIARALGGATLTQTGTVVGTP---GYMAPEQA--RGEPVDP--RSDVYSLGVTLY 199

                 ....*...
gi 115430241 214 EVFNGPLP 221
Cdd:COG0515  200 ELLTGRPP 207
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
32-221 9.66e-03

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: 38.65  E-value: 9.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  32 HRGRKKATGSPVSIFVYDV-KPGAEEQTQVakaafKR----FKTLRHPNILAYIDGLETEKCLHVVTEAVtPLGIYLKAR 106
Cdd:cd14003   17 KLARHKLTGEKVAIKIIDKsKLKEEIEEKI-----KReieiMKLLNHPNIIKLYEVIETENKIYLVMEYA-SGGELFDYI 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241 107 VEAGGLKELEISWGLHQIVKALSFLVNdCSLIH------NnvcmaaVFVDRAGEWKLGglDYMYSAQGNGGGPPRK--GI 178
Cdd:cd14003   91 VNNGRLSEDEARRFFQQLISAVDYCHS-NGIVHrdlkleN------ILLDKNGNLKII--DFGLSNEFRGGSLLKTfcGT 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 115430241 179 PeleQYDPPELADSSGRVVREkwsADMWRLGCLIWEVFNGPLP 221
Cdd:cd14003  162 P---AYAAPEVLLGRKYDGPK---ADVWSLGVILYAMLTGYLP 198
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
56-160 9.66e-03

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 38.93  E-value: 9.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115430241  56 EQTQVAKAAFKRFKT-------LRHPNILAYIDGLET----EKCLHVVTEAVTP--LGIYLKaRVEAGGLKELEiSWgLH 122
Cdd:cd14031   44 QDRKLTKAEQQRFKEeaemlkgLQHPNIVRFYDSWESvlkgKKCIVLVTELMTSgtLKTYLK-RFKVMKPKVLR-SW-CR 120
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 115430241 123 QIVKALSFL-VNDCSLIHNNVCMAAVFVD-RAGEWKLGGL 160
Cdd:cd14031  121 QILKGLQFLhTRTPPIIHRDLKCDNIFITgPTGSVKIGDL 160
 
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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