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Conserved domains on  [gi|530405409|ref|XP_005254228|]
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tau-tubulin kinase 2 isoform X1 [Homo sapiens]

Protein Classification

protein kinase family protein( domain architecture ID 229378)

protein kinase family protein may catalyze the transfer of the gamma-phosphoryl group from ATP to substrates such as serine/threonine and/or tyrosine residues on proteins, or may be a pseudokinase

CATH:  1.10.510.10
PubMed:  16244704
SCOP:  4003661

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
75-287 2.28e-152

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd14129:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 262  Bit Score: 457.98  E-value: 2.28e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   75 KMESGKDHVCRFIGCGRNDRFNYVVMQLQGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFA 154
Cdd:cd14129    50 KKLQGKDHVCRFIGCGRNDRFNYVVMQLQGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFA 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  155 MGRFPSTCRKCYMLDFGLARQFTNSCGDVRPPRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRK 234
Cdd:cd14129   130 MGRFPSTCRKCYMLDFGLARQFTNSCGDVRPPRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRK 209
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530405409  235 IKDKEQVGSIKERYDHRLMLKHLPPEFSIFLDHISSLDYFTKPDYQLLTSVFD 287
Cdd:cd14129   210 IKDKEQVGSIKERYEHRLMLKHLPPEFSVFLDHISGLDYFTKPDYQLLVSVFD 262
 
Name Accession Description Interval E-value
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
75-287 2.28e-152

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. Mutations in TTBK2 is associated with the development of spinocerebellar ataxia type 11, belonging to a group of neurodegenerative disorders characterized by progressive incoordination, dysarthria and impairment of eye movements. Brain tissues of SCA11 patients show the presence of neurofibrillary tangles and tau deposition in the brain, similar to Alzheimer's disease (AD) patients. The TTBK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271031 [Multi-domain]  Cd Length: 262  Bit Score: 457.98  E-value: 2.28e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   75 KMESGKDHVCRFIGCGRNDRFNYVVMQLQGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFA 154
Cdd:cd14129    50 KKLQGKDHVCRFIGCGRNDRFNYVVMQLQGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFA 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  155 MGRFPSTCRKCYMLDFGLARQFTNSCGDVRPPRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRK 234
Cdd:cd14129   130 MGRFPSTCRKCYMLDFGLARQFTNSCGDVRPPRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRK 209
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530405409  235 IKDKEQVGSIKERYDHRLMLKHLPPEFSIFLDHISSLDYFTKPDYQLLTSVFD 287
Cdd:cd14129   210 IKDKEQVGSIKERYEHRLMLKHLPPEFSVFLDHISGLDYFTKPDYQLLVSVFD 262
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
82-233 1.02e-20

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 97.01  E-value: 1.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   82 HVCRFIGCGRNDRFNYVVMQL-QGRNLADLRRSqsRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFps 160
Cdd:COG0515    68 NIVRVYDVGEEDGRPYLVMEYvEGESLADLLRR--RGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPD-- 143
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530405409  161 tcRKCYMLDFGLARQFTNScgDVRPPRAVAgfrGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWR 233
Cdd:COG0515   144 --GRVKLIDFGIARALGGA--TLTQTGTVV---GTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFD 209
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
81-270 9.80e-18

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 84.50  E-value: 9.80e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409     81 DHVCRFIGCGRNDRFNYVVMQL-QGRNLADLRRSqsRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMgrfp 159
Cdd:smart00220   57 PNIVRLYDVFEDEDKLYLVMEYcEGGDLFDLLKK--RGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILL---- 130
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409    160 STCRKCYMLDFGLARQFTnscgdvrPPRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRkikDKE 239
Cdd:smart00220  131 DEDGHVKLADFGLARQLD-------PGEKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFP---GDD 200
                           170       180       190
                    ....*....|....*....|....*....|.
gi 530405409    240 QVGSIKERydhrlmLKHLPPEFSIFLDHISS 270
Cdd:smart00220  201 QLLELFKK------IGKPKPPFPPPEWDISP 225
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
131-287 7.02e-15

putative serine/threonine kinase; Provisional


Pssm-ID: 165211 [Multi-domain]  Cd Length: 294  Bit Score: 76.91  E-value: 7.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  131 ILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLDFGLARQFTNSCGDVRPPRAVAGF-RGTVRYASINAHRNREM 209
Cdd:PHA02882  135 MLTTLEYIHEHGISHGDIKPENIMV----DGNNRGYIIDYGIASHFIIHGKHIEYSKEQKDLhRGTLYYAGLDAHNGACV 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  210 GRHDDLWSLFYMLVEFVVGQLPWRKIKDKEQV------GSIKERYDHRLMLKHLPPEFSIFLDHISSLDYFTKPDYQLLT 283
Cdd:PHA02882  211 TRRGDLESLGYCMLKWAGIKLPWKGFGHNGNLihaakcDFIKRLHEGKIKIKNANKFIYDFIECVTKLSYEEKPDYDALI 290

                  ....
gi 530405409  284 SVFD 287
Cdd:PHA02882  291 KIFD 294
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
90-179 8.26e-08

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 56.34  E-value: 8.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   90 GRNDRFNYVVMQL-QGRNLADLRRSqsRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFamgrfpstcrkcyML 168
Cdd:NF033483   76 GEDGGIPYIVMEYvDGRTLKDYIRE--HGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNI-------------LI 140
                          90       100
                  ....*....|....*....|
gi 530405409  169 ---------DFGLARQFTNS 179
Cdd:NF033483  141 tkdgrvkvtDFGIARALSST 160
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
81-175 3.49e-05

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: 46.72  E-value: 3.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409    81 DHVCRFIGCGRNDRFNYVVMQL-QGRNLAD-LRRSQSRgtFTISTTLRLGRQILESIESIHSVGFLHRDIkpsnfamgrf 158
Cdd:pfam07714   61 PNIVKLLGVCTQGEPLYIVTEYmPGGDLLDfLRKHKRK--LTLKDLLSMALQIAKGMEYLESKNFVHRDL---------- 128
                           90       100
                   ....*....|....*....|....*.
gi 530405409   159 psTCRKCyML---------DFGLARQ 175
Cdd:pfam07714  129 --AARNC-LVsenlvvkisDFGLSRD 151
BREX_PglW NF033442
BREX system serine/threonine kinase PglW; Members of this family are PglW, a predicted serine ...
99-174 2.86e-04

BREX system serine/threonine kinase PglW; Members of this family are PglW, a predicted serine/threonine kinase of the Pgl (phage growth limitation) system (now called BREX type 2) and the BREX type 3 system.


Pssm-ID: 468028 [Multi-domain]  Cd Length: 1387  Bit Score: 45.33  E-value: 2.86e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530405409   99 VMQLQGR-NLAD-LRRSqsrGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFPSTCRKCYMLDFGLAR 174
Cdd:NF033442  585 LLEYAGEqTLAErLRKE---GRLSLDLLERFGDDLLSAVVHLEGQGVWHRDIKPDNIGIRPRPSRTLHLVLFDFSLAG 659
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
93-179 6.25e-03

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 39.50  E-value: 6.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409    93 DRFNYV-VMQ-LQGRNLADLRRSqsrgtftisTTLRLGRQILESIESIHSVGFLHRDIKPSNFamgRFPStcRKCYMLDF 170
Cdd:TIGR03724   68 DPDNKTiVMEyIEGKPLKDVIEE---------NGDELAREIGRLVGKLHKAGIVHGDLTTSNI---IVRD--DKVYLIDF 133

                   ....*....
gi 530405409   171 GLARqFTNS 179
Cdd:TIGR03724  134 GLGK-YSDE 141
 
Name Accession Description Interval E-value
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
75-287 2.28e-152

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. Mutations in TTBK2 is associated with the development of spinocerebellar ataxia type 11, belonging to a group of neurodegenerative disorders characterized by progressive incoordination, dysarthria and impairment of eye movements. Brain tissues of SCA11 patients show the presence of neurofibrillary tangles and tau deposition in the brain, similar to Alzheimer's disease (AD) patients. The TTBK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271031 [Multi-domain]  Cd Length: 262  Bit Score: 457.98  E-value: 2.28e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   75 KMESGKDHVCRFIGCGRNDRFNYVVMQLQGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFA 154
Cdd:cd14129    50 KKLQGKDHVCRFIGCGRNDRFNYVVMQLQGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFA 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  155 MGRFPSTCRKCYMLDFGLARQFTNSCGDVRPPRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRK 234
Cdd:cd14129   130 MGRFPSTCRKCYMLDFGLARQFTNSCGDVRPPRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRK 209
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530405409  235 IKDKEQVGSIKERYDHRLMLKHLPPEFSIFLDHISSLDYFTKPDYQLLTSVFD 287
Cdd:cd14129   210 IKDKEQVGSIKERYEHRLMLKHLPPEFSVFLDHISGLDYFTKPDYQLLVSVFD 262
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
75-287 1.34e-134

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. Genetic variations in TTBK1 are linked to Alzheimer's disease (AD). Hyperphosphorylated tau is a major component of paired helical filaments that accumulate in the brain of AD patients. Studies in transgenic mice show that TTBK1 is involved in the phosphorylation-dependent pathogenic aggregation of tau. The TTBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271032 [Multi-domain]  Cd Length: 262  Bit Score: 411.34  E-value: 1.34e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   75 KMESGKDHVCRFIGCGRNDRFNYVVMQLQGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFA 154
Cdd:cd14130    50 KKLQGKDHVCRFIGCGRNEKFNYVVMQLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFA 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  155 MGRFPSTCRKCYMLDFGLARQFTNSCGDVRPPRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRK 234
Cdd:cd14130   130 MGRLPSTYRKCYMLDFGLARQYTNTTGEVRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRK 209
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530405409  235 IKDKEQVGSIKERYDHRLMLKHLPPEFSIFLDHISSLDYFTKPDYQLLTSVFD 287
Cdd:cd14130   210 IKDKEQVGMIKEKYEHRMLLKHMPSEFHLFLDHIASLDYFTKPDYQLIMSVFE 262
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
75-287 1.30e-133

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


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 408.57  E-value: 1.30e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   75 KME-------SGKDHVCRFIGCGRNDRFNYVVMQLQGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRD 147
Cdd:cd14017    43 KMEvavlkklQGKPHFCRLIGCGRTERYNYIVMTLLGPNLAELRRSQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRD 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  148 IKPSNFAMGRFPSTCRKCYMLDFGLARQFTNSCGDV-RPPRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFV 226
Cdd:cd14017   123 VKPSNFAIGRGPSDERTVYILDFGLARQYTNKDGEVeRPPRNAAGFRGTVRYASVNAHRNKEQGRRDDLWSWFYMLIEFV 202
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530405409  227 VGQLPWRKIKDKEQVGSIKERYDHRLMLKHLPPEFSIFLDHISSLDYFTKPDYQLLTSVFD 287
Cdd:cd14017   203 TGQLPWRKLKDKEEVGKMKEKIDHEELLKGLPKEFFQILKHIRSLSYFDTPDYKKLHSLLE 263
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
79-286 4.33e-61

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


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 210.01  E-value: 4.33e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   79 GKDHVCRFIGCGRNDRFNYVVMQLQGRNLADLRRSQSRgTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRf 158
Cdd:cd14016    54 GGPGIPRLYWFGQEGDYNVMVMDLLGPSLEDLFNKCGR-KFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMGL- 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  159 PSTCRKCYMLDFGLARQFTNS-CGDVRPPRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKD 237
Cdd:cd14016   132 GKNSNKVYLIDFGLAKKYRDPrTGKHIPYREGKSLTGTARYASINAHLGIEQSRRDDLESLGYVLIYFLKGSLPWQGLKA 211
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530405409  238 K------EQVGSIKERYDHRLMLKHLPPEFSIFLDHISSLDYFTKPDYQLLTSVF 286
Cdd:cd14016   212 QskkekyEKIGEKKMNTSPEELCKGLPKEFAKYLEYVRSLKFEEEPDYDYLRQLF 266
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
89-288 7.83e-38

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. The delta and epsilon isoforms of CK1 play important roles in circadian rhythm and cell growth. They phosphorylate PERIOD proteins (PER1-3), which are circadian clock proteins that fulfill negative regulatory functions. PER phosphorylation leads to its degradation. However, CRY proteins form a complex with PER and CK1delta/epsilon that protects PER from degradation and leads to nuclear accummulation of the complex, which inhibits BMAL1-CLOCK dependent transcription activation. CK1delta/epsilon also phosphorylate the tumor suppressor p53 and the cellular oncogene Mdm2, which are key regulators of cell growth, genome integrity, and the development of cancer. This subfamily also includes the CK1 fungal proteins Saccharomyces cerevisiae HRR25 and Schizosaccharomyces pombe HHP1. These fungal proteins are involved in DNA repair. The CK1 delta/epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271027 [Multi-domain]  Cd Length: 275  Bit Score: 143.28  E-value: 7.83e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   89 CGRNDRFNYVVMQLQGRNLADLRRSQSRgTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGrfpsTCRK---C 165
Cdd:cd14125    64 YGVEGDYNVMVMDLLGPSLEDLFNFCSR-KFSLKTVLMLADQMISRIEYVHSKNFIHRDIKPDNFLMG----LGKKgnlV 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  166 YMLDFGLARQFTNSCGDVRPP-RAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKdkeqVGSI 244
Cdd:cd14125   139 YIIDFGLAKKYRDPRTHQHIPyRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNRGSLPWQGLK----AATK 214
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530405409  245 KERYDH----------RLMLKHLPPEFSIFLDHISSLDYFTKPDYQLLTSVFDN 288
Cdd:cd14125   215 KQKYEKisekkmstpiEVLCKGFPSEFATYLNYCRSLRFDDKPDYSYLRRLFRD 268
STKc_CK1_alpha cd14128
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze ...
85-286 1.26e-36

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. CK1alpha plays a role in cell cycle progression, spindle dynamics, and chromosome segregation. It is also involved in regulating apoptosis mediated by Fas or the retinoid X receptor (RXR), and is a positive regulator of Wnt signaling. CK1alpha phosphorylates the NS5A protein of flaviviruses such as the Hepatitis C virus (HCV) and yellow fever virus (YFV), and influences flaviviral replication. The CK1 alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271030 [Multi-domain]  Cd Length: 266  Bit Score: 139.56  E-value: 1.26e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   85 RFIGCGRNdrFNYVVMQLQGRNLADLRRSQSRgTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGrFPSTCRK 164
Cdd:cd14128    62 RWYGQEKD--YNVLVMDLLGPSLEDLFNFCSR-RFTMKTVLMLADQMIGRIEYVHNKNFIHRDIKPDNFLMG-IGRHCNK 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  165 CYMLDFGLARQFTNS-CGDVRPPRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKDK----- 238
Cdd:cd14128   138 LFLIDFGLAKKYRDSrTRQHIPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRGSLPWQGLKAAtkkqk 217
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 530405409  239 -EQVGSIKERYDHRLMLKHLPPEFSIFLDHISSLDYFTKPDYQLLTSVF 286
Cdd:cd14128   218 yEKISEKKMSTPVEVLCKGFPAEFAMYLNYCRGLRFEEAPDYMYLRQLF 266
STKc_CK1_gamma cd14126
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; STKs catalyze ...
86-303 1.27e-35

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. CK1gamma proteins are unique within the CK1 subfamily in that they are palmitoylated at the C-termini and are anchored to the plasma membrane. CK1gamma is involved in transducing the signaling of LDL-receptor-related protein 6 (LRP6) through direct phosphorylation following Wnt stimulation, resulting in the recruitment of the scaffold protein Axin. In Xenopus embryos, CK1gamma is required during anterio-posterior patterning. In higher vertebrates, three CK1gamma (gamma1-3) isoforms exist. In mammalian cells, CK1gamma2 has been implicated in regulating the synthesis of sphingomyelin, a phospholipid that is found in the outer leaflet of the plasma membrane, by hyperphosphorylating and inactivating the ceramide transfer protein CERT. CK1gamma2 also phosphorylates the transcription factor Smad-3 resulting in its ubiquitination and degradation. It inhibits Smad-3 mediated responses of Transforming Growth Factor-beta (TGF-beta) including cell growth arrest. The CK1 gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271028 [Multi-domain]  Cd Length: 288  Bit Score: 137.56  E-value: 1.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   86 FIGCGRndrFNYVVMQLQGRNLADLRRSQSRgTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfPSTCRK- 164
Cdd:cd14126    64 FGPCGK---YNAMVLELLGPSLEDLFDLCDR-TFSLKTVLMIAIQLISRIEYVHSKHLIYRDVKPENFLIGR-QSTKKQh 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  165 -CYMLDFGLARQFTNS-CGDVRPPRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKdkeqVG 242
Cdd:cd14126   139 vIHIIDFGLAKEYIDPeTNKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLK----AD 214
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530405409  243 SIKERYDH----------RLMLKHLPPEFSIFLDHISSLDYFTKPDYQLLTSVFDNSIKTFGVIESDPFDW 303
Cdd:cd14126   215 TLKERYQKigdtkratpiEVLCENFPEEMATYLRYVRRLDFFETPDYDYLRKLFTDLFDRKGYTDDYEFDW 285
STKc_CK1_fungal cd14127
Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 1; ...
90-294 7.60e-35

Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. This subfamily is composed of fungal CK1 homolog 1 proteins, also called Yck1 in Saccharomyces cerevisiae and Cki1 in Schizosaccharomyces pombe. Yck1 (or Yck1p) and Cki1 are plasma membrane-anchored proteins. Yck1 phosphorylates and regulates Khd1p, a RNA-binding protein that represses translation of bud-localized mRNA. Cki1 phosphorylates and regulates phosphatidylinositol (PI)-(4)P-5-kinase, which catalyzes the last step in the sythesis of PI(4,5)P2, which is involved in actin cytoskeleton remodeling and membrane traffic. The fungal CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271029 [Multi-domain]  Cd Length: 277  Bit Score: 134.93  E-value: 7.60e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   90 GRNDRFNYVVMQLQGRNLADLRRSQSRgTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfPST--CRKCYM 167
Cdd:cd14127    65 GQEGLHNILVIDLLGPSLEDLFDLCGR-KFSVKTVVMVAKQMLTRVQTIHEKNLIYRDIKPDNFLIGR-PGTknANVIHV 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  168 LDFGLARQFTNSCGDVRPP-RAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKDK------EQ 240
Cdd:cd14127   143 VDFGMAKQYRDPKTKQHIPyREKKSLSGTARYMSINTHLGREQSRRDDLEALGHVFMYFLRGSLPWQGLKAAtnkqkyEK 222
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530405409  241 VGSIKERYDHRLMLKHLPPEFSIFLDHISSLDYFTKPDYQLLTSVFDNSIKTFG 294
Cdd:cd14127   223 IGEKKQSTPIRDLCEGFPEEFAQYLEYVRNLGFDETPDYDYLRGLFSKALKDLG 276
STKc_VRK cd14015
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs ...
85-286 6.81e-29

Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins (VRK1, VRK2, and VRK3) while invertebrates, specifically fruit flies and nematodes, seem to carry only a single ortholog. Mutations of VRK in Drosophila and Caenorhabditis elegans showed varying phenotypes ranging from embryonic lethality to mitotic and meiotic defects resulting in sterility. In vertebrates, VRK1 is implicated in cell cycle progression and proliferation, nuclear envelope assembly, and chromatin condensation. VRK2 is involved in modulating JNK signaling. VRK3 is an inactive pseudokinase that inhibits ERK signaling. The VRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270917 [Multi-domain]  Cd Length: 300  Bit Score: 118.15  E-value: 6.81e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   85 RFIGCG----RNDRFNYVVMQLQGRNLADLRRsQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGrFPS 160
Cdd:cd14015    87 RYIGSGsheyKGEKYRFLVMPRFGRDLQKIFE-KNGKRFPEKTVLQLALRILDVLEYIHENGYVHADIKASNLLLG-FGK 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  161 TCRKCYMLDFGLARQFTNSCGDVR----PPRAvagFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWR-KI 235
Cdd:cd14015   165 NKDQVYLVDYGLASRYCPNGKHKEykedPRKA---HNGTIEFTSRDAHKGVAPSRRGDLEILGYNMLQWLCGKLPWEdNL 241
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 530405409  236 KDKEQVGSIKERY--DHRLMLKHL------PPEFSIFLDHISSLDYFTKPDYQLLTSVF 286
Cdd:cd14015   242 KNPEYVQKQKEKYmdDIPLLLKKCfpgkdvPEELQKYLKYVASLEYEEKPDYEKLRKIL 300
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
82-225 7.70e-27

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: 109.67  E-value: 7.70e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   82 HVCRFIGCGRNDRFNYVVMQL-QGRNLADLRRSQsRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfps 160
Cdd:cd00180    52 NIVKLYDVFETENFLYLVMEYcEGGSLKDLLKEN-KGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDS--- 127
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530405409  161 tCRKCYMLDFGLARQFTNSCGDVRPpravAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEF 225
Cdd:cd00180   128 -DGTVKLADFGLAKDLDSDDSLLKT----TGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL 187
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
82-233 1.02e-20

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 97.01  E-value: 1.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   82 HVCRFIGCGRNDRFNYVVMQL-QGRNLADLRRSqsRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFps 160
Cdd:COG0515    68 NIVRVYDVGEEDGRPYLVMEYvEGESLADLLRR--RGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPD-- 143
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530405409  161 tcRKCYMLDFGLARQFTNScgDVRPPRAVAgfrGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWR 233
Cdd:COG0515   144 --GRVKLIDFGIARALGGA--TLTQTGTVV---GTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFD 209
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
82-233 5.40e-18

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: 85.33  E-value: 5.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   82 HVCRFIGCGRNDRFNYVVMQL-QGRNLAD-LRRsqsRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFP 159
Cdd:cd14014    61 NIVRVYDVGEDDGRPYIVMEYvEGGSLADlLRE---RGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDG 137
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530405409  160 stcrKCYMLDFGLARQFtnscgDVRPPRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWR 233
Cdd:cd14014   138 ----RVKLTDFGIARAL-----GDSGLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFD 202
STKc_VRK1 cd14122
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 1; STKs ...
83-286 5.67e-18

Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. Vertebrates contain three VRK proteins. Human VRK1 is implicated in the regulation of many cellular processes including cell cycle progression and proliferation, stress responses, nuclear envelope assembly and chromatin condensation. It regulates cell cycle progression during the DNA replication period by inducing cyclin D1 expression. VRK1 also phosphorylates and regulates some transcription factors including p53, c-Jun, ATF2, and nuclear factor BAF. VRK1 stabilizes p53 by interfering with its mdm2-mediated degradation. Accumulation of p53, which blocks cell growth and division, is modulated by an autoregulatory loop between p53 and VRK1 (accumulated p53 downregulates VRK1). This autoregulatory loop has been found to be nonfunctional in some lung carcinomas. The VRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271024 [Multi-domain]  Cd Length: 301  Bit Score: 86.09  E-value: 5.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   83 VCRFIGCGRND----RFNYVVMQLQGRNLADLRRSQSRgTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRf 158
Cdd:cd14122    85 VPKYWGSGLHEkngkSYRFMIMDRFGSDLQKIYEANAK-RFSRKTVLQLGLRILDILEYIHEHEYVHGDIKASNLLLSY- 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  159 pSTCRKCYMLDFGLARQFtnsCGDVRPPRAVAGFR----GTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWR- 233
Cdd:cd14122   163 -KNPDQVYLVDYGLAYRY---CPEGVHKEYKEDPKrchdGTIEFTSIDAHKGVAPSRRGDLEILGYCMIQWLCGHLPWEd 238
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530405409  234 KIKDKEQVGSIKERY--------DHRLMLKHLPPEFSIFLDHISSLDYFTKPDYQLLTSVF 286
Cdd:cd14122   239 NLKDPNYVRDSKIRYrdniselmEKCFPGKNKPGEIRKYMETVKLLGYTEKPLYPHLREIL 299
STKc_VRK2 cd14123
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 2; STKs ...
94-285 7.14e-18

Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins. VRK2 exists as two alternative splice forms, A and B, which differ in their C-terminal regions. VRK2A, the predominant isoform, contains a hydrophobic tail and is anchored to the ER and mitochondria. It is expressed in all cell types. VRK2B lacks a membrane-anchor tail and is detected in the cytosol and the nucleus. Like VRK1, it can stabilize p53. VRK2B functionally replaces VRK1 in the nucleus of cell types where VRK1 is absent. VRK2 modulates hypoxia-induced stress responses by interacting with TAK1, an atypical MAPK kinase kinase which triggers cascades that activate JNK following oxidative stress. VRK2 also interacts with JIP1, a scaffold protein that assembles three consecutive members of a MAPK pathway. This interaction prevents the association of JNK with the signaling complex, leading to reduced phosphorylation and AP1-dependent transcription. The VRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271025 [Multi-domain]  Cd Length: 302  Bit Score: 85.67  E-value: 7.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   94 RFNYVVMQLQGRNLADLRrSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfpSTCRKCYMLDFGLA 173
Cdd:cd14123   102 SYRFMVMDRLGTDLQKIL-IDNGGQFKKTTVLQLGIRMLDVLEYIHENEYVHGDIKAANLLLGY--RNPNEVYLADYGLS 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  174 RQFT---NSCGDVRPPRAvaGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPW-RKIKDKEQVGSIKERYD 249
Cdd:cd14123   179 YRYCpngNHKEYKENPRK--GHNGTIEFTSLDAHKGVAPSRRGDLEILGYCMLHWLCGKLPWeQNLKNPVAVQEAKAKLL 256
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 530405409  250 HRL---MLKHLPP-----EFSIFLDHISSLDYFTKPDYQLLTSV 285
Cdd:cd14123   257 SNLpdsVLKWSTGgsssmEIAQFLSRVKDLAYDEKPDYQALKKI 300
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
81-270 9.80e-18

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 84.50  E-value: 9.80e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409     81 DHVCRFIGCGRNDRFNYVVMQL-QGRNLADLRRSqsRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMgrfp 159
Cdd:smart00220   57 PNIVRLYDVFEDEDKLYLVMEYcEGGDLFDLLKK--RGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILL---- 130
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409    160 STCRKCYMLDFGLARQFTnscgdvrPPRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRkikDKE 239
Cdd:smart00220  131 DEDGHVKLADFGLARQLD-------PGEKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFP---GDD 200
                           170       180       190
                    ....*....|....*....|....*....|.
gi 530405409    240 QVGSIKERydhrlmLKHLPPEFSIFLDHISS 270
Cdd:smart00220  201 QLLELFKK------IGKPKPPFPPPEWDISP 225
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
131-287 7.02e-15

putative serine/threonine kinase; Provisional


Pssm-ID: 165211 [Multi-domain]  Cd Length: 294  Bit Score: 76.91  E-value: 7.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  131 ILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLDFGLARQFTNSCGDVRPPRAVAGF-RGTVRYASINAHRNREM 209
Cdd:PHA02882  135 MLTTLEYIHEHGISHGDIKPENIMV----DGNNRGYIIDYGIASHFIIHGKHIEYSKEQKDLhRGTLYYAGLDAHNGACV 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  210 GRHDDLWSLFYMLVEFVVGQLPWRKIKDKEQV------GSIKERYDHRLMLKHLPPEFSIFLDHISSLDYFTKPDYQLLT 283
Cdd:PHA02882  211 TRRGDLESLGYCMLKWAGIKLPWKGFGHNGNLihaakcDFIKRLHEGKIKIKNANKFIYDFIECVTKLSYEEKPDYDALI 290

                  ....
gi 530405409  284 SVFD 287
Cdd:PHA02882  291 KIFD 294
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
82-267 4.66e-13

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: 70.63  E-value: 4.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   82 HVCRFIGCGRNDRFNYVVM-QLQGRNLADLRRSqsRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSN---FAMGR 157
Cdd:cd06606    60 NIVRYLGTERTENTLNIFLeYVPGGSLASLLKK--FGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANilvDSDGV 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  158 fpstcrkCYMLDFGLARQFtnscGDVRPPRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKD 237
Cdd:cd06606   138 -------VKLADFGCAKRL----AEIATGEGTKSLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSELGN 206
                         170       180       190
                  ....*....|....*....|....*....|....
gi 530405409  238 KEQV----GSIKErydHRLMLKHLPPEFSIFLDH 267
Cdd:cd06606   207 PVAAlfkiGSSGE---PPPIPEHLSEEAKDFLRK 237
PK_VRK3 cd14124
Pseudokinase domain of Vaccinia Related Kinase 3; The pseudokinase domain shows similarity to ...
79-282 8.30e-12

Pseudokinase domain of Vaccinia Related Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins. VRK3 is an inactive pseudokinase that is unable to bind ATP. It achieves its regulatory function through protein-protein interactions. It negatively regulates ERK signaling by binding directly and enhancing the activity of the MAPK phosphatase VHR (vaccinia H1-related), which dephosphorylates and inactivates ERK. The VRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271026 [Multi-domain]  Cd Length: 298  Bit Score: 67.56  E-value: 8.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   79 GKDHVCRFIG---C---GRNDRFNYVVMQLQGRNLADLRrSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSN 152
Cdd:cd14124    74 KKLHSTDLLGipsCvgfGVHDSYRFLVFPSLGQSLQSAL-DEGKGVLSEKAVLQLACRLLDALEFIHENEYVHGDITAEN 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  153 FAMGrfPSTCRKCYMLDFGLARQFtnsCGDVRPPRAVAGFR----GTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVG 228
Cdd:cd14124   153 IFVD--PEDQSEVYLAGYGFAFRY---CPGGKHVEYREGSRspheGDIEFISLDSHKGAGPSRRSDLQSLGYCMLKWLTG 227
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530405409  229 QLPWRKIK-DKEQVGSIKERY--------DHRLMLKHLPPEFSIFLDHISSLDYFTKPDYQLL 282
Cdd:cd14124   228 SLPWSNLLhNTEDIMKQKERFmddvpgflGPCFHQKKVSEALQKYLKVVMALQYEEKPDYAML 290
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
83-262 1.98e-11

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: 65.64  E-value: 1.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   83 VCRFIGCGRNDRFNYVVMQL-QGRNLADLRRSQSRgTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFPsT 161
Cdd:cd13999    52 IVQFIGACLSPPPLCIVTEYmPGGSLYDLLHKKKI-PLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENF-T 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  162 CRKCymlDFGLARqFTNSCGDVRppravAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKDKEQV 241
Cdd:cd13999   130 VKIA---DFGLSR-IKNSTTEKM-----TGVVGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIA 200
                         170       180
                  ....*....|....*....|.
gi 530405409  242 GSIKERYDHRLMLKHLPPEFS 262
Cdd:cd13999   201 AAVVQKGLRPPIPPDCPPELS 221
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
82-225 5.69e-11

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 64.62  E-value: 5.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   82 HVCRFIGCGRNDRFNYVVMQL-QGRNLAD-LRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSN-FamgrF 158
Cdd:cd13996    65 NIVRYYTAWVEEPPLYIQMELcEGGTLRDwIDRRNSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNiF----L 140
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530405409  159 PSTCRKCYMLDFGLARQFTNSCGDVRPPRAVAGFR--------GTVRYASINAHRNREMGRHDDLWS----LFYMLVEF 225
Cdd:cd13996   141 DNDDLQVKIGDFGLATSIGNQKRELNNLNNNNNGNtsnnsvgiGTPLYASPEQLDGENYNEKADIYSlgiiLFEMLHPF 219
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
120-232 1.34e-09

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 60.39  E-value: 1.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  120 TISTTLRLGR------------QILESIESIHSVGFLHRDIKPSNFAMGRfpSTCRKcyMLDFGLARQFTNScGDVRPPR 187
Cdd:cd06626    85 TLEELLRHGRildeavirvytlQLLEGLAYLHENGIVHRDIKPANIFLDS--NGLIK--LGDFGSAVKLKNN-TTTMAPG 159
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 530405409  188 AVAGFRGTVRYAS---INAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 232
Cdd:cd06626   160 EVNSLVGTPAYMApevITGNKGEGHGRAADIWSLGCVVLEMATGKRPW 207
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
97-186 3.68e-09

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 59.47  E-value: 3.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQLQGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFamgrfpsTCRKCYML---DFGLA 173
Cdd:cd07830    74 YFVFEYMEGNLYQLMKDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENL-------LVSGPEVVkiaDFGLA 146
                          90
                  ....*....|...
gi 530405409  174 RQFTNscgdvRPP 186
Cdd:cd07830   147 REIRS-----RPP 154
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
97-232 4.60e-09

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 58.72  E-value: 4.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQL-QGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLDFGLARQ 175
Cdd:cd14008    82 YLVLEYcEGGPVMELDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLL----TADGTVKISDFGVSEM 157
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530405409  176 FTNSCGDVR---------PPRAVAGFRGTVRyasinahrnremGRHDDLWSL---FYMlveFVVGQLPW 232
Cdd:cd14008   158 FEDGNDTLQktagtpaflAPELCDGDSKTYS------------GKAADIWALgvtLYC---LVFGRLPF 211
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
81-240 4.84e-09

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 58.50  E-value: 4.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   81 DHVCRFIGCGRNDRFNYVVMQL-QGRNLAD-------LRRSQSRGTFTisttlrlgrQILESIESIHSVGFLHRDIKPSN 152
Cdd:cd14069    60 KNVVRFYGHRREGEFQYLFLEYaSGGELFDkiepdvgMPEDVAQFYFQ---------QLMAGLKYLHSCGITHRDIKPEN 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  153 famgrfpstcrkcyML----------DFGLARQFTNSCGDvrppRAVAGFRGTVRYASINAHRNREM-GRHDDLWSLFYM 221
Cdd:cd14069   131 --------------LLldendnlkisDFGLATVFRYKGKE----RLLNKMCGTLPYVAPELLAKKKYrAEPVDVWSCGIV 192
                         170
                  ....*....|....*....
gi 530405409  222 LVEFVVGQLPWRKIKDKEQ 240
Cdd:cd14069   193 LFAMLAGELPWDQPSDSCQ 211
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
97-181 1.03e-08

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: 57.49  E-value: 1.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQL-QGRNLADlrRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFaMGRFPSTCRKCYMLDFGLARQ 175
Cdd:cd05117    75 YLVMELcTGGELFD--RIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENI-LLASKDPDSPIKIIDFGLAKI 151
                          90
                  ....*....|..
gi 530405409  176 FTNS------CG 181
Cdd:cd05117   152 FEEGeklktvCG 163
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
97-244 1.06e-08

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


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 57.63  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQLQGRNLADLRRSQSRGtFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFPSTCRKCymlDFGLARQF 176
Cdd:cd05118    77 CLVFELMGMNLYELIKDYPRG-LPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELGQLKLA---DFGLARSF 152
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530405409  177 TNSCGDV----RPPRAVAGFRGTVRYasinahrnremGRHDDLWSLFYMLVEFVVGQLPWRKIKDKEQVGSI 244
Cdd:cd05118   153 TSPPYTPyvatRWYRAPEVLLGAKPY-----------GSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKI 213
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
125-224 1.14e-08

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 57.50  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  125 LRLGRQILESIESIHSVGFLHRDIKPSNFamgrFPSTCRKCYMLDFGLARQFTNscgdvrpPRAVAGFRGTVRYASINAH 204
Cdd:cd14047   120 LEIFEQITKGVEYIHSKKLIHRDLKPSNI----FLVDTGKVKIGDFGLVTSLKN-------DGKRTKSKGTLSYMSPEQI 188
                          90       100
                  ....*....|....*....|
gi 530405409  205 RNREMGRHDDLWSLFYMLVE 224
Cdd:cd14047   189 SSQDYGKEVDIYALGLILFE 208
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
85-235 1.27e-08

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: 57.21  E-value: 1.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   85 RFIGCGRNDRFNYVVM-QLQGRNLADLRRSQSRgTFT---ISTTLRlgrQILESIESIHSVGFLHRDIKPSNFAMgrfpS 160
Cdd:cd05122    61 KYYGSYLKKDELWIVMeFCSGGSLKDLLKNTNK-TLTeqqIAYVCK---EVLKGLEYLHSHGIIHRDIKAANILL----T 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  161 TCRKCYMLDFGLARQFTNSCGDVRppravagFRGTVRYAS---INAhrnremGRHD---DLWSLFYMLVEFVVGQLPWRK 234
Cdd:cd05122   133 SDGEVKLIDFGLSAQLSDGKTRNT-------FVGTPYWMApevIQG------KPYGfkaDIWSLGITAIEMAEGKPPYSE 199

                  .
gi 530405409  235 I 235
Cdd:cd05122   200 L 200
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
97-175 1.57e-08

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 58.07  E-value: 1.57e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530405409   97 YVVMQLQGRNLADLRRSQSrgtFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGrfpSTCrKCYMLDFGLARQ 175
Cdd:cd07851    96 YLVTHLMGADLNNIVKCQK---LSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVN---EDC-ELKILDFGLARH 167
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
41-232 4.42e-08

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


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 55.90  E-value: 4.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   41 GTGCLCSCSTISVYCNEWGRRAAGYPECWNpsERKMESGKDH--VCRFIGCGRND-RFNYVVMQLQGRNLADLRrsQSRG 117
Cdd:cd06630    23 KTGTLMAVKQVSFCRNSSSEQEEVVEAIRE--EIRMMARLNHpnIVRMLGATQHKsHFNIFVEWMAGGSVASLL--SKYG 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  118 TFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGrfpSTCRKCYMLDFGLARQFTNSCgdvrpprAVAG-----F 192
Cdd:cd06630    99 AFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVD---STGQRLRIADFGAAARLASKG-------TGAGefqgqL 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 530405409  193 RGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 232
Cdd:cd06630   169 LGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPW 208
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
130-233 4.78e-08

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 56.07  E-value: 4.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  130 QILESIESIHSVGFLHRDIKPSNFAMGRFPSTCrkcyMLDFGLARQFTN------------SCGDVRPPRAvAGFRGTVR 197
Cdd:cd05581   109 EIVLALEYLHSKGIIHRDLKPENILLDEDMHIK----ITDFGTAKVLGPdsspestkgdadSQIAYNQARA-ASFVGTAE 183
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 530405409  198 YASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWR 233
Cdd:cd05581   184 YVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFR 219
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
93-175 4.88e-08

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 56.50  E-value: 4.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   93 DRFN--YVVMQLQGRNLADLRRSQSRGTFTISTtlrLGRQILESIESIHSVGFLHRDIKPSNFAMGRfpsTCrKCYMLDF 170
Cdd:cd07880    90 DRFHdfYLVMPFMGTDLGKLMKHEKLSEDRIQF---LVYQMLKGLKYIHAAGIIHRDLKPGNLAVNE---DC-ELKILDF 162

                  ....*
gi 530405409  171 GLARQ 175
Cdd:cd07880   163 GLARQ 167
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
128-193 6.66e-08

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


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 54.92  E-value: 6.66e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530405409  128 GRQILESIESIHSVGFLHRDIKPSNFAmgrFPSTCRKCYMLDFGLArQFTNSCGDVRPPRA-VAGFR 193
Cdd:cd14019   107 LRNLFKALKHVHSFGIIHRDVKPGNFL---YNRETGKGVLVDFGLA-QREEDRPEQRAPRAgTRGFR 169
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
90-179 8.26e-08

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 56.34  E-value: 8.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   90 GRNDRFNYVVMQL-QGRNLADLRRSqsRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFamgrfpstcrkcyML 168
Cdd:NF033483   76 GEDGGIPYIVMEYvDGRTLKDYIRE--HGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNI-------------LI 140
                          90       100
                  ....*....|....*....|
gi 530405409  169 ---------DFGLARQFTNS 179
Cdd:NF033483  141 tkdgrvkvtDFGIARALSST 160
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
129-234 9.81e-08

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 54.63  E-value: 9.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  129 RQILESIESIHSVGFLHRDIKPSNFAmgrFPSTcrKCYMLDFGLARQFTNscgDVRPPRavaGFRGTVRYASINAHRNRE 208
Cdd:cd13995   103 KHVLKGLDFLHSKNIIHHDIKPSNIV---FMST--KAVLVDFGLSVQMTE---DVYVPK---DLRGTEIYMSPEVILCRG 171
                          90       100
                  ....*....|....*....|....*.
gi 530405409  209 MGRHDDLWSLFYMLVEFVVGQLPWRK 234
Cdd:cd13995   172 HNTKADIYSLGATIIHMQTGSPPWVR 197
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
81-232 1.08e-07

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 54.65  E-value: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   81 DHVCRFIGCGRN---DRFNYVVMQLQGRNLADlrRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFamgr 157
Cdd:cd06653    64 DRIVQYYGCLRDpeeKKLSIFVEYMPGGSVKD--QLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANI---- 137
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530405409  158 FPSTCRKCYMLDFGLARQFTNSCgdvRPPRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 232
Cdd:cd06653   138 LRDSAGNVKLGDFGASKRIQTIC---MSGTGIKSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPW 209
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
93-229 1.27e-07

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


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 55.05  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   93 DRFN--YVVMQLQGRNLADLRRSQSrgtFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfpsTCrKCYMLDF 170
Cdd:cd07877    92 EEFNdvYLVTHLMGADLNNIVKCQK---LTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNE---DC-ELKILDF 164
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530405409  171 GLARQFTNScgdvrppraVAGFRGTVRYAS----IN-AHRNREMgrhdDLWSLFYMLVEFVVGQ 229
Cdd:cd07877   165 GLARHTDDE---------MTGYVATRWYRApeimLNwMHYNQTV----DIWSVGCIMAELLTGR 215
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
129-264 1.42e-07

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


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 54.24  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  129 RQILESIESIHSVGFLHRDIKPSNFAMGRfpstCRKCYMLDFGLARQFTNsCGDVRPPRAvAGFRGTVRYASINAHRNRE 208
Cdd:cd13994   105 KQILRGVAYLHSHGIAHRDLKPENILLDE----DGVLKLTDFGTAEVFGM-PAEKESPMS-AGLCGSEPYMAPEVFTSGS 178
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530405409  209 M-GRHDDLWSLFYMLVEFVVGQLPWRKIKDKEQVGSIKERYDHRLMLKHLPPEFSIF 264
Cdd:cd13994   179 YdGRAVDVWSCGIVLFALFTGRFPWRSAKKSDSAYKAYEKSGDFTNGPYEPIENLLP 235
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
97-186 1.53e-07

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 54.26  E-value: 1.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQLQGRNLADLRRSQSRgTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGrfPSTCRKcyMLDFGLARQF 176
Cdd:cd07832    76 VLVFEYMLSSLSEVLRDEER-PLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLIS--STGVLK--IADFGLARLF 150
                          90
                  ....*....|
gi 530405409  177 TNscGDVRPP 186
Cdd:cd07832   151 SE--EDPRLY 158
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
97-233 1.66e-07

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


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 54.66  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQL-QGRNLadLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfPSTCRKCYMLDFGLARq 175
Cdd:cd14179    78 FLVMELlKGGEL--LERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTD-ESDNSEIKIIDFGFAR- 153
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  176 ftnscgdVRPP--RAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWR 233
Cdd:cd14179   154 -------LKPPdnQPLKTPCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQ 206
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
130-234 1.88e-07

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 53.89  E-value: 1.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  130 QILESIESIHSVGFLHRDIKPSNFAMGRFPSTCRKCymlDFGLARQFTNSCgDVRppravagfRGTVRYAS----INAHR 205
Cdd:cd13993   115 QLIDAVKHCHSLGIYHRDIKPENILLSQDEGTVKLC---DFGLATTEKISM-DFG--------VGSEFYMApecfDEVGR 182
                          90       100       110
                  ....*....|....*....|....*....|.
gi 530405409  206 NREM--GRHDDLWSLFYMLVEFVVGQLPWRK 234
Cdd:cd13993   183 SLKGypCAAGDIWSLGIILLNLTFGRNPWKI 213
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
93-229 1.96e-07

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 54.67  E-value: 1.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   93 DRFN--YVVMQLQGRNLADLRRSQSrgtFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfpsTCrKCYMLDF 170
Cdd:cd07878    90 ENFNevYLVTNLMGADLNNIVKCQK---LSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNE---DC-ELRILDF 162
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530405409  171 GLARQFTNScgdvrppraVAGFRGTVRYAS----IN-AHRNREMgrhdDLWSLFYMLVEFVVGQ 229
Cdd:cd07878   163 GLARQADDE---------MTGYVATRWYRApeimLNwMHYNQTV----DIWSVGCIMAELLKGK 213
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
81-232 2.23e-07

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


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 53.89  E-value: 2.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   81 DHVCRFIGCGRN--DRFNYVVMQLQ-GRNLADlrRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFamgr 157
Cdd:cd06652    64 ERIVQYYGCLRDpqERTLSIFMEYMpGGSIKD--QLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANI---- 137
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530405409  158 FPSTCRKCYMLDFGLARQFTNSCGDVRPPRAVAgfrGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 232
Cdd:cd06652   138 LRDSVGNVKLGDFGASKRLQTICLSGTGMKSVT---GTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPW 209
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
144-232 2.67e-07

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 53.60  E-value: 2.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  144 LHRDIKPSNFAM---GRFpstcRKCymlDFGLARQFTNSCGDVrppravagFRGTVRYASINAHRNREMGRHDDLWSLFY 220
Cdd:cd06620   127 IHRDIKPSNILVnskGQI----KLC---DFGVSGELINSIADT--------FVGTSTYMSPERIQGGKYSVKSDVWSLGL 191
                          90
                  ....*....|..
gi 530405409  221 MLVEFVVGQLPW 232
Cdd:cd06620   192 SIIELALGEFPF 203
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
127-231 3.44e-07

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 54.06  E-value: 3.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  127 LGRQILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLDFGLAR---QFTNSCGDvrpprAVagfrGTVRYAS--- 200
Cdd:PLN00034  173 VARQILSGIAYLHRRHIVHRDIKPSNLLI----NSAKNVKIADFGVSRilaQTMDPCNS-----SV----GTIAYMSper 239
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 530405409  201 INAHRNRemGRHD----DLWSLFYMLVEFVVGQLP 231
Cdd:PLN00034  240 INTDLNH--GAYDgyagDIWSLGVSILEFYLGRFP 272
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
109-177 3.47e-07

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 53.25  E-value: 3.47e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530405409  109 DLRR--SQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfpSTCRKcyMLDFGLARQFT 177
Cdd:cd07829    83 DLKKylDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINR--DGVLK--LADFGLARAFG 149
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
83-232 3.88e-07

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 52.86  E-value: 3.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   83 VCRFIGCGRNDRFNYVVMQL-QGRNLADLrrSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMgrFPST 161
Cdd:cd14098    63 IVRLIDWYEDDQHIYLVMEYvEGGDLMDF--IMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILI--TQDD 138
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530405409  162 CRKCYMLDFGLAR-QFTNScgdvrpprAVAGFRGTVRYAS---INAHRNREMGRHD---DLWSLFYMLVEFVVGQLPW 232
Cdd:cd14098   139 PVIVKISDFGLAKvIHTGT--------FLVTFCGTMAYLApeiLMSKEQNLQGGYSnlvDMWSVGCLVYVMLTGALPF 208
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
93-247 4.07e-07

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 53.46  E-value: 4.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   93 DRFN-YVVMQ-LQGRNLadLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSN--FAMGRFPSTCRkcyML 168
Cdd:cd14092    70 DELHtYLVMElLRGGEL--LERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENllFTDEDDDAEIK---IV 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  169 DFGLARqftnscgdVRP---PRAVAGFrgTVRYAS--INAHRNREMGRHD--DLWSLFYMLVEFVVGQLPWRKIKDKEQV 241
Cdd:cd14092   145 DFGFAR--------LKPenqPLKTPCF--TLPYAApeVLKQALSTQGYDEscDLWSLGVILYTMLSGQVPFQSPSRNESA 214

                  ....*.
gi 530405409  242 GSIKER 247
Cdd:cd14092   215 AEIMKR 220
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
97-238 4.08e-07

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 53.34  E-value: 4.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQ-LQGRNLADLRRSQSRgtFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfPSTCRKCYMLDFGLARQ 175
Cdd:cd14180    77 YLVMElLRGGELLDRIKKKAR--FSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYAD-ESDGAVLKVIDFGFARL 153
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530405409  176 FTNSCGDVRPPRAvagfrgTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKDK 238
Cdd:cd14180   154 RPQGSRPLQTPCF------TLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGK 210
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
97-174 5.18e-07

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: 52.37  E-value: 5.18e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530405409   97 YVVMQL-QGRNLADlrRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFaMGRFPSTCRKCYMLDFGLAR 174
Cdd:cd14083    77 YLVMELvTGGELFD--RIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENL-LYYSPDEDSKIMISDFGLSK 152
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
97-181 5.46e-07

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


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 52.69  E-value: 5.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQL-QGRNLADlrRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFaMGRFPSTCRKCYMLDFGLARQ 175
Cdd:cd14166    76 YLVMQLvSGGELFD--RILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENL-LYLTPDENSKIMITDFGLSKM 152
                          90
                  ....*....|.
gi 530405409  176 FTN-----SCG 181
Cdd:cd14166   153 EQNgimstACG 163
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
114-271 6.58e-07

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 52.09  E-value: 6.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  114 QSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGrFPSTCRKCymlDFGLARQFTNScgdvrpPRAVagFR 193
Cdd:cd14007    92 KKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLG-SNGELKLA---DFGWSVHAPSN------RRKT--FC 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  194 GTVRYASinahrnREM---GRHD---DLWSLFYMLVEFVVGQLPWRKIKDKEQVGSIKE-RYDhrlMLKHLPPEFSiflD 266
Cdd:cd14007   160 GTLDYLP------PEMvegKEYDykvDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNvDIK---FPSSVSPEAK---D 227

                  ....*
gi 530405409  267 HISSL 271
Cdd:cd14007   228 LISKL 232
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
93-240 7.46e-07

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 52.67  E-value: 7.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   93 DRFNYVVMQ-LQGrnlADLRRSQSR-GTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMG-------------- 156
Cdd:cd05573    73 EDHLYLVMEyMPG---GDLMNLLIKyDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDadghikladfglct 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  157 RFPSTCRKCYMLDFGLARQFTNSCGDVRPPRAVAGFR-----GTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLP 231
Cdd:cd05573   150 KMNKSGDRESYLNDSVNTLFQDNVLARRRPHKQRRVRaysavGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPP 229
                         170
                  ....*....|....*...
gi 530405409  232 ---------WRKIKDKEQ 240
Cdd:cd05573   230 fysdslvetYSKIMNWKE 247
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
123-267 8.07e-07

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 51.94  E-value: 8.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  123 TTLRLGRQILESIESIHSVGFLHRDIKPSNFAMgrFPSTCRKCYMLDFGLARQftnscgdvrppravagfRG-TVRYAS- 200
Cdd:cd13987    92 RVKRCAAQLASALDFMHSKNLVHRDIKPENVLL--FDKDCRRVKLCDFGLTRR-----------------VGsTVKRVSg 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  201 -INAHRNR--EMGRHD--------DLWS----LFYMLvefvVGQLPWRKIKDKEQVGSIKERYDHRLMLKhLPPEFSIFL 265
Cdd:cd13987   153 tIPYTAPEvcEAKKNEgfvvdpsiDVWAfgvlLFCCL----TGNFPWEKADSDDQFYEEFVRWQKRKNTA-VPSQWRRFT 227

                  ..
gi 530405409  266 DH 267
Cdd:cd13987   228 PK 229
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
97-285 1.08e-06

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 51.74  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQLQGRNLADL-----RRSQSRGTFT-------ISTTLRLGRQILESIESIHSVGFLHRDIKPSN-FAMGrfpSTCr 163
Cdd:cd14049    83 YIQMQLCELSLWDWivernKRPCEEEFKSapytpvdVDVTTKILQQLLEGVTYIHSMGIVHRDLKPRNiFLHG---SDI- 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  164 KCYMLDFGLArqftnsCGDV-------------RPPRAVAGFrGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVgql 230
Cdd:cd14049   159 HVRIGDFGLA------CPDIlqdgndsttmsrlNGLTHTSGV-GTCLYAAPEQLEGSHYDFKSDMYSIGVILLELFQ--- 228
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530405409  231 PWRKIKDKEQV------GSIKERYDHRLmlkhlpPEFSIFLDHISSLDYFTKPD-YQLLTSV 285
Cdd:cd14049   229 PFGTEMERAEVltqlrnGQIPKSLCKRW------PVQAKYIKLLTSTEPSERPSaSQLLESE 284
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
81-232 1.11e-06

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


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 51.62  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   81 DHVCRFIGCGRN--DRFNYVVMQ-LQGRNLADlrRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFamgr 157
Cdd:cd06651    69 ERIVQYYGCLRDraEKTLTIFMEyMPGGSVKD--QLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANI---- 142
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530405409  158 FPSTCRKCYMLDFGLARQFTNSCGDVRPPRAVAgfrGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 232
Cdd:cd06651   143 LRDSAGNVKLGDFGASKRLQTICMSGTGIRSVT---GTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW 214
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
129-244 1.32e-06

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: 51.25  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  129 RQILESIESIHSVGFLHRDIKPSNF---AMGRFPstcrkcyMLDFGLARQFTNscgdvrpPRAVAGFRGTVRYAS--INA 203
Cdd:cd06632   109 RQILSGLAYLHSRNTVHRDIKGANIlvdTNGVVK-------LADFGMAKHVEA-------FSFAKSFKGSPYWMApeVIM 174
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 530405409  204 HRNREMGRHDDLWSLFYMLVEFVVGQLPWrkiKDKEQVGSI 244
Cdd:cd06632   175 QKNSGYGLAVDIWSLGCTVLEMATGKPPW---SQYEGVAAI 212
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
74-228 1.35e-06

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


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 51.11  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   74 RKMESGKDHVCRFIGC--GRNDRFnyVVMQLQGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPS 151
Cdd:cd14133    54 KKDKADKYHIVRLKDVfyFKNHLC--IVFELLSQNLYEFLKQNKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPE 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  152 NFAMGRfPSTCR-KcyMLDFGLARQFTNSCGDV------RPPRAVAGFRGTVRYasinahrnremgrhdDLWSLFYMLVE 224
Cdd:cd14133   132 NILLAS-YSRCQiK--IIDFGSSCFLTQRLYSYiqsryyRAPEVILGLPYDEKI---------------DMWSLGCILAE 193

                  ....
gi 530405409  225 FVVG 228
Cdd:cd14133   194 LYTG 197
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
130-271 1.35e-06

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


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 51.93  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  130 QILESIESIHSVGFLHRDIKPSNFAMGRfpstCRKCYMLDFGLARQFtNSCGDVRPPRAVagfrGTVRY------ASINA 203
Cdd:cd05601   110 ELVLAIHSLHSMGYVHRDIKPENILIDR----TGHIKLADFGSAAKL-SSDKTVTSKMPV----GTPDYiapevlTSMNG 180
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530405409  204 HRNREMGRHDDLWSLFYMLVEFVVGQLPWRKikdkeqvGSIKERYDHRLMLK---HLPPEFSI---FLDHISSL 271
Cdd:cd05601   181 GSKGTYGVECDWWSLGIVAYEMLYGKTPFTE-------DTVIKTYSNIMNFKkflKFPEDPKVsesAVDLIKGL 247
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
97-218 1.39e-06

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


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 51.43  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQL-QGRNLADlrRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfPSTCRKCYMLDFGLARq 175
Cdd:cd14169    77 YLAMELvTGGELFD--RIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAT-PFEDSKIMISDFGLSK- 152
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 530405409  176 ftnscgdVRPPRAVAGFRGTVRYASINAHRNREMGRHDDLWSL 218
Cdd:cd14169   153 -------IEAQGMLSTACGTPGYVAPELLEQKPYGKAVDVWAI 188
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
91-304 1.74e-06

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 51.93  E-value: 1.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   91 RNDRFNYVVMQ-LQGRNLADLRRS----QSRGTFTISttlrlgrQILESIESIHSVGFLHRDIKPSNFAMGRfpstCRKC 165
Cdd:cd05622   143 QDDRYLYMVMEyMPGGDLVNLMSNydvpEKWARFYTA-------EVVLALDAIHSMGFIHRDVKPDNMLLDK----SGHL 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  166 YMLDFGLARQFtNSCGDVRPPRAVagfrGTVRYASINAHRNR----EMGRHDDLWSLFYMLVEFVVGQLPWRKikdKEQV 241
Cdd:cd05622   212 KLADFGTCMKM-NKEGMVRCDTAV----GTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPFYA---DSLV 283
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530405409  242 GSIKERYDHRLMLKHlpPEFSIFLDHISSL--DYFTKPDYQLLTSVFDnSIKTFGVIESDPFDWE 304
Cdd:cd05622   284 GTYSKIMNHKNSLTF--PDDNDISKEAKNLicAFLTDREVRLGRNGVE-EIKRHLFFKNDQWAWE 345
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
78-237 1.85e-06

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 51.06  E-value: 1.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   78 SGKDHVCRFIG--CGRNDRFNYVVMQLQGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAM 155
Cdd:cd14131    57 KGSDRIIQLYDyeVTDEDDYLYMVMECGEIDLATILKKKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLL 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  156 --GRFpstcrKcyMLDFGLARQF----TNSCGDVRPpravagfrGTVRYAS------INAHRNRE----MGRHDDLWSLF 219
Cdd:cd14131   137 vkGRL-----K--LIDFGIAKAIqndtTSIVRDSQV--------GTLNYMSpeaikdTSASGEGKpkskIGRPSDVWSLG 201
                         170
                  ....*....|....*...
gi 530405409  220 YMLVEFVVGQLPWRKIKD 237
Cdd:cd14131   202 CILYQMVYGKTPFQHITN 219
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
91-155 1.86e-06

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 51.03  E-value: 1.86e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530405409   91 RNDRFNYVVMQL-QGRNLAD-LRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSN--FAM 155
Cdd:cd14048    85 MDEVYLYIQMQLcRKENLKDwMNRRCTMESRELFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNvfFSL 153
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
82-178 2.19e-06

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: 50.63  E-value: 2.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   82 HVCRFIGCGRNDRFNYVVMQL-QGRNLADLRRSqsRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfps 160
Cdd:cd14099    62 NIVKFHDCFEDEENVYILLELcSNGSLMELLKR--RKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDE--- 136
                          90       100
                  ....*....|....*....|..
gi 530405409  161 tcrkcYML----DFGLARQFTN 178
Cdd:cd14099   137 -----NMNvkigDFGLAARLEY 153
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
130-231 2.65e-06

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 50.29  E-value: 2.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  130 QILESIESIHSVGFLHRDIKPSNF---AMGRFPSTcrkcymlDFGLARQftnscGDVRppRAVAGFRGTVRYASINAHRN 206
Cdd:cd05579   101 EIVLALEYLHSHGIIHRDLKPDNIlidANGHLKLT-------DFGLSKV-----GLVR--RQIKLSIQKKSNGAPEKEDR 166
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 530405409  207 REMGRHD----------------DLWSLFYMLVEFVVGQLP 231
Cdd:cd05579   167 RIVGTPDylapeillgqghgktvDWWSLGVILYEFLVGIPP 207
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
130-178 2.74e-06

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


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 51.02  E-value: 2.74e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 530405409  130 QILESIESIHSVGFLHRDIKPSNFAMGrfpSTCRkCYMLDFGLARQFTN 178
Cdd:cd07852   115 QLLKALKYLHSGGVIHRDLKPSNILLN---SDCR-VKLADFGLARSLSQ 159
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
40-174 2.96e-06

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


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 50.35  E-value: 2.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   40 LGTGClcsCSTIsVYCNEW-GRRAAG---YPECWNPSERK---MESGKDH--VCRFIGCGRNDRFNYVVMQLQGRNLADL 110
Cdd:cd13982     9 LGYGS---EGTI-VFRGTFdGRPVAVkrlLPEFFDFADREvqlLRESDEHpnVIRYFCTEKDRQFLYIALELCAASLQDL 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530405409  111 RRSQSRGTFTISTTL---RLGRQILESIESIHSVGFLHRDIKPSNFAMGRFPSTCRKCYML-DFGLAR 174
Cdd:cd13982    85 VESPRESKLFLRPGLepvRLLRQIASGLAHLHSLNIVHRDLKPQNILISTPNAHGNVRAMIsDFGLCK 152
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
81-175 3.03e-06

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 50.22  E-value: 3.03e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409     81 DHVCRFIGCGRNDRFNYVVMQL-QGRNLADLRRsQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfP 159
Cdd:smart00219   61 PNVVKLLGVCTEEEPLYIVMEYmEGGDLLSYLR-KNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGE-N 138
                            90
                    ....*....|....*.
gi 530405409    160 STCRKCymlDFGLARQ 175
Cdd:smart00219  139 LVVKIS---DFGLSRD 151
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
130-174 3.05e-06

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


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 50.77  E-value: 3.05e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 530405409  130 QILESIESIHSVGFLHRDIKPSNFAMGrfpSTC--RKCymlDFGLAR 174
Cdd:cd07849   114 QILRGLKYIHSANVLHRDLKPSNLLLN---TNCdlKIC---DFGLAR 154
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
126-236 3.19e-06

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


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 50.26  E-value: 3.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  126 RLGRQILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLDFGLARQFTNSCGDVrppravagFRGTVRYASINAHR 205
Cdd:cd06619    99 RIAVAVVKGLTYLWSLKILHRDVKPSNMLV----NTRGQVKLCDFGVSTQLVNSIAKT--------YVGTNAYMAPERIS 166
                          90       100       110
                  ....*....|....*....|....*....|.
gi 530405409  206 NREMGRHDDLWSLFYMLVEFVVGQLPWRKIK 236
Cdd:cd06619   167 GEQYGIHSDVWSLGISFMELALGRFPYPQIQ 197
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
129-239 3.37e-06

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


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 50.05  E-value: 3.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  129 RQILESIESIHSVGFLHRDIKPSNFAMGRFPSTcrkcYMLDFGLARQF-------TNSCGD--VRPPRAVAGfrgtvrya 199
Cdd:cd14118   122 RDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHV----KIADFGVSNEFegddallSSTAGTpaFMAPEALSE-------- 189
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 530405409  200 sinaHRNREMGRHDDLWSLFYMLVEFVVGQLPW---------RKIKDKE 239
Cdd:cd14118   190 ----SRKKFSGKALDIWAMGVTLYCFVFGRCPFeddhilglhEKIKTDP 234
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
126-173 3.51e-06

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


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 50.06  E-value: 3.51e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 530405409  126 RLGRQILESIESIHSVGFLHRDIKPSNFamgrFPSTCRKCYMLDFGLA 173
Cdd:cd14046   108 RLFRQILEGLAYIHSQGIIHRDLKPVNI----FLDSNGNVKIGDFGLA 151
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
81-261 4.23e-06

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 49.85  E-value: 4.23e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409     81 DHVCRFIGCGRNDRFNYVVMQL-QGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfP 159
Cdd:smart00221   61 PNIVKLLGVCTEEEPLMIVMEYmPGGDLLDYLRKNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGE-N 139
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409    160 STCRKCymlDFGLARqFTNSCGDVRPPRAvagfRGTVRYASINAHRNREMGRHDDLWS---LFYMLVEFvvGQLPWRKIK 236
Cdd:smart00221  140 LVVKIS---DFGLSR-DLYDDDYYKVKGG----KLPIRWMAPESLKEGKFTSKSDVWSfgvLLWEIFTL--GEEPYPGMS 209
                           170       180
                    ....*....|....*....|....*.
gi 530405409    237 DKEQVGSIKERYdhRLML-KHLPPEF 261
Cdd:smart00221  210 NAEVLEYLKKGY--RLPKpPNCPPEL 233
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
91-251 4.43e-06

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


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 50.38  E-value: 4.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   91 RNDRFNYVVMQ-LQGRNLADLRRS----QSRGTFTISttlrlgrQILESIESIHSVGFLHRDIKPSNFAMGRFPstcrKC 165
Cdd:cd05621   122 QDDKYLYMVMEyMPGGDLVNLMSNydvpEKWAKFYTA-------EVVLALDAIHSMGLIHRDVKPDNMLLDKYG----HL 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  166 YMLDFGLARQFtNSCGDVRPPRAVagfrGTVRYASINAHRNR----EMGRHDDLWSLFYMLVEFVVGQLPWRKikdKEQV 241
Cdd:cd05621   191 KLADFGTCMKM-DETGMVHCDTAV----GTPDYISPEVLKSQggdgYYGRECDWWSVGVFLFEMLVGDTPFYA---DSLV 262
                         170
                  ....*....|
gi 530405409  242 GSIKERYDHR 251
Cdd:cd05621   263 GTYSKIMDHK 272
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
126-232 4.94e-06

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 49.74  E-value: 4.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  126 RLGRQILESIESIHSVGFLHRDIKPSNFAMgrFPSTCRKcyMLDFGLARQFTNSCGDVRPPRAVAGFRGTVRYASINAHR 205
Cdd:cd06631   107 RYTKQILEGVAYLHNNNVIHRDIKGNNIML--MPNGVIK--LIDFGCAKRLCINLSSGSQSQLLKSMRGTPYWMAPEVIN 182
                          90       100
                  ....*....|....*....|....*..
gi 530405409  206 NREMGRHDDLWSLFYMLVEFVVGQLPW 232
Cdd:cd06631   183 ETGHGRKSDIWSIGCTVFEMATGKPPW 209
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
97-268 5.58e-06

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


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 49.62  E-value: 5.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQL-QGRNLADLRrsQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAM----GRFPSTCRKCYML-DF 170
Cdd:cd14202    77 YLVMEYcNGGDLADYL--HTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLsysgGRKSNPNNIRIKIaDF 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  171 GLARQFTNSCgdvrpprAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKDKEqvgsIKERYD- 249
Cdd:cd14202   155 GFARYLQNNM-------MAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQD----LRLFYEk 223
                         170
                  ....*....|....*....
gi 530405409  250 HRLMLKHLPPEFSIFLDHI 268
Cdd:cd14202   224 NKSLSPNIPRETSSHLRQL 242
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
97-231 5.85e-06

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 49.22  E-value: 5.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQL-QGRNLADLRRSQSRGTFTISTtlRLGRQILESIESIHSVGFLHRDIKPSNFAMGrfpstcrKCYML---DFGL 172
Cdd:cd14162    76 YIIMELaENGDLLDYIRKNGALPEPQAR--RWFRQLVAGVEYCHSKGVVHRDLKCENLLLD-------KNNNLkitDFGF 146
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530405409  173 ARqftnscgdvRPPRAVAGFR-------GTVRYASINAHRNREM-GRHDDLWSLFYMLVEFVVGQLP 231
Cdd:cd14162   147 AR---------GVMKTKDGKPklsetycGSYAYASPEILRGIPYdPFLSDIWSMGVVLYTMVYGRLP 204
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
110-179 5.87e-06

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 49.48  E-value: 5.87e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530405409  110 LRRSQSRgtFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAM---GRFPSTcrkcymlDFGLARQFTNS 179
Cdd:cd07840    94 LDNPEVK--FTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILInndGVLKLA-------DFGLARPYTKE 157
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
92-175 6.34e-06

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 49.55  E-value: 6.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   92 NDRFNYVVMQL-QGRNLAD--LRRSQsrgtFTISTTLRLGRQILESIESIHSVGFLHRDIKPSN--FA-MGRFPSTCRKC 165
Cdd:cd14091    65 DGNSVYLVTELlRGGELLDriLRQKF----FSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNilYAdESGDPESLRIC 140
                          90
                  ....*....|
gi 530405409  166 ymlDFGLARQ 175
Cdd:cd14091   141 ---DFGFAKQ 147
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
92-235 6.37e-06

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


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 49.31  E-value: 6.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   92 NDRFNYVVMQLQGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAM-GRFpsTCRkcyMLDF 170
Cdd:cd14004    79 DDEFYYLVMEKHGSGMDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILdGNG--TIK---LIDF 153
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530405409  171 GLARQFTNSCGDVrppravagFRGTVRYASINAHR-NREMGRHDDLWSLFYMLVEFVVGQLPWRKI 235
Cdd:cd14004   154 GSAAYIKSGPFDT--------FVGTIDYAAPEVLRgNPYGGKEQDIWALGVLLYTLVFKENPFYNI 211
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
78-278 6.47e-06

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 49.25  E-value: 6.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   78 SGKDHVCRFIGCGRNDRFN----YVVMQLQGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVG--FLHRDIKPS 151
Cdd:cd13985    55 CGHPNIVQYYDSAILSSEGrkevLLLMEYCPGSLVDILEKSPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIE 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  152 NFAMgrfpSTCRKCYMLDFGLARqfTNSCGDVRPPRAVA-----GFRGTVRY---ASINAHRNREMGRHDDLWSL---FY 220
Cdd:cd13985   135 NILF----SNTGRFKLCDFGSAT--TEHYPLERAEEVNIieeeiQKNTTPMYrapEMIDLYSKKPIGEKADIWALgclLY 208
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530405409  221 MLVEFvvgQLPWrkiKDKEQVGSIKERYD----HRlmlkhLPPEFSIFLDHISSLDYFTKPD 278
Cdd:cd13985   209 KLCFF---KLPF---DESSKLAIVAGKYSipeqPR-----YSPELHDLIRHMLTPDPAERPD 259
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
81-232 6.54e-06

Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MEKK3, MEKK2, and related proteins; all contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKK) that activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 49.28  E-value: 6.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   81 DHVCRFIGCGRNDRFNYVVMQ-LQGRNLADLRRSQsrGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFamgrFP 159
Cdd:cd06625    62 ERIVQYYGCLQDEKSLSIFMEyMPGGSVKDEIKAY--GALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANI----LR 135
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530405409  160 STCRKCYMLDFGLARQFTNSC--GDVRPpravagFRGTVRYAS---INAHrnrEMGRHDDLWSLFYMLVEFVVGQLPW 232
Cdd:cd06625   136 DSNGNVKLGDFGASKRLQTICssTGMKS------VTGTPYWMSpevINGE---GYGRKADIWSVGCTVVEMLTTKPPW 204
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
97-239 6.71e-06

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 49.05  E-value: 6.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQ-LQGRNLADlrRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNF---AMGRFPSTcrkcymlDFGL 172
Cdd:cd05123    69 YLVLDyVPGGELFS--HLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENIlldSDGHIKLT-------DFGL 139
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530405409  173 ARQFTNscgdvRPPRAVAgFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLP---------WRKIKDKE 239
Cdd:cd05123   140 AKELSS-----DGDRTYT-FCGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPfyaenrkeiYEKILKSP 209
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
126-283 8.75e-06

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 48.88  E-value: 8.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  126 RLGRQILESIESIHSV-GFLHRDIKPSNFAMGRfPSTCRKCymlDFGLARQFTNScgdvrppraVAG-FRGTVRYASINA 203
Cdd:cd06605   103 KIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNS-RGQVKLC---DFGVSGQLVDS---------LAKtFVGTRSYMAPER 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  204 HRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKDK------EQVGSIKERYDHRLMLKHLPPEFSIFLDHISSLDYFTKP 277
Cdd:cd06605   170 ISGGKYTVKSDIWSLGLSLVELATGRFPYPPPNAKpsmmifELLSYIVDEPPPLLPSGKFSPDFQDFVSQCLQKDPTERP 249

                  ....*.
gi 530405409  278 DYQLLT 283
Cdd:cd06605   250 SYKELM 255
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
97-233 8.94e-06

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 48.85  E-value: 8.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQL-QGRNLADLRrsQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAM---GRFPSTCR--KCYMLDF 170
Cdd:cd14201    81 FLVMEYcNGGDLADYL--QAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLsyaSRKKSSVSgiRIKIADF 158
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530405409  171 GLARQFTNScgdvrppRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWR 233
Cdd:cd14201   159 GFARYLQSN-------MMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQ 214
K-ycf53 COG5752
Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 ...
85-248 9.88e-06

Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 porphyrin-binding domain [Signal transduction mechanisms];


Pssm-ID: 444462 [Multi-domain]  Cd Length: 466  Bit Score: 49.62  E-value: 9.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   85 RFIGCGRNDRFNYVVMQL-QGRNLADlrRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFaMGRfpSTCR 163
Cdd:COG5752   102 ELLAYFEQDQRLYLVQEFiEGQTLAQ--ELEKKGVFSESQIWQLLKDLLPVLQFIHSRNVIHRDIKPANI-IRR--RSDG 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  164 KCYMLDFGLARQFTN-----------SCGDVRPPRAvagfRGTVRYASinahrnremgrhdDLWSLFYMLVEFVVGQLP- 231
Cdd:COG5752   177 KLVLIDFGVAKLLTItallqtgtiigTPEYMAPEQL----RGKVFPAS-------------DLYSLGVTCIYLLTGVSPf 239
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 530405409  232 -----------WR--------------KIKDKEQVGSIKERY 248
Cdd:COG5752   240 dlfdvsedrwvWRdflppgtkvsdrlgQILDKLLQNALKQRY 281
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
97-174 9.88e-06

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


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 48.49  E-value: 9.88e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530405409   97 YVVMQL-QGRNLADlrRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFPSTcRKCYMLDFGLAR 174
Cdd:cd14167    77 YLIMQLvSGGELFD--RIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSLDED-SKIMISDFGLSK 152
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
97-175 1.09e-05

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 48.30  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQL-QGRNLADlrRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFaMGRFPSTCRKCYMLDFGLARQ 175
Cdd:cd14087    73 YMVMELaTGGELFD--RIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENL-LYYHPGPDSKIMITDFGLAST 149
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
93-179 1.10e-05

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


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 49.06  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   93 DRFN--YVVMQLQGRNLADLRRSQSRGT------FTIsttlrlgrQILESIESIHSVGFLHRDIKPSNFAMGrfpSTCRK 164
Cdd:cd07834    74 EEFNdvYIVTELMETDLHKVIKSPQPLTddhiqyFLY--------QILRGLKYLHSAGVIHRDLKPSNILVN---SNCDL 142
                          90
                  ....*....|....*
gi 530405409  165 CYmLDFGLARQFTNS 179
Cdd:cd07834   143 KI-CDFGLARGVDPD 156
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
82-268 1.11e-05

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: 48.28  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   82 HVCRFIGCGRNDRFNYVVMQL-QGRNLADlrRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFamgrfps 160
Cdd:cd14003    60 NIIKLYEVIETENKIYLVMEYaSGGELFD--YIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENI------- 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  161 tcrkcyML---------DFGLARQFTN------SCgdvrppravagfrGTVRYAS--INAHRNREmGRHDDLWS----LF 219
Cdd:cd14003   131 ------LLdkngnlkiiDFGLSNEFRGgsllktFC-------------GTPAYAApeVLLGRKYD-GPKADVWSlgviLY 190
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 530405409  220 YMLvefvVGQLPWRKIKDKEQVGSIKERYDHrlMLKHLPPEFSIFLDHI 268
Cdd:cd14003   191 AML----TGYLPFDDDNDSKLFRKILKGKYP--IPSHLSPDARDLIRRM 233
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
129-243 1.11e-05

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


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 48.43  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  129 RQILESIESIHSVGFLHRDIKPSNFAMGRFPSTCRkcyMLDFGlarqftnsCGDVRPPRAVAGFRGTVRYAS---INAHR 205
Cdd:cd14100   113 RQVLEAVRHCHNCGVLHRDIKDENILIDLNTGELK---LIDFG--------SGALLKDTVYTDFDGTRVYSPpewIRFHR 181
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 530405409  206 NRemGRHDDLWSLFYMLVEFVVGQLPWRkiKDKEQVGS 243
Cdd:cd14100   182 YH--GRSAAVWSLGILLYDMVCGDIPFE--HDEEIIRG 215
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
97-231 1.22e-05

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 48.36  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQL-QGRNLADLRRSQsrGTFTISTTLRLGRQILESIESIHSV-GFLHRDIKPSNFAMGRfpstcRKCYML-DFGLA 173
Cdd:cd06623    75 SIVLEYmDGGSLADLLKKV--GKIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINS-----KGEVKIaDFGIS 147
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 530405409  174 RQFTNScGDVRppravAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLP 231
Cdd:cd06623   148 KVLENT-LDQC-----NTFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFP 199
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
85-231 1.26e-05

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 48.56  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   85 RFIGCGRNDRFNYVVM-QLQGRNLADLRRSQSRGTFTISTTLRL-GRQILESIESIHSVGFLHRDIKPSNFAMGRFPSTC 162
Cdd:cd06624    69 QYLGSVSEDGFFKIFMeQVPGGSLSALLRSKWGPLKDNENTIGYyTKQILEGLKYLHDNKIVHRDIKGDNVLVNTYSGVV 148
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530405409  163 RkcyMLDFGLARQFT--NSCGDVrppravagFRGTVRYAS--INAHRNREMGRHDDLWSLFYMLVEFVVGQLP 231
Cdd:cd06624   149 K---ISDFGTSKRLAgiNPCTET--------FTGTLQYMApeVIDKGQRGYGPPADIWSLGCTIIEMATGKPP 210
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
97-232 1.68e-05

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 48.10  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQL-QGRNLAD--LRR---SQSRGTFTISTtlrlgrqILESIESIHSVGFLHRDIKPSNFAM---GRFPSTCRKCym 167
Cdd:cd14175    71 YLVTELmRGGELLDkiLRQkffSEREASSVLHT-------ICKTVEYLHSQGVVHRDLKPSNILYvdeSGNPESLRIC-- 141
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530405409  168 lDFGLARQFTNSCGDVRPPRAVAGFrgtvryASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 232
Cdd:cd14175   142 -DFGFAKQLRAENGLLMTPCYTANF------VAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPF 199
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
94-232 1.83e-05

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


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 48.09  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   94 RFNYVVMQL-QGRNLAD--LRR---SQSRGTFTISTtlrlgrqILESIESIHSVGFLHRDIKPSNFAM---GRFPSTCRK 164
Cdd:cd14178    70 KFVYLVMELmRGGELLDriLRQkcfSEREASAVLCT-------ITKTVEYLHSQGVVHRDLKPSNILYmdeSGNPESIRI 142
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530405409  165 CymlDFGLARQFTNSCGDVRPPRAVAGFrgtvryASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 232
Cdd:cd14178   143 C---DFGFAKQLRAENGLLMTPCYTANF------VAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPF 201
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
97-288 1.87e-05

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 47.73  E-value: 1.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQLQGR-NLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLDFGLARQ 175
Cdd:cd05072    78 YIITEYMAKgSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLV----SESLMCKIADFGLARV 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  176 FTNSCGDVRppravAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVV-GQLPWRKIKDKEQVGSIKERYDHRLMl 254
Cdd:cd05072   154 IEDNEYTAR-----EGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPYPGMSNSDVMSALQRGYRMPRM- 227
                         170       180       190
                  ....*....|....*....|....*....|....
gi 530405409  255 KHLPPEFSIFLDHISSLDYFTKPDYQLLTSVFDN 288
Cdd:cd05072   228 ENCPDELYDIMKTCWKEKAEERPTFDYLQSVLDD 261
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
92-233 2.13e-05

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 47.82  E-value: 2.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   92 NDRFNYVVMQ-LQGRNLADLRRSqsRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFPSTcrkcYMLDF 170
Cdd:cd05612    72 DQRFLYMLMEyVPGGELFSYLRN--SGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHI----KLTDF 145
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530405409  171 GLARQFTNS----CgdvrppravagfrGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWR 233
Cdd:cd05612   146 GFAKKLRDRtwtlC-------------GTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFF 199
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
130-239 2.22e-05

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 48.47  E-value: 2.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  130 QILESIESIHSVGFLHRDIKPSN-FAMgrfPSTCRKcyMLDFGLARQFTNSCG-DVrppraVAGFRGTVRYASINAHRNR 207
Cdd:PTZ00267  177 QIVLALDEVHSRKMMHRDLKSANiFLM---PTGIIK--LGDFGFSKQYSDSVSlDV-----ASSFCGTPYYLAPELWERK 246
                          90       100       110
                  ....*....|....*....|....*....|..
gi 530405409  208 EMGRHDDLWSLFYMLVEFVVGQLPWRKIKDKE 239
Cdd:PTZ00267  247 RYSKKADMWSLGVILYELLTLHRPFKGPSQRE 278
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
97-185 2.57e-05

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


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 47.75  E-value: 2.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQLQGRNLADLRRSQSRgTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMgrfpsTCRKCYML-DFGLARQ 175
Cdd:cd07845    84 FLVMEYCEQDLASLLDNMPT-PFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLL-----TDKGCLKIaDFGLART 157
                          90
                  ....*....|
gi 530405409  176 FTNSCGDVRP 185
Cdd:cd07845   158 YGLPAKPMTP 167
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
129-244 2.58e-05

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 47.31  E-value: 2.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  129 RQILESIESIHSVGFLHRDIKPSNFAMgrFPSTCRKCYMLDFGLARQFTNScGDVRPpravagFRGTVRYASINAHRNRE 208
Cdd:cd14191   107 RQISEGVEYIHKQGIVHLDLKPENIMC--VNKTGTKIKLIDFGLARRLENA-GSLKV------LFGTPEFVAPEVINYEP 177
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 530405409  209 MGRHDDLWSLFYMLVEFVVGQLPWRKIKDKEQVGSI 244
Cdd:cd14191   178 IGYATDMWSIGVICYILVSGLSPFMGDNDNETLANV 213
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
97-245 2.75e-05

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 47.28  E-value: 2.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQL-QGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFamgrFPSTCRKCYMLDFGLARQ 175
Cdd:cd08219    74 YIVMEYcDGGDLMQKIKLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNI----FLTQNGKVKLGDFGSARL 149
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530405409  176 FTNscgdvrPPRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLP-----WRKIKDKEQVGSIK 245
Cdd:cd08219   150 LTS------PGAYACTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPfqansWKNLILKVCQGSYK 218
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
130-232 2.89e-05

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 47.42  E-value: 2.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  130 QILESIESIHSVGFLHRDIKPSNFAMGrfpSTCRKC--YMLDFGLARQFTNScgdvrpPRAVAGFRGTVRYASINAHRNR 207
Cdd:cd14086   108 QILESVNHCHQNGIVHRDLKPENLLLA---SKSKGAavKLADFGLAIEVQGD------QQAWFGFAGTPGYLSPEVLRKD 178
                          90       100
                  ....*....|....*....|....*
gi 530405409  208 EMGRHDDLWSLFYMLVEFVVGQLPW 232
Cdd:cd14086   179 PYGKPVDIWACGVILYILLVGYPPF 203
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
81-286 3.14e-05

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 47.14  E-value: 3.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   81 DHVCRFIGCGRN-DRFNYVVMQLQGRNLADLRrsQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfp 159
Cdd:cd06628    66 ENIVQYLGSSSDaNHLNIFLEYVPGGSVATLL--NNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDN-- 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  160 STCRKcyMLDFGLARQ-----FTNSCGDVRPpravaGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRK 234
Cdd:cd06628   142 KGGIK--ISDFGISKKleansLSTKNNGARP-----SLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPD 214
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530405409  235 IKDKEQVGSIKErydhrLMLKHLPPEFSI----FLDHISSLDYFTKPDY-QLLTSVF 286
Cdd:cd06628   215 CTQMQAIFKIGE-----NASPTIPSNISSeardFLEKTFEIDHNKRPTAdELLKHPF 266
pknD PRK13184
serine/threonine-protein kinase PknD;
109-262 3.15e-05

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 48.61  E-value: 3.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  109 DLRRSQSRGTFtisttLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFPstcrKCYMLDFGLAR-------------- 174
Cdd:PRK13184  105 ELAEKTSVGAF-----LSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFG----EVVILDWGAAIfkkleeedlldidv 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  175 QFTNSCGD--VRPPRAVagfrGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWR-----KIKDKEQVGSIKER 247
Cdd:PRK13184  176 DERNICYSsmTIPGKIV----GTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRrkkgrKISYRDVILSPIEV 251
                         170
                  ....*....|....*
gi 530405409  248 YDHRlmlkHLPPEFS 262
Cdd:PRK13184  252 APYR----EIPPFLS 262
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
97-232 3.28e-05

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 47.23  E-value: 3.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQ-LQGRNLADLRRSQSRGTFTISTTLRlgrQILESIESIHSVGFLHRDIKPSNFAMGRFPSTcrkcYMLDFGLarq 175
Cdd:cd06647    80 WVVMEyLAGGSLTDVVTETCMDEGQIAAVCR---ECLQALEFLHSNQVIHRDIKSDNILLGMDGSV----KLTDFGF--- 149
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 530405409  176 ftnsCGDVRPP-RAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 232
Cdd:cd06647   150 ----CAQITPEqSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY 203
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
116-239 3.41e-05

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


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 46.87  E-value: 3.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  116 RGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFPSTCRkcyMLDFGlarqftnsCGDVRPPRAVAGFRGT 195
Cdd:cd14102    99 KGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLRTGELK---LIDFG--------SGALLKDTVYTDFDGT 167
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 530405409  196 VRYAS---INAHRNRemGRHDDLWSLFYMLVEFVVGQLPWRkiKDKE 239
Cdd:cd14102   168 RVYSPpewIRYHRYH--GRSATVWSLGVLLYDMVCGDIPFE--QDEE 210
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
81-175 3.49e-05

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: 46.72  E-value: 3.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409    81 DHVCRFIGCGRNDRFNYVVMQL-QGRNLAD-LRRSQSRgtFTISTTLRLGRQILESIESIHSVGFLHRDIkpsnfamgrf 158
Cdd:pfam07714   61 PNIVKLLGVCTQGEPLYIVTEYmPGGDLLDfLRKHKRK--LTLKDLLSMALQIAKGMEYLESKNFVHRDL---------- 128
                           90       100
                   ....*....|....*....|....*.
gi 530405409   159 psTCRKCyML---------DFGLARQ 175
Cdd:pfam07714  129 --AARNC-LVsenlvvkisDFGLSRD 151
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
97-177 3.76e-05

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: 46.93  E-value: 3.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQLQGRNLADLRRSQSRGtFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfPSTCRKCymlDFGLARQF 176
Cdd:cd07833    76 YLVFEYVERTLLELLEASPGG-LPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSE-SGVLKLC---DFGFARAL 150

                  .
gi 530405409  177 T 177
Cdd:cd07833   151 T 151
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
97-175 4.11e-05

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 46.48  E-value: 4.11e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530405409   97 YVVMQLQGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLDFGLARQ 175
Cdd:cd14119    72 YMVMEYCVGGLQEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLL----TTDGTLKISDFGVAEA 146
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
97-248 4.18e-05

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 46.51  E-value: 4.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQLQGR-NLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLDFGLARQ 175
Cdd:cd05082    76 YIVTEYMAKgSLVDYLRSRGRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLV----SEDNVAKVSDFGLTKE 151
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530405409  176 FTNSCGDVRPPravagfrgtVRYASINAHRNREMGRHDDLWSLFYMLVE-FVVGQLPWRKIKDKEQVGSIKERY 248
Cdd:cd05082   152 ASSTQDTGKLP---------VKWTAPEALREKKFSTKSDVWSFGILLWEiYSFGRVPYPRIPLKDVVPRVEKGY 216
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
92-232 4.29e-05

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 46.73  E-value: 4.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   92 NDRFnYVVMQL-QGRNLADLRRS--QSRGTFTISTTLRLGRQILESIESIH-SVGFLHRDIKPSNFAMGrfpsTCRKCYM 167
Cdd:cd08528    81 NDRL-YIVMELiEGAPLGEHFSSlkEKNEHFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLG----EDDKVTI 155
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530405409  168 LDFGLARQFTNSCGDVrppRAVAgfrGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 232
Cdd:cd08528   156 TDFGLAKQKGPESSKM---TSVV---GTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPF 214
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
130-176 4.54e-05

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: 46.80  E-value: 4.54e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 530405409  130 QILESIESIHSVGFLHRDIKPSNF---AMGrfpstcrKCYMLDFGLARQF 176
Cdd:cd07841   110 MTLRGLEYLHSNWILHRDLKPNNLliaSDG-------VLKLADFGLARSF 152
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
134-231 4.63e-05

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 46.99  E-value: 4.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  134 SIESIHSVGFLHRDIKPSNF---AMGRFPstcrkcyMLDFGLARQFtNSCGDVRPPRAVagfrGTVRYASINAHRNRE-- 208
Cdd:cd05596   137 ALDAIHSMGFVHRDVKPDNMlldASGHLK-------LADFGTCMKM-DKDGLVRSDTAV----GTPDYISPEVLKSQGgd 204
                          90       100
                  ....*....|....*....|....*
gi 530405409  209 --MGRHDDLWSLFYMLVEFVVGQLP 231
Cdd:cd05596   205 gvYGRECDWWSVGVFLYEMLVGDTP 229
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
82-231 4.85e-05

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: 46.48  E-value: 4.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   82 HVCRFIGCGRNDRFNYVVMQ-LQGRNLAD-LRRsqsRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMgrfp 159
Cdd:cd14081    62 NVLKLYDVYENKKYLYLVLEyVSGGELFDyLVK---KGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLL---- 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  160 STCRKCYMLDFGLAR-QFTN-----SCgdvrppravagfrGTVRYAS--INAHRNREmGRHDDLWSLFYMLVEFVVGQLP 231
Cdd:cd14081   135 DEKNNIKIADFGMASlQPEGslletSC-------------GSPHYACpeVIKGEKYD-GRKADIWSCGVILYALLVGALP 200
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
73-236 5.02e-05

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: 46.61  E-value: 5.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   73 ERKMESGKD----HVCRFIGCGRNDRFNYVVMQL-QGRNLAD-------LRRSQSRGTFtisttlrlgRQILESIESIHS 140
Cdd:cd14078    49 KTEIEALKNlshqHICRLYHVIETDNKIFMVLEYcPGGELFDyivakdrLSEDEARVFF---------RQIVSAVAYVHS 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  141 VGFLHRDIKPSNFAMGRFpstcRKCYMLDFGLARQftnscgdvrpPRAVAGFR-----GTVRYASINAHRNRE-MGRHDD 214
Cdd:cd14078   120 QGYAHRDLKPENLLLDED----QNLKLIDFGLCAK----------PKGGMDHHletccGSPAYAAPELIQGKPyIGSEAD 185
                         170       180       190
                  ....*....|....*....|....*....|.
gi 530405409  215 LWSLFYMLVEFVVGQLP---------WRKIK 236
Cdd:cd14078   186 VWSMGVLLYALLCGFLPfdddnvmalYRKIQ 216
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
97-174 5.17e-05

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


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 46.21  E-value: 5.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQ-LQGRNLADlrRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFPSTCRKCYML-----DF 170
Cdd:cd14120    68 YLVMEyCNGGDLAD--YLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGRKPSPNDIrlkiaDF 145

                  ....
gi 530405409  171 GLAR 174
Cdd:cd14120   146 GFAR 149
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
82-249 5.39e-05

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 46.77  E-value: 5.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   82 HVCRFIGCGRNDRFNYVVMQ-LQGRNLA--DLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRf 158
Cdd:cd14094    66 HIVELLETYSSDGMLYMVFEfMDGADLCfeIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAS- 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  159 PSTCRKCYMLDFGLARQFTNS----CGDVrppravagfrGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRK 234
Cdd:cd14094   145 KENSAPVKLGGFGVAIQLGESglvaGGRV----------GTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG 214
                         170
                  ....*....|....*
gi 530405409  235 IKDKEQVGSIKERYD 249
Cdd:cd14094   215 TKERLFEGIIKGKYK 229
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
90-176 5.78e-05

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


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 46.45  E-value: 5.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   90 GRNDRFNYVVMQLQGRNLADLRrSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAM---GRFpSTCrkcy 166
Cdd:cd07843    75 GSNLDKIYMVMEYVEHDLKSLM-ETMKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLnnrGIL-KIC---- 148
                          90
                  ....*....|
gi 530405409  167 mlDFGLARQF 176
Cdd:cd07843   149 --DFGLAREY 156
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
97-253 6.34e-05

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 46.95  E-value: 6.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQLQGRNLAD---LRRSQSRGTFtisttlrLGRQILESIESIHSVGFLHRDIKPSNFAMgrfPSTCrKCYMLDFGLA 173
Cdd:cd07876   102 YLVMELMDANLCQvihMELDHERMSY-------LLYQMLCGIKHLHSAGIIHRDLKPSNIVV---KSDC-TLKILDFGLA 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  174 RqfTNSCGDVRPPRAVagfrgTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQL---------PWRKIkdKEQVGSI 244
Cdd:cd07876   171 R--TACTNFMMTPYVV-----TRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVifqgtdhidQWNKV--IEQLGTP 241

                  ....*....
gi 530405409  245 KERYDHRLM 253
Cdd:cd07876   242 SAEFMNRLQ 250
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
133-270 7.39e-05

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 46.09  E-value: 7.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  133 ESIESIHSVGFLHRDIKPSNFAMGRFPSTCRKCYMLDFGLARQFTnscgdvRPPRAVAgfrGTVRYASINAHRNREMGRH 212
Cdd:cd14185   109 EALVYIHSKHIVHRDLKPENLLVQHNPDKSTTLKLADFGLAKYVT------GPIFTVC---GTPTYVAPEILSEKGYGLE 179
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 530405409  213 DDLWSLFYMLVEFVVGQLPWRKI-KDKEQVGSIKERYDHRLmlkhLPPefsiFLDHISS 270
Cdd:cd14185   180 VDMWAAGVILYILLCGFPPFRSPeRDQEELFQIIQLGHYEF----LPP----YWDNISE 230
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
97-252 7.39e-05

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 46.25  E-value: 7.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQLQGRNLA-----DLrrSQSRGTFtisttlrLGRQILESIESIHSVGFLHRDIKPSNFAMgrfPSTCrKCYMLDFG 171
Cdd:cd07850    81 YLVMELMDANLCqviqmDL--DHERMSY-------LLYQMLCGIKHLHSAGIIHRDLKPSNIVV---KSDC-TLKILDFG 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  172 LARQftnscgdvrpprAVAGFRGT----VRYasinaHRNRE----MGRHD--DLWSLFYMLVEFVVGQL---------PW 232
Cdd:cd07850   148 LART------------AGTSFMMTpyvvTRY-----YRAPEvilgMGYKEnvDIWSVGCIMGEMIRGTVlfpgtdhidQW 210
                         170       180
                  ....*....|....*....|
gi 530405409  233 RKIkdKEQVGSIKERYDHRL 252
Cdd:cd07850   211 NKI--IEQLGTPSDEFMSRL 228
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
130-229 8.14e-05

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: 45.88  E-value: 8.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  130 QILESIESIHSVGFLHRDIKPSNFAMGrfPSTCRKcyMLDFGLARqFTNSCGDV-------RPPRAVAGFRGTVRYasin 202
Cdd:cd07846   108 QILRGIDFCHSHNIIHRDIKPENILVS--QSGVVK--LCDFGFAR-TLAAPGEVytdyvatRWYRAPELLVGDTKY---- 178
                          90       100
                  ....*....|....*....|....*..
gi 530405409  203 ahrnremGRHDDLWSLFYMLVEFVVGQ 229
Cdd:cd07846   179 -------GKAVDVWAVGCLVTEMLTGE 198
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
106-231 8.31e-05

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 46.56  E-value: 8.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  106 NLADLRRSQSRgtFTISttlrlgrQILESIESIHSVGFLHRDIKPSNF---AMGRFPSTcrkcymlDFGLARQFTNS--- 179
Cdd:cd05600   104 NSGILSEEHAR--FYIA-------EMFAAISSLHQLGYIHRDLKPENFlidSSGHIKLT-------DFGLASGTLSPkki 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  180 -CGDVRPPRAvagFRGTVRYASINAHRN--REMGRHD----------------------------DLWSLFYMLVEFVVG 228
Cdd:cd05600   168 eSMKIRLEEV---KNTAFLELTAKERRNiyRAMRKEDqnyansvvgspdymapevlrgegydltvDYWSLGCILFECLVG 244

                  ...
gi 530405409  229 QLP 231
Cdd:cd05600   245 FPP 247
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
97-280 8.37e-05

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


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 45.83  E-value: 8.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQLQGR-NLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfpstCRKCYMLDFGLARQ 175
Cdd:cd05069    82 YIVTEFMGKgSLLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGD----NLVCKIADFGLARL 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  176 FTNSCGDVRppravAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVV-GQLPWRKIKDKEQVGSIKERYD----- 249
Cdd:cd05069   158 IEDNEYTAR-----QGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMVNREVLEQVERGYRmpcpq 232
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 530405409  250 ------HRLM---LKHLPPEFSIFlDHISSL--DYF--TKPDYQ 280
Cdd:cd05069   233 gcpeslHELMklcWKKDPDERPTF-EYIQSFleDYFtaTEPQYQ 275
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
97-249 8.47e-05

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


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 46.19  E-value: 8.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQL-QGRNLADlrRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFaMGRFPSTCRKCYMLDFGLARQ 175
Cdd:cd14168    84 YLVMQLvSGGELFD--RIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENL-LYFSQDEESKIMISDFGLSKM 160
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530405409  176 ftNSCGDVRPPRAvagfrGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKDK---EQVGSIKERYD 249
Cdd:cd14168   161 --EGKGDVMSTAC-----GTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSklfEQILKADYEFD 230
PLN03225 PLN03225
Serine/threonine-protein kinase SNT7; Provisional
95-173 8.60e-05

Serine/threonine-protein kinase SNT7; Provisional


Pssm-ID: 215638 [Multi-domain]  Cd Length: 566  Bit Score: 46.71  E-value: 8.60e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530405409   95 FNYVVMQLQGRNLADLRRSQSRGTFTISTTLRlgrQILESIESIHSVGFLHRDIKPSNFAmgrFPSTCRKCYMLDFGLA 173
Cdd:PLN03225  231 FPYNVEPYLLGKVQDLPKGLERENKIIQTIMR---QILFALDGLHSTGIVHRDVKPQNII---FSEGSGSFKIIDLGAA 303
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
135-231 8.75e-05

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 46.16  E-value: 8.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  135 IESIHSVGFLHRDIKPSNFAMGRfpSTCRKcyMLDFGLarqftnsCgdvrppravAGFR--------------GTVRYAS 200
Cdd:cd05598   114 IESVHKMGFIHRDIKPDNILIDR--DGHIK--LTDFGL-------C---------TGFRwthdskyylahslvGTPNYIA 173
                          90       100       110
                  ....*....|....*....|....*....|.
gi 530405409  201 INAHRNREMGRHDDLWSLFYMLVEFVVGQLP 231
Cdd:cd05598   174 PEVLLRTGYTQLCDWWSVGVILYEMLVGQPP 204
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
98-179 1.01e-04

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 45.91  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   98 VVMQLQGRNLADLRRSQSRgtFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFamgrFPSTCRKCYMLDFGLARQFT 177
Cdd:PTZ00024   97 LVMDIMASDLKKVVDRKIR--LTESQVKCILLQILNGLNVLHKWYFMHRDLSPANI----FINSKGICKIADFGLARRYG 170

                  ..
gi 530405409  178 NS 179
Cdd:PTZ00024  171 YP 172
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
78-152 1.02e-04

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 46.02  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   78 SGKDHVCRFIGCgrndrFNY-----VVMQLQGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSN 152
Cdd:cd14134    71 NGKSHCVQLRDW-----FDYrghmcIVFELLGPSLYDFLKKNNYGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPEN 145
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
95-247 1.08e-04

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: 45.20  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   95 FNYVVmqLQGRnladLRRSQSRGTFtisttlrlgRQILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLDFGLAR 174
Cdd:cd14072    87 FDYLV--AHGR----MKEKEARAKF---------RQIVSAVQYCHQKRIVHRDLKAENLLL----DADMNIKIADFGFSN 147
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530405409  175 QFTnscgdvrPPRAVAGFRGTVRYASINAHRNREM-GRHDDLWSLFYMLVEFVVGQLPWrkikDKEQVGSIKER 247
Cdd:cd14072   148 EFT-------PGNKLDTFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPF----DGQNLKELRER 210
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
111-232 1.11e-04

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


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 45.33  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  111 RRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGrfpsTCRKCYMLDFGLARQFTNS-----CG--DV 183
Cdd:cd14116    94 RELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLG----SAGELKIADFGWSVHAPSSrrttlCGtlDY 169
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 530405409  184 RPPRAVAGfrgtvryasinahrnREMGRHDDLWSLFYMLVEFVVGQLPW 232
Cdd:cd14116   170 LPPEMIEG---------------RMHDEKVDLWSLGVLCYEFLVGKPPF 203
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
97-179 1.26e-04

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 45.82  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQLQGRNLADLRRSQsrGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGrfpSTCrKCYMLDFGLARQF 176
Cdd:cd07855    86 YVVLDLMESDLHHIIHSD--QPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVN---ENC-ELKIGDFGMARGL 159

                  ...
gi 530405409  177 TNS 179
Cdd:cd07855   160 CTS 162
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
81-231 1.36e-04

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: 44.89  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   81 DHVCRFIGCGRNDRFNYVVMQ-LQGRNLADLRRsQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFP 159
Cdd:cd06614    56 PNIVDYYDSYLVGDELWVVMEyMDGGSLTDIIT-QNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDG 134
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530405409  160 StcrkCYMLDFGLARQFTNScgdvRPPRA--VagfrGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLP 231
Cdd:cd06614   135 S----VKLADFGFAAQLTKE----KSKRNsvV----GTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPP 196
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
96-232 1.41e-04

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 44.85  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   96 NYVVMQLQGRNLADLRR--SQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLDFGLA 173
Cdd:cd14186    74 NYVYLVLEMCHNGEMSRylKNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLL----TRNMNIKIADFGLA 149
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 530405409  174 RQFTnscgdvRPPRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 232
Cdd:cd14186   150 TQLK------MPHEKHFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPF 202
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
82-289 1.49e-04

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: 44.92  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   82 HVCRFIGCGRNDRFNYVVMQL-QGRNLADLRRSqsRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFamgrFPS 160
Cdd:cd14187    68 HVVGFHGFFEDNDFVYVVLELcRRRSLLELHKR--RKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNL----FLN 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  161 TCRKCYMLDFGLArqfTNSCGDVRPPRAVAgfrGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKDKEQ 240
Cdd:cd14187   142 DDMEVKIGDFGLA---TKVEYDGERKKTLC---GTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKET 215
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 530405409  241 VGSIKEryDHRLMLKHLPPEFSIFLDHISSLDYFTKPDY-QLLTSVFDNS 289
Cdd:cd14187   216 YLRIKK--NEYSIPKHINPVAASLIQKMLQTDPTARPTInELLNDEFFTS 263
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
134-231 1.53e-04

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


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 45.42  E-value: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  134 SIESIHSVGFLHRDIKPSNFAMGRfpstCRKCYMLDFGlarqftnSC------GDVRPPRAVagfrGTVRYASINAHRNR 207
Cdd:cd05597   114 AIDSIHQLGYVHRDIKPDNVLLDR----NGHIRLADFG-------SClklredGTVQSSVAV----GTPDYISPEILQAM 178
                          90       100
                  ....*....|....*....|....*....
gi 530405409  208 EMGRHD-----DLWSLFYMLVEFVVGQLP 231
Cdd:cd05597   179 EDGKGRygpecDWWSLGVCMYEMLYGETP 207
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
82-233 1.58e-04

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


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 44.91  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   82 HVCRFIGCGRNDRFNYVVMQ-LQGRNLAD-LRRsqsRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMgrfp 159
Cdd:cd14009    53 NIVRLYDVQKTEDFIYLVLEyCAGGDLSQyIRK---RGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLL---- 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  160 STCRKCYML---DFGLARQFtnscgdvrPPRAVAG-FRGTVRYasinahrnreMG-------RHD---DLWSLFYMLVEF 225
Cdd:cd14009   126 STSGDDPVLkiaDFGFARSL--------QPASMAEtLCGSPLY----------MApeilqfqKYDakaDLWSVGAILFEM 187

                  ....*...
gi 530405409  226 VVGQLPWR 233
Cdd:cd14009   188 LVGKPPFR 195
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
97-175 1.62e-04

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


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 43.41  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQ-LQGRNLADLRRSQSRgtftistTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfpstcRKCYMLDFGLARQ 175
Cdd:COG3642    32 DLVMEyIEGETLADLLEEGEL-------PPELLRELGRLLARLHRAGIVHGDLTTSNILVDD-----GGVYLIDFGLARY 99
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
129-238 1.76e-04

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


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 44.94  E-value: 1.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  129 RQILESIESIHSVGFLHRDIKPSNFAMGRFPSTcrkcYMLDFGLARQFTnscGDVRPPRAVAGFRGTVRYASINAHRNRE 208
Cdd:cd14200   131 RDIVLGIEYLHYQKIVHRDIKPSNLLLGDDGHV----KIADFGVSNQFE---GNDALLSSTAGTPAFMAPETLSDSGQSF 203
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 530405409  209 MGRHDDLWSLFYMLVEFVVGQLPW---------RKIKDK 238
Cdd:cd14200   204 SGKALDVWAMGVTLYCFVYGKCPFidefilalhNKIKNK 242
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
73-265 1.82e-04

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


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 44.83  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   73 ERKMESGKD----HVCRFIGCGRNDRFNYVVMQlqgRNLAD-LRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRD 147
Cdd:cd14112    48 VREFESLRTlqheNVQRLIAAFKPSNFAYLVME---KLQEDvFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLD 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  148 IKPSNFAMGRFPSTCRKcyMLDFGLArQFTNSCGDVRPPravagfrGTVRYASINAHRNRE-MGRHDDLWSLFYMLVEFV 226
Cdd:cd14112   125 VQPDNIMFQSVRSWQVK--LVDFGRA-QKVSKLGKVPVD-------GDTDWASPEFHNPETpITVQSDIWGLGVLTFCLL 194
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 530405409  227 VGQLPWRKIKDKE---QVGSIKERYDHRLMLKHLPPEFSIFL 265
Cdd:cd14112   195 SGFHPFTSEYDDEeetKENVIFVKCRPNLIFVEATQEALRFA 236
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
129-250 1.86e-04

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 44.69  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  129 RQILESIESIHSVGFLHRDIKPSNFAMGRFPSTCRkCYMLDFGLARQFTNS------CGDVR--PPRAVAGFrGTVRYas 200
Cdd:cd14084   118 YQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEECL-IKITDFGLSKILGETslmktlCGTPTylAPEVLRSF-GTEGY-- 193
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 530405409  201 inahrnremGRHDDLWSL----FYMLvefvVGQLPW----RKIKDKEQVGSIKERYDH 250
Cdd:cd14084   194 ---------TRAVDCWSLgvilFICL----SGYPPFseeyTQMSLKEQILSGKYTFIP 238
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
97-280 1.92e-04

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 44.67  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQLQGR-NLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGrfpsTCRKCYMLDFGLARQ 175
Cdd:cd05070    79 YIVTEYMSKgSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVG----NGLICKIADFGLARL 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  176 FTNSCGDVRppravAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVV-GQLPWRKIKDKEQVGSIKERYD----- 249
Cdd:cd05070   155 IEDNEYTAR-----QGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQVERGYRmpcpq 229
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 530405409  250 ------HRLML---KHLPPEFSIFlDHISSL--DYF--TKPDYQ 280
Cdd:cd05070   230 dcpislHELMIhcwKKDPEERPTF-EYLQGFleDYFtaTEPQYQ 272
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
130-247 1.93e-04

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


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 44.96  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  130 QILESIESIHSVGFLHRDIKPSNFAMGRFPSTcrkcYMLDFGLARQFTNscGDvrpprAVAGFRGTVRYASINAHRNREM 209
Cdd:cd05632   112 EILCGLEDLHRENTVYRDLKPENILLDDYGHI----RISDLGLAVKIPE--GE-----SIRGRVGTVGYMAPEVLNNQRY 180
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 530405409  210 GRHDDLWSLFYMLVEFVVGQLPWRKIKDKEQVGSIKER 247
Cdd:cd05632   181 TLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVDRR 218
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
89-232 2.02e-04

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


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 44.64  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   89 CGRNDRFNYVVMQLQGRNLadLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFaMGRFPSTCRKCYML 168
Cdd:cd14174    69 FEDDTRFYLVFEKLRGGSI--LAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENI-LCESPDKVSPVKIC 145
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530405409  169 DFGLAR--QFTNSCGDVRPPRAVAGFrGTVRYASINAHR--NREMGRHD---DLWSLFYMLVEFVVGQLPW 232
Cdd:cd14174   146 DFDLGSgvKLNSACTPITTPELTTPC-GSAEYMAPEVVEvfTDEATFYDkrcDLWSLGVILYIMLSGYPPF 215
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
72-272 2.11e-04

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: 44.66  E-value: 2.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   72 SERKMESGK----DHVCRFIG--CGRNDRFN----YVVMQ-LQGRNLADLRrsQSRGTFTISTTLRLGRQILESIESIHS 140
Cdd:cd14012    45 LEKELESLKklrhPNLVSYLAfsIERRGRSDgwkvYLLTEyAPGGSLSELL--DSVGSVPLDTARRWTLQLLEALEYLHR 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  141 VGFLHRDIKPSNFAMGRFPSTCrKCYMLDFGLARQFTNSCGdvRPPRAVagFRGTVRYASINAHRNREMGRHDDLWSLFY 220
Cdd:cd14012   123 NGVVHKSLHAGNVLLDRDAGTG-IVKLTDYSLGKTLLDMCS--RGSLDE--FKQTYWLPPELAQGSKSPTRKTDVWDLGL 197
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530405409  221 MLVEFVVGQLPWrkikdkeqvgsikERYDHRLMLK---HLPPEFSIFLDHISSLD 272
Cdd:cd14012   198 LFLQMLFGLDVL-------------EKYTSPNPVLvslDLSASLQDFLSKCLSLD 239
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
97-232 2.19e-04

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 44.72  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQ-LQGRNLADLRRSQSRGTFTISTTLRlgrQILESIESIHSVGFLHRDIKPSNFAMGRFPSTcrkcYMLDFGLarq 175
Cdd:cd06654    93 WVVMEyLAGGSLTDVVTETCMDEGQIAAVCR---ECLQALEFLHSNQVIHRDIKSDNILLGMDGSV----KLTDFGF--- 162
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 530405409  176 ftnsCGDVRPPRAV-AGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 232
Cdd:cd06654   163 ----CAQITPEQSKrSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPY 216
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
135-247 2.36e-04

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 44.60  E-value: 2.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  135 IESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLDFGLARQFTNScgdvrppRAVAGFRGTVRYASINAHRNREMGRHDD 214
Cdd:cd05631   115 LEDLQRERIVYRDLKPENILL----DDRGHIRISDLGLAVQIPEG-------ETVRGRVGTVGYMAPEVINNEKYTFSPD 183
                          90       100       110
                  ....*....|....*....|....*....|...
gi 530405409  215 LWSLFYMLVEFVVGQLPWRKIKDKEQVGSIKER 247
Cdd:cd05631   184 WWGLGCLIYEMIQGQSPFRKRKERVKREEVDRR 216
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
129-246 2.41e-04

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: 44.15  E-value: 2.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  129 RQILESIESIHSVGFLHRDIKPSNFamgrFPSTCRKCYMLDFGLARQFTNscgdvrPPRAVAGFRGTVRYASINAHRNRE 208
Cdd:cd14189   108 KQIISGLKYLHLKGILHRDLKLGNF----FINENMELKVGDFGLAARLEP------PEQRKKTICGTPNYLAPEVLLRQG 177
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 530405409  209 MGRHDDLWSLFYMLVEFVVGQLPWRKIKDKEQVGSIKE 246
Cdd:cd14189   178 HGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQ 215
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
129-173 2.47e-04

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


Pssm-ID: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 44.74  E-value: 2.47e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 530405409  129 RQILESIESIHSVGFLHRDIKPSNFAmgrFPSTCRKCYMLDFGLA 173
Cdd:cd14013   127 RQILVALRKLHSTGIVHRDVKPQNII---VSEGDGQFKIIDLGAA 168
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
130-174 2.50e-04

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


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 44.73  E-value: 2.50e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 530405409  130 QILESIESIHSVGFLHRDIKPSNFAMGrfpSTCRkCYMLDFGLAR 174
Cdd:cd07853   111 QILRGLKYLHSAGILHRDIKPGNLLVN---SNCV-LKICDFGLAR 151
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
131-286 2.54e-04

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 44.34  E-value: 2.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  131 ILESIESIHS-VGFLHRDIKPSNFAMGRFPstcrKCYMLDFGLARQFTNSCGDVRPpravAGFRGTVRYASINAHRNreM 209
Cdd:cd06617   112 IVKALEYLHSkLSVIHRDVKPSNVLINRNG----QVKLCDFGISGYLVDSVAKTID----AGCKPYMAPERINPELN--Q 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  210 GRHD---DLWSLFYMLVEFVVGQLPWRKIKDK-EQVGSIKERYDHRLMLKHLPPEFSIFLDHISSLDYFTKPDY-QLLTS 284
Cdd:cd06617   182 KGYDvksDVWSLGITMIELATGRFPYDSWKTPfQQLKQVVEEPSPQLPAEKFSPEFQDFVNKCLKKNYKERPNYpELLQH 261

                  ..
gi 530405409  285 VF 286
Cdd:cd06617   262 PF 263
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
107-282 2.63e-04

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 44.17  E-value: 2.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  107 LADLRRSQsRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfpSTCRKcyMLDFGLAR-----QFTNSCG 181
Cdd:cd05112    86 LSDYLRTQ-RGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGE--NQVVK--VSDFGMTRfvlddQYTSSTG 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  182 DVRPpravagfrgtVRYASINAHRNREMGRHDDLWSLFYMLVE-FVVGQLPWRKIKDKEQVGSIKEryDHRLMLKHLPPE 260
Cdd:cd05112   161 TKFP----------VKWSSPEVFSFSRYSSKSDVWSFGVLMWEvFSEGKIPYENRSNSEVVEDINA--GFRLYKPRLAST 228
                         170       180
                  ....*....|....*....|....
gi 530405409  261 fSIF--LDHISSLDYFTKPDYQLL 282
Cdd:cd05112   229 -HVYeiMNHCWKERPEDRPSFSLL 251
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
97-232 2.69e-04

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 44.33  E-value: 2.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQ-LQGRNLADLRRSQSRGTFTISTTLRlgrQILESIESIHSVGFLHRDIKPSNFAMGRFPSTcrkcYMLDFGLarq 175
Cdd:cd06655    92 FVVMEyLAGGSLTDVVTETCMDEAQIAAVCR---ECLQALEFLHANQVIHRDIKSDNVLLGMDGSV----KLTDFGF--- 161
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 530405409  176 ftnsCGDVRPPRAV-AGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 232
Cdd:cd06655   162 ----CAQITPEQSKrSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY 215
BREX_PglW NF033442
BREX system serine/threonine kinase PglW; Members of this family are PglW, a predicted serine ...
99-174 2.86e-04

BREX system serine/threonine kinase PglW; Members of this family are PglW, a predicted serine/threonine kinase of the Pgl (phage growth limitation) system (now called BREX type 2) and the BREX type 3 system.


Pssm-ID: 468028 [Multi-domain]  Cd Length: 1387  Bit Score: 45.33  E-value: 2.86e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530405409   99 VMQLQGR-NLAD-LRRSqsrGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFPSTCRKCYMLDFGLAR 174
Cdd:NF033442  585 LLEYAGEqTLAErLRKE---GRLSLDLLERFGDDLLSAVVHLEGQGVWHRDIKPDNIGIRPRPSRTLHLVLFDFSLAG 659
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
92-241 2.86e-04

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


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 44.61  E-value: 2.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   92 NDRFNYVVMQLQGRNLAdLRRSQSRgTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAM---GRFPSTcrkcyml 168
Cdd:cd05595    67 HDRLCFVMEYANGGELF-FHLSRER-VFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLdkdGHIKIT------- 137
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530405409  169 DFGLARQFTNSCGDVRPpravagFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKiKDKEQV 241
Cdd:cd05595   138 DFGLCKEGITDGATMKT------FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN-QDHERL 203
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
119-241 3.04e-04

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 43.92  E-value: 3.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  119 FTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFamgrFPSTCRKCYMLDFGLARQFT--NSCGDVRPPravagfRGTV 196
Cdd:cd14062    86 FEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNI----FLHEDLTVKIGDFGLATVKTrwSGSQQFEQP------TGSI 155
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 530405409  197 RYASINAHRNREMGR---HDDLWSLFYMLVEFVVGQLPWRKIKDKEQV 241
Cdd:cd14062   156 LWMAPEVIRMQDENPysfQSDVYAFGIVLYELLTGQLPYSHINNRDQI 203
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
97-231 3.19e-04

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 44.27  E-value: 3.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQ-LQGRNLADLRRSQSRGTFTISTTLRlgrQILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLDFGLARQ 175
Cdd:cd06640    78 WIIMEyLGGGSALDLLRAGPFDEFQIATMLK---EILKGLDYLHSEKKIHRDIKAANVLL----SEQGDVKLADFGVAGQ 150
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530405409  176 FTnscgDVRPPRAVagFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLP 231
Cdd:cd06640   151 LT----DTQIKRNT--FVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPP 200
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
138-231 3.39e-04

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 44.35  E-value: 3.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  138 IHSVgfLHRDIKPSNFAMgrfpSTCRKCYMLDFGLARQFTNSCGDvrppravaGFRGTVRYASinahRNREMGRH----D 213
Cdd:cd06615   118 KHKI--MHRDVKPSNILV----NSRGEIKLCDFGVSGQLIDSMAN--------SFVGTRSYMS----PERLQGTHytvqS 179
                          90
                  ....*....|....*...
gi 530405409  214 DLWSLFYMLVEFVVGQLP 231
Cdd:cd06615   180 DIWSLGLSLVEMAIGRYP 197
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
129-185 3.60e-04

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 44.02  E-value: 3.60e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530405409  129 RQILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLDFGLARQFTNScgDVRP 185
Cdd:cd07864   123 KQLLEGLNYCHKKNFLHRDIKCSNILL----NNKGQIKLADFGLARLYNSE--ESRP 173
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
83-191 3.67e-04

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 43.63  E-value: 3.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   83 VCRFIG-CGRNDRFNYVVMQLQGRNLADLRRSQSRgTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNfAMGRFPST 161
Cdd:cd14065    50 ILRFIGvCVKDNKLNFITEYVNGGTLEELLKSMDE-QLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKN-CLVREANR 127
                          90       100       110
                  ....*....|....*....|....*....|...
gi 530405409  162 CRKCYMLDFGLARQ---FTNSCGDVRPPRAVAG 191
Cdd:cd14065   128 GRNAVVADFGLAREmpdEKTKKPDRKKRLTVVG 160
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
130-232 4.01e-04

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: 43.86  E-value: 4.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  130 QILESIESIHSVGFLHRDIKPSNFamgrFPSTCRKCYMLDFGLARQFTNSCgdvrppRAVAGFRGTVRYASinAHRNREM 209
Cdd:cd08228   114 QLCSAVEHMHSRRVMHRDIKPANV----FITATGVVKLGDLGLGRFFSSKT------TAAHSLVGTPYYMS--PERIHEN 181
                          90       100
                  ....*....|....*....|....*
gi 530405409  210 GRH--DDLWSLFYMLVEFVVGQLPW 232
Cdd:cd08228   182 GYNfkSDIWSLGCLLYEMAALQSPF 206
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
129-173 4.19e-04

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


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 44.07  E-value: 4.19e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 530405409  129 RQILESIESIHSVGFLHRDIKPSNFAMGRfpsTCRKCYMLDFGLA 173
Cdd:cd14132   119 YELLKALDYCHSKGIMHRDVKPHNIMIDH---EKRKLRLIDWGLA 160
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
122-223 4.29e-04

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


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 43.76  E-value: 4.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  122 STTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFpSTCRKCYMLDFGLARQFTNSCgDVRPpravagFRGTVRYASI 201
Cdd:cd14198   110 NDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSI-YPLGDIKIVDFGMSRKIGHAC-ELRE------IMGTPEYLAP 181
                          90       100
                  ....*....|....*....|....*
gi 530405409  202 NAHRNREMGRHDDLWS---LFYMLV 223
Cdd:cd14198   182 EILNYDPITTATDMWNigvIAYMLL 206
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
97-234 4.37e-04

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 43.50  E-value: 4.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQ-LQGRNLADL-RRSQSRGTF---TISTTLRlgrQILESIESIHSVGFLHRDIKPSNFAMGRFPSTcrkcYMLDFG 171
Cdd:cd06610    75 WLVMPlLSGGSLLDImKSSYPRGGLdeaIIATVLK---EVLKGLEYLHSNGQIHRDVKAGNILLGEDGSV----KIADFG 147
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530405409  172 L-ARQFTNSCgdvRPPRAVAGFRGTVRY-ASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRK 234
Cdd:cd06610   148 VsASLATGGD---RTRKVRKTFVGTPCWmAPEVMEQVRGYDFKADIWSFGITAIELATGAAPYSK 209
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
76-265 4.64e-04

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 43.62  E-value: 4.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   76 MESGKDHVCRFIGCGRNDRFNYVVMQL-QGRNLADLRRSQSRGTFTISTTLRlgrQILESIESIHSVGFLHRDIKPSNFA 154
Cdd:cd06917    57 KLGQPKNIIKYYGSYLKGPSLWIIMDYcEGGSIRTLMRAGPIAERYIAVIMR---EVLVALKFIHKDGIIHRDIKAANIL 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  155 MGRfPSTCRKCymlDFGLARQFTNSCGDvrppRAVagFRGTVRYASINAHRN-REMGRHDDLWSLFYMLVEFVVGQLPWR 233
Cdd:cd06917   134 VTN-TGNVKLC---DFGVAASLNQNSSK----RST--FVGTPYWMAPEVITEgKYYDTKADIWSLGITTYEMATGNPPYS 203
                         170       180       190
                  ....*....|....*....|....*....|..
gi 530405409  234 KIKDKEQVGSIKERYDHRLMLKHLPPEFSIFL 265
Cdd:cd06917   204 DVDALRAVMLIPKSKPPRLEGNGYSPLLKEFV 235
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
117-244 4.69e-04

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: 43.52  E-value: 4.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  117 GTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGrFPSTCRKCymlDFGLARQFTNSCGDVrpprAVAGFRGTV 196
Cdd:cd06629   103 GKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVD-LEGICKIS---DFGISKKSDDIYGNN----GATSMQGSV 174
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 530405409  197 RYASINAHRNREMGRHD--DLWSLFYMLVEFVVGQLPWrkiKDKEQVGSI 244
Cdd:cd06629   175 FWMAPEVIHSQGQGYSAkvDIWSLGCVVLEMLAGRRPW---SDDEAIAAM 221
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
97-248 4.90e-04

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 43.34  E-value: 4.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQ-LQGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLDFGLARQ 175
Cdd:cd05067    77 YIITEyMENGSLVDFLKTPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILV----SDTLSCKIADFGLARL 152
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530405409  176 FTNSCGDVRppravAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVV-GQLPWRKIKDKEQVGSIKERY 248
Cdd:cd05067   153 IEDNEYTAR-----EGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVThGRIPYPGMTNPEVIQNLERGY 221
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
130-262 4.96e-04

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 43.47  E-value: 4.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  130 QILESIESIHSVGFLHRDIKPSNFAMGRFPSTcrkcYMLDFGLARQftnscgdVRPPRAVAGFRGTVRYASINAHRNREM 209
Cdd:cd05630   110 EICCGLEDLHRERIVYRDLKPENILLDDHGHI----RISDLGLAVH-------VPEGQTIKGRVGTVGYMAPEVVKNERY 178
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530405409  210 GRHDDLWSLFYMLVEFVVGQLPWRKIKDKeqvgsIKERYDHRLmLKHLPPEFS 262
Cdd:cd05630   179 TFSPDWWALGCLLYEMIAGQSPFQQRKKK-----IKREEVERL-VKEVPEEYS 225
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
97-185 5.09e-04

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


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 43.51  E-value: 5.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQLQGRNLADLRrSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfpSTCRKcyMLDFGLARQF 176
Cdd:cd07865    95 YLVFEFCEHDLAGLL-SNKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITK--DGVLK--LADFGLARAF 169

                  ....*....
gi 530405409  177 TNSCGDVRP 185
Cdd:cd07865   170 SLAKNSQPN 178
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
97-232 5.25e-04

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 43.56  E-value: 5.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQ-LQGRNLADLRRSQSRGTFTISTTLRlgrQILESIESIHSVGFLHRDIKPSNFAMGRFPSTcrkcYMLDFGLarq 175
Cdd:cd06656    92 WVVMEyLAGGSLTDVVTETCMDEGQIAAVCR---ECLQALDFLHSNQVIHRDIKSDNILLGMDGSV----KLTDFGF--- 161
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 530405409  176 ftnsCGDVRPPRAV-AGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 232
Cdd:cd06656   162 ----CAQITPEQSKrSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY 215
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
130-174 5.36e-04

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


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 43.90  E-value: 5.36e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 530405409  130 QILESIESIHSVGFLHRDIKPSNFAMGrfpSTC--RKCymlDFGLAR 174
Cdd:cd07858   116 QLLRGLKYIHSANVLHRDLKPSNLLLN---ANCdlKIC---DFGLAR 156
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
97-180 5.55e-04

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: 43.22  E-value: 5.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQL-QGRNLADL--RRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSN-FAMGRFpstcrkcyML---D 169
Cdd:cd08215    75 CIVMEYaDGGDLAQKikKQKKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNiFLTKDG--------VVklgD 146
                          90
                  ....*....|.
gi 530405409  170 FGLARQFTNSC 180
Cdd:cd08215   147 FGISKVLESTT 157
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
97-232 5.60e-04

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 43.02  E-value: 5.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQL-QGRNLADlRRSQSRGT-FTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFamgrFPSTCRKCYML-DFGLA 173
Cdd:cd08225    75 FIVMEYcDGGDLMK-RINRQRGVlFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNI----FLSKNGMVAKLgDFGIA 149
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 530405409  174 RQFTNScgdVRPPRAVAgfrGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 232
Cdd:cd08225   150 RQLNDS---MELAYTCV---GTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPF 202
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
130-174 6.00e-04

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


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 43.74  E-value: 6.00e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 530405409  130 QILESIESIHSVGFLHRDIKPSNFAMGRfpsTCrKCYMLDFGLAR 174
Cdd:cd07879   125 QMLCGLKYIHSAGIIHRDLKPGNLAVNE---DC-ELKILDFGLAR 165
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
97-218 6.26e-04

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


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 43.17  E-value: 6.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQLQGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNF---AMGRFPSTcRKCymlDFGLA 173
Cdd:cd14082    78 FVVMEKLHGDMLEMILSSEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVllaSAEPFPQV-KLC---DFGFA 153
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 530405409  174 RQFtnscGDVRPPRAVAgfrGTVRYASINAHRNREMGRHDDLWSL 218
Cdd:cd14082   154 RII----GEKSFRRSVV---GTPAYLAPEVLRNKGYNRSLDMWSV 191
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
97-174 6.28e-04

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


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 43.33  E-value: 6.28e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530405409   97 YVVMQLQGRNLADLRRSQSRGTFTISTTLRlgrQILESIESIHSVGFLHRDIKPSNFAMGRfpsTCrKCYMLDFGLAR 174
Cdd:cd07856    86 YFVTELLGTDLHRLLTSRPLEKQFIQYFLY---QILRGLKYVHSAGVIHRDLKPSNILVNE---NC-DLKICDFGLAR 156
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
130-235 6.33e-04

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 43.10  E-value: 6.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  130 QILESIESIHS---VGFLHRDIKPSNFAM---GRFPSTCRKCYML-DFGLARQFTnscgdvRPPRAVAGfrGTVRYASIN 202
Cdd:cd14146   110 QIARGMLYLHEeavVPILHRDLKSSNILLlekIEHDDICNKTLKItDFGLAREWH------RTTKMSAA--GTYAWMAPE 181
                          90       100       110
                  ....*....|....*....|....*....|...
gi 530405409  203 AHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKI 235
Cdd:cd14146   182 VIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGI 214
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
129-274 6.37e-04

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: 43.08  E-value: 6.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  129 RQILESIESIHSVGFLHRDIKPSNFamgrFPSTCRKCYMLDFGLARQFtNSCGDVRppRAVAgfrGTVRYASINAHRNRE 208
Cdd:cd14188   108 RQIVSGLKYLHEQEILHRDLKLGNF----FINENMELKVGDFGLAARL-EPLEHRR--RTIC---GTPNYLSPEVLNKQG 177
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530405409  209 MGRHDDLWSLFYMLVEFVVGQLPWRKIKDKEQVGSIKE-RYDHRLML----KHL-------PPEFSIFLDHISSLDYF 274
Cdd:cd14188   178 HGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREaRYSLPSSLlapaKHLiasmlskNPEDRPSLDEIIRHDFF 255
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
97-259 6.62e-04

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 42.85  E-value: 6.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQLqGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGR-FpstcrKCYMLDFGLARQ 175
Cdd:cd14165    78 YIVMEL-GVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKdF-----NIKLTDFGFSKR 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  176 F-TNSCGDVRPPRAvagFRGTVRYAS---INAHRNREmgRHDDLWSLFYMLVEFVVGQLPWRKIKDKEQvgsIKERYDHR 251
Cdd:cd14165   152 ClRDENGRIVLSKT---FCGSAAYAApevLQGIPYDP--RIYDIWSLGVILYIMVCGSMPYDDSNVKKM---LKIQKEHR 223

                  ....*...
gi 530405409  252 LmlkHLPP 259
Cdd:cd14165   224 V---RFPR 228
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
129-176 6.70e-04

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 42.98  E-value: 6.70e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 530405409  129 RQILESIESIHSVGFLHRDIKPSNFAMGRfpSTCRKCYMLDFGLARQF 176
Cdd:cd14103    98 RQICEGVQYMHKQGILHLDLKPENILCVS--RTGNQIKIIDFGLARKY 143
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
130-245 6.93e-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: 42.71  E-value: 6.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  130 QILESIESIHSVGFLHRDIKPSNFamgrFPSTCRKCYMLDFGlarqFTNSCgdvRPPRAVAGFRGTVRYASINAHRNRE- 208
Cdd:cd14075   109 QIVSAVKHMHENNIIHRDLKAENV----FYASNNCVKVGDFG----FSTHA---KRGETLNTFCGSPPYAAPELFKDEHy 177
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 530405409  209 MGRHDDLWSLFYMLVEFVVGQLPWRkikdKEQVGSIK 245
Cdd:cd14075   178 IGIYVDIWALGVLLYFMVTGVMPFR----AETVAKLK 210
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
131-232 7.12e-04

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


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 43.47  E-value: 7.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  131 ILESIESIHSVGFLHRDIKPSNFAM---GRFPSTCRKCymlDFGLARQFTNSCGDVRPPRAVAGFrgtvryASINAHRNR 207
Cdd:cd14176   122 ITKTVEYLHAQGVVHRDLKPSNILYvdeSGNPESIRIC---DFGFAKQLRAENGLLMTPCYTANF------VAPEVLERQ 192
                          90       100
                  ....*....|....*....|....*
gi 530405409  208 EMGRHDDLWSLFYMLVEFVVGQLPW 232
Cdd:cd14176   193 GYDAACDIWSLGVLLYTMLTGYTPF 217
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
92-186 7.37e-04

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


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 43.17  E-value: 7.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   92 NDRFNYVVMQLQGRNLadLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFPSTC--RKCymlD 169
Cdd:cd14090    72 DERFYLVFEKMRGGPL--LSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVSpvKIC---D 146
                          90
                  ....*....|....*..
gi 530405409  170 FGLARQFTNSCGDVRPP 186
Cdd:cd14090   147 FDLGSGIKLSSTSMTPV 163
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
135-153 8.07e-04

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 42.99  E-value: 8.07e-04
                          10
                  ....*....|....*....
gi 530405409  135 IESIHSVGFLHRDIKPSNF 153
Cdd:cd05599   114 IESIHKLGYIHRDIKPDNL 132
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
82-231 8.30e-04

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 42.75  E-value: 8.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   82 HVCRFIGCGRNDRFNYVVMQ-LQGRNLADLRRSQSRGTFTISTTLRlgrQILESIESIHSVGFLHRDIKPSNFAMgrfpS 160
Cdd:cd06641    63 YVTKYYGSYLKDTKLWIIMEyLGGGSALDLLEPGPLDETQIATILR---EILKGLDYLHSEKKIHRDIKAANVLL----S 135
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530405409  161 TCRKCYMLDFGLARQFTnscgDVRPPRavAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLP 231
Cdd:cd06641   136 EHGEVKLADFGVAGQLT----DTQIKR--N*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPP 200
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
34-237 8.38e-04

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 42.82  E-value: 8.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   34 VKWKPPLGTGCLCSCSTISvycnewgRRAAGYPECWNPSERKMESGKD----------------HVCRFIGCGRNDRFNY 97
Cdd:cd14077    17 VKLAKHIRTGEKCAIKIIP-------RASNAGLKKEREKRLEKEISRDirtireaalssllnhpHICRLRDFLRTPNHYY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   98 VVMQ-LQGRNLAD-------LRRSQSRgtftisttlRLGRQILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLD 169
Cdd:cd14077    90 MLFEyVDGGQLLDyiishgkLKEKQAR---------KFARQIASALDYLHRNSIVHRDLKIENILI----SKSGNIKIID 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  170 FGLARQFtnscgdvRPPRAVAGFRGTVRYAS---INAhrNREMGRHDDLWSLFYMLVEFVVGQLPW---------RKIKD 237
Cdd:cd14077   157 FGLSNLY-------DPRRLLRTFCGSLYFAApelLQA--QPYTGPEVDVWSFGVVLYVLVCGKVPFddenmpalhAKIKK 227
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
97-174 8.42e-04

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


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 43.15  E-value: 8.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQLQGRNLAD---LRRSQSRGTFTISttlrlgrQILESIESIHSVGFLHRDIKPSNFAMgrfPSTCrKCYMLDFGLA 173
Cdd:cd07874    98 YLVMELMDANLCQviqMELDHERMSYLLY-------QMLCGIKHLHSAGIIHRDLKPSNIVV---KSDC-TLKILDFGLA 166

                  .
gi 530405409  174 R 174
Cdd:cd07874   167 R 167
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
130-231 8.78e-04

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: 42.62  E-value: 8.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  130 QILESIESIHSVGFLHRDIKPSNFAMGRfPSTCRKCymlDFGLARqfTNSCGDVrpprAVAGFRGTVRYASINAHRNREM 209
Cdd:cd14002   107 QLVSALHYLHSNRIIHRDMKPQNILIGK-GGVVKLC---DFGFAR--AMSCNTL----VLTSIKGTPLYMAPELVQEQPY 176
                          90       100
                  ....*....|....*....|..
gi 530405409  210 GRHDDLWSLFYMLVEFVVGQLP 231
Cdd:cd14002   177 DHTADLWSLGCILYELFVGQPP 198
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
97-174 8.79e-04

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


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 43.11  E-value: 8.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQLQGRNLAD---LRRSQSRGTFTISttlrlgrQILESIESIHSVGFLHRDIKPSNFAMgrfPSTCrKCYMLDFGLA 173
Cdd:cd07875   105 YIVMELMDANLCQviqMELDHERMSYLLY-------QMLCGIKHLHSAGIIHRDLKPSNIVV---KSDC-TLKILDFGLA 173

                  .
gi 530405409  174 R 174
Cdd:cd07875   174 R 174
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
93-303 8.80e-04

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


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 43.16  E-value: 8.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   93 DRFN--YVVMQLQGRNLADLRRS-QSRGTFTISTTLRlgrQILESIESIHSVGFLHRDIKPSNFAMGrfpSTCrKCYMLD 169
Cdd:cd07857    76 GNFNelYLYEELMEADLHQIIRSgQPLTDAHFQSFIY---QILCGLKYIHSANVLHRDLKPGNLLVN---ADC-ELKICD 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  170 FGLARQFTNScgdvrpPRAVAGFrgTVRYASINAHR-------NREMGRHDDLWSLFYMLVEFvVGQLPWRKIKDkeqvg 242
Cdd:cd07857   149 FGLARGFSEN------PGENAGF--MTEYVATRWYRapeimlsFQSYTKAIDVWSVGCILAEL-LGRKPVFKGKD----- 214
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530405409  243 sikerYDHRL--MLKHL--PPEFSifLDHISSldyftkPDYQlltsvfdNSIKTFGVIESDPFDW 303
Cdd:cd07857   215 -----YVDQLnqILQVLgtPDEET--LSRIGS------PKAQ-------NYIRSLPNIPKKPFES 259
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
130-178 9.26e-04

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


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 43.04  E-value: 9.26e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 530405409  130 QILESIESIHSVGFLHRDIKPSN-FAMGRFPStCRKCYMLDFGLARQFTN 178
Cdd:cd07842   116 QILNGIHYLHSNWVLHRDLKPANiLVMGEGPE-RGVVKIGDLGLARLFNA 164
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
97-173 9.65e-04

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 42.31  E-value: 9.65e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530405409   97 YVVMQL-QGRNLADLRRSQSRgtFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFPSTCRKCYMLDFGLA 173
Cdd:cd14095    74 YLVMELvKGGDLFDAITSSTK--FTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEDGSKSLKLADFGLA 149
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
93-250 1.03e-03

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


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 42.62  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   93 DRFNYVVMQLQGRNLadLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFPstcrKCYMLDFGL 172
Cdd:cd05620    69 EHLFFVMEFLNGGDL--MFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDG----HIKIADFGM 142
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530405409  173 ARQftNSCGDVRppraVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKDKEQVGSIKERYDH 250
Cdd:cd05620   143 CKE--NVFGDNR----ASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPH 214
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
72-231 1.05e-03

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


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 42.21  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   72 SERK--MESGKDHVCRFIGCGRNDRFNYVVMQL-QGRNLADLRRSqsRGTFTISTTLRLGRQILESIESIHSVGFLHRDI 148
Cdd:cd05572    42 SEKEilEECNSPFIVKLYRTFKDKKYLYMLMEYcLGGELWTILRD--RGLFDEYTARFYTACVVLAFEYLHSRGIIYRDL 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  149 KPSNFAM---GRFpstcrkcYMLDFGLARQftnscgdVRPPRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEF 225
Cdd:cd05572   120 KPENLLLdsnGYV-------KLVDFGFAKK-------LGSGRKTWTFCGTPEYVAPEIILNKGYDFSVDYWSLGILLYEL 185

                  ....*.
gi 530405409  226 VVGQLP 231
Cdd:cd05572   186 LTGRPP 191
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
126-248 1.14e-03

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 42.47  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  126 RLGRQILESIESIHSVGFLHRDIKPSNFAMGRFpstcRKCYMLDFGLARQFTNSCGDVRPPRAvagfrGTVRYASINAHR 205
Cdd:cd14076   110 RLFAQLISGVAYLHKKGVVHRDLKLENLLLDKN----RNLVITDFGFANTFDHFNGDLMSTSC-----GSPCYAAPELVV 180
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 530405409  206 NREM--GRHDDLWSLFYMLVEFVVGQLPWRKIKDKEQVGSIKERY 248
Cdd:cd14076   181 SDSMyaGRKADIWSCGVILYAMLAGYLPFDDDPHNPNGDNVPRLY 225
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
97-245 1.16e-03

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 42.60  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQLQGRNLadLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLDFGLARQf 176
Cdd:cd05619    83 FVMEYLNGGDL--MFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILL----DKDGHIKIADFGMCKE- 155
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530405409  177 tNSCGDVRppraVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKDKEQVGSIK 245
Cdd:cd05619   156 -NMLGDAK----TSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIR 219
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
97-248 1.17e-03

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


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 42.32  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQ-LQGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLDFGLARQ 175
Cdd:cd05073    81 YIITEfMAKGSLLDFLKSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILV----SASLVCKIADFGLARV 156
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530405409  176 FTNSCGDVRppravAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVV-GQLPWRKIKDKEQVGSIKERY 248
Cdd:cd05073   157 IEDNEYTAR-----EGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTyGRIPYPGMSNPEVIRALERGY 225
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
97-260 1.25e-03

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


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 42.05  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQL--QGRNLADLRrsQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGrfpSTCrKCYMLDFGLAR 174
Cdd:cd05059    75 FIVTEYmaNGCLLNYLR--ERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVG---EQN-VVKVSDFGLAR 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  175 -----QFTNSCGDVRPpravagfrgtVRYASINAHRNREMGRHDDLWSLFYMLVE-FVVGQLPWRKIKDKEQVGSIKERY 248
Cdd:cd05059   149 yvlddEYTSSVGTKFP----------VKWSPPEVFMYSKFSSKSDVWSFGVLMWEvFSEGKMPYERFSNSEVVEHISQGY 218
                         170
                  ....*....|..
gi 530405409  249 dhRLMLKHLPPE 260
Cdd:cd05059   219 --RLYRPHLAPT 228
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
130-177 1.29e-03

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


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 42.34  E-value: 1.29e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 530405409  130 QILESIESIHSVGFLHRDIKPSNFAMGRFPSTCRKCYMLDFGLARQFT 177
Cdd:cd13981   114 ELLKVVEALHEVGIIHGDIKPDNFLLRLEICADWPGEGENGWLSKGLK 161
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
122-231 1.35e-03

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 42.28  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  122 STTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfPSTCRKCymlDFGLARQF----------TNSCGDVRPPRAVAG 191
Cdd:cd14010    94 SSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDG-NGTLKLS---DFGLARREgeilkelfgqFSDEGNVNKVSKKQA 169
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 530405409  192 FRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLP 231
Cdd:cd14010   170 KRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPP 209
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
97-183 1.46e-03

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 41.79  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQLQGRnlAD-LRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLDFGLARQ 175
Cdd:cd14080    78 FIFMEYAEH--GDlLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILL----DSNNNVKLSDFGFARL 151

                  ....*...
gi 530405409  176 FTNSCGDV 183
Cdd:cd14080   152 CPDDDGDV 159
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
144-231 1.48e-03

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


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 42.35  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  144 LHRDIKPSNFAMgrfpSTCRKCYMLDFGLARQFTNSCGDvrppravaGFRGTVRYASINAHRNREMGRHDDLWSLFYMLV 223
Cdd:cd06650   126 MHRDVKPSNILV----NSRGEIKLCDFGVSGQLIDSMAN--------SFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLV 193

                  ....*...
gi 530405409  224 EFVVGQLP 231
Cdd:cd06650   194 EMAVGRYP 201
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
72-231 1.49e-03

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


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 42.18  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   72 SERKMESGKDH--VCRFIGCGRNDRFNYVVMQ-LQGRNLAD-LRRSqsrGTFTISTTLRLGRQILESIESIHSVGFLHRD 147
Cdd:cd05580    50 NEKRILSEVRHpfIVNLLGSFQDDRNLYMVMEyVPGGELFSlLRRS---GRFPNDVAKFYAAEVVLALEYLHSLDIVYRD 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  148 IKPSNFAMGRFPSTcrkcYMLDFGLARQFTNS----CgdvrppravagfrGTVRYASINAHRNREMGRHDDLWSLFYMLV 223
Cdd:cd05580   127 LKPENLLLDSDGHI----KITDFGFAKRVKDRtytlC-------------GTPEYLAPEIILSKGHGKAVDWWALGILIY 189

                  ....*...
gi 530405409  224 EFVVGQLP 231
Cdd:cd05580   190 EMLAGYPP 197
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
97-280 1.52e-03

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


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 41.98  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQLQGR-NLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfpstCRKCYMLDFGLARQ 175
Cdd:cd05071    79 YIVTEYMSKgSLLDFLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGE----NLVCKVADFGLARL 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  176 FTNSCGDVRppravAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVV-GQLPWRKIKDKEQVGSIKERYD----- 249
Cdd:cd05071   155 IEDNEYTAR-----QGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTkGRVPYPGMVNREVLDQVERGYRmpcpp 229
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 530405409  250 ------HRLMLK--HLPPEFSIFLDHISSL--DYF--TKPDYQ 280
Cdd:cd05071   230 ecpeslHDLMCQcwRKEPEERPTFEYLQAFleDYFtsTEPQYQ 272
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
130-177 1.66e-03

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 41.92  E-value: 1.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 530405409  130 QILESIESIHSVGFLHRDIKPSNFAMGRfpstcRKCYML-DFGLARQFT 177
Cdd:cd07866   123 QLLEGINYLHENHILHRDIKAANILIDN-----QGILKIaDFGLARPYD 166
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
77-171 1.68e-03

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


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 42.15  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   77 ESGKDHVCRFIgcgrnDRFNY-----VVMQLQGRNLADLRRSQS-RGtFTISTTLRLGRQILESIESIHSVGFLHRDIKP 150
Cdd:cd14210    71 PDDKHNIVRYK-----DSFIFrghlcIVFELLSINLYELLKSNNfQG-LSLSLIRKFAKQILQALQFLHKLNIIHCDLKP 144
                          90       100
                  ....*....|....*....|.
gi 530405409  151 SNFAMGRFPSTCRKcyMLDFG 171
Cdd:cd14210   145 ENILLKQPSKSSIK--VIDFG 163
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
82-179 1.73e-03

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


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 41.85  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   82 HVCRFIGCGRNDRFNYVVMQ-LQGRNLADLRRSQSRGTFTISTTLRlgrQILESIESIHSVGFLHRDIKPSNFAMgrfpS 160
Cdd:cd06609    60 YITKYYGSFLKGSKLWIIMEyCGGGSVLDLLKPGPLDETYIAFILR---EVLLGLEYLHSEGKIHRDIKAANILL----S 132
                          90
                  ....*....|....*....
gi 530405409  161 TCRKCYMLDFGLARQFTNS 179
Cdd:cd06609   133 EEGDVKLADFGVSGQLTST 151
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
114-259 1.80e-03

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 41.77  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  114 QSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGrfpSTCrKCYMLDFGLAR-----QFTNSCGDVRPpra 188
Cdd:cd05114    92 QRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVN---DTG-VVKVSDFGMTRyvlddQYTSSSGAKFP--- 164
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530405409  189 vagfrgtVRYASINAHRNREMGRHDDLWSLFYMLVE-FVVGQLPWRKIKDKEQVGSIKEryDHRLMLKHLPP 259
Cdd:cd05114   165 -------VKWSPPEVFNYSKFSSKSDVWSFGVLMWEvFTEGKMPFESKSNYEVVEMVSR--GHRLYRPKLAS 227
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
82-174 1.87e-03

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


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 41.72  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   82 HVCRFIGCGRND-RFNYVVMQLQGRNLADLRRSQSRgTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFamgrFPS 160
Cdd:cd14154    51 NVLKFIGVLYKDkKLNLITEYIPGGTLKDVLKDMAR-PLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNC----LVR 125
                          90
                  ....*....|....
gi 530405409  161 TCRKCYMLDFGLAR 174
Cdd:cd14154   126 EDKTVVVADFGLAR 139
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
93-241 1.92e-03

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 41.99  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   93 DRFNYVVMQLQGRNLAdLRRSQSRgTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFPSTcrkcYMLDFGL 172
Cdd:cd05593    88 DRLCFVMEYVNGGELF-FHLSRER-VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHI----KITDFGL 161
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530405409  173 ARQFTNSCGDVRPpravagFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKiKDKEQV 241
Cdd:cd05593   162 CKEGITDAATMKT------FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN-QDHEKL 223
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
97-174 1.93e-03

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


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 42.07  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQLQGrnlADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFamgrFPSTcrKCYML---DFGLA 173
Cdd:cd07854    92 YIVQEYME---TDLANVLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANV----FINT--EDLVLkigDFGLA 162

                  .
gi 530405409  174 R 174
Cdd:cd07854   163 R 163
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
97-232 2.00e-03

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 41.51  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQL-QGRNLADLRRSQsrGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFpstcrKCYMLDFGLARQ 175
Cdd:cd14163    77 YLVMELaEDGDVFDCVLHG--GPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGF-----TLKLTDFGFAKQ 149
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530405409  176 FTNSCGDVRppravAGFRGTVRYASINA-----HRNREmgrhDDLWSLFYMLVEFVVGQLPW 232
Cdd:cd14163   150 LPKGGRELS-----QTFCGSTAYAAPEVlqgvpHDSRK----GDIWSMGVVLYVMLCAQLPF 202
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
97-173 2.06e-03

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


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 41.56  E-value: 2.06e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530405409   97 YVVMQL-QGRNLADLRRSQSRGTFTISTTLRLgrQILESIESIHSVGFLHRDIKPSNFAMGRFPSTCRKCYMLDFGLA 173
Cdd:cd14184    75 YLVMELvKGGDLFDAITSSTKYTERDASAMVY--NLASALKYLHGLCIVHRDIKPENLLVCEYPDGTKSLKLGDFGLA 150
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
119-241 2.11e-03

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


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 41.56  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  119 FTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFamgrFPSTCRKCYMLDFGLARQFTNSCGDvrppRAVAGFRGTVRY 198
Cdd:cd14149   105 FQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNI----FLHEGLTVKIGDFGLATVKSRWSGS----QQVEQPTGSILW 176
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 530405409  199 AS---INAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKDKEQV 241
Cdd:cd14149   177 MApevIRMQDNNPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQI 222
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
129-232 2.14e-03

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


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 41.49  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  129 RQILESIESIHSVGFLHRDIKPSNFAMGRFPSTcrkcYMLDFGLARQFTNSCGDVRPPRAVAGFRGTvryASINAHRNRE 208
Cdd:cd14199   133 QDLIKGIEYLHYQKIIHRDVKPSNLLVGEDGHI----KIADFGVSNEFEGSDALLTNTVGTPAFMAP---ETLSETRKIF 205
                          90       100
                  ....*....|....*....|....
gi 530405409  209 MGRHDDLWSLFYMLVEFVVGQLPW 232
Cdd:cd14199   206 SGKALDVWAMGVTLYCFVFGQCPF 229
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
131-231 2.25e-03

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


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 41.64  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  131 ILESIESIHSVGFLHRDIKPSNFAMgrfpstCRK--CYMLDFGLARQFTNScgdvrppraVAG-FRGTVRYASINAHRNR 207
Cdd:cd06621   114 VLKGLSYLHSRKIIHRDIKPSNILL------TRKgqVKLCDFGVSGELVNS---------LAGtFTGTSYYMAPERIQGG 178
                          90       100
                  ....*....|....*....|....
gi 530405409  208 EMGRHDDLWSLFYMLVEFVVGQLP 231
Cdd:cd06621   179 PYSITSDVWSLGLTLLEVAQNRFP 202
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
129-177 2.28e-03

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: 41.10  E-value: 2.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 530405409  129 RQILESIESIHSVGFLHRDIKPSNFAMGRFPSTCRKcyMLDFGLARQFT 177
Cdd:cd14006    96 RQLLEGLQYLHNHHILHLDLKPENILLADRPSPQIK--IIDFGLARKLN 142
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
99-152 2.34e-03

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


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 41.49  E-value: 2.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530405409   99 VMQLQGRNLADLRRSQsRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSN 152
Cdd:cd07831    78 VFELMDMNLYELIKGR-KRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPEN 130
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
125-233 2.44e-03

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 41.71  E-value: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  125 LRLGRQILESIESIHSVGFLHRDIKPSNFaMGRFPSTCRKCYML-DFGLARQFTNScgdvrppRAVAGFRGTVRY----- 198
Cdd:cd13988    99 LIVLRDVVAGMNHLRENGIVHRDIKPGNI-MRVIGEDGQSVYKLtDFGAARELEDD-------EQFVSLYGTEEYlhpdm 170
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 530405409  199 ---ASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWR 233
Cdd:cd13988   171 yerAVLRKDHQKKYGATVDLWSIGVTFYHAATGSLPFR 208
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
94-232 2.51e-03

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


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 41.54  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   94 RFNYVVMQL-QGRNLAD--LR------RSQSRGTFTISTTlrlgrqilesIESIHSVGFLHRDIKPSNFAMGRFPSTCRK 164
Cdd:cd14177    71 RYVYLVTELmKGGELLDriLRqkffseREASAVLYTITKT----------VDYLHCQGVVHRDLKPSNILYMDDSANADS 140
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530405409  165 CYMLDFGLARQFTNSCGDVRPPRAVAGFrgtvryASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 232
Cdd:cd14177   141 IRICDFGFAKQLRGENGLLLTPCYTANF------VAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPF 202
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
98-262 2.63e-03

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 41.78  E-value: 2.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   98 VVMQLQGRNLADLR-----RSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMgrfpstCRK--CYMLDF 170
Cdd:PTZ00283  114 IALVLDYANAGDLRqeiksRAKTNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILL------CSNglVKLGDF 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  171 GLARQFTNSC-GDVRppravAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPW-----RKIKDKEQVGsi 244
Cdd:PTZ00283  188 GFSKMYAATVsDDVG-----RTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFdgenmEEVMHKTLAG-- 260
                         170
                  ....*....|....*...
gi 530405409  245 keRYDhrlmlkHLPPEFS 262
Cdd:PTZ00283  261 --RYD------PLPPSIS 270
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
129-245 2.64e-03

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 41.03  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  129 RQILESIESIHSVGFLHRDIKPSNFAMGRFPSTCRKcyMLDFGLARQFTnscgdvrPPRAVAGFRGTVRYASINAHRNRE 208
Cdd:cd14114   107 RQVCEGLCHMHENNIVHLDIKPENIMCTTKRSNEVK--LIDFGLATHLD-------PKESVKVTTGTAEFAAPEIVEREP 177
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 530405409  209 MGRHDDLWS---LFYMLVEfvvGQLPWRKIKDKEQVGSIK 245
Cdd:cd14114   178 VGFYTDMWAvgvLSYVLLS---GLSPFAGENDDETLRNVK 214
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
130-232 2.92e-03

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 40.93  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  130 QILESIESIHSVGFLHRDIKPSNF---AMGRFPSTcrkcymlDFGLARQftnscGDVRppRAVAGFRGTVRY---ASINA 203
Cdd:cd05611   105 EVVLGVEDLHQRGIIHRDIKPENLlidQTGHLKLT-------DFGLSRN-----GLEK--RHNKKFVGTPDYlapETILG 170
                          90       100
                  ....*....|....*....|....*....
gi 530405409  204 HRNREMGrhdDLWSLFYMLVEFVVGQLPW 232
Cdd:cd05611   171 VGDDKMS---DWWSLGCVIFEFLFGYPPF 196
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
88-152 2.93e-03

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


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 41.33  E-value: 2.93e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530405409   88 GCGRNDRFNYVVMQLQGRNLADLRRSQSRGTFTISTTL-RL-GRQILESIESIHSVGFLHRDIKPSN 152
Cdd:cd14137    70 GEKKDEVYLNLVMEYMPETLYRVIRHYSKNKQTIPIIYvKLySYQLFRGLAYLHSLGICHRDIKPQN 136
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
130-176 3.32e-03

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 40.96  E-value: 3.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 530405409  130 QILESIESIHSVGFLHRDIKPSNFAMGRFPSTCRkcyMLDFGLARQF 176
Cdd:PLN00009  110 QILRGIAYCHSHRVLHRDLKPQNLLIDRRTNALK---LADFGLARAF 153
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
98-193 3.36e-03

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


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 40.71  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   98 VVMQLQGRNLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAM-GRFPSTCRKCYMLDFGLArQF 176
Cdd:cd14068    62 LVMELAPKGSLDALLQQDNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLfTLYPNCAIIAKIADYGIA-QY 140
                          90
                  ....*....|....*..
gi 530405409  177 TNSCGdVRPPRAVAGFR 193
Cdd:cd14068   141 CCRMG-IKTSEGTPGFR 156
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
114-291 3.36e-03

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 41.00  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  114 QSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFPstcRKCYMLDFGLARQF-TNSCGDvrppravagf 192
Cdd:PHA03390  101 KKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAK---DRIYLCDYGLCKIIgTPSCYD---------- 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  193 rGTVRYAS---INAHRNremGRHDDLWSLFYMLVEFVVGQLPWRKIKDKE-QVGSIKERYDHRL-MLKHLPPEFSIFLDH 267
Cdd:PHA03390  168 -GTLDYFSpekIKGHNY---DVSFDWWAVGVLTYELLTGKHPFKEDEDEElDLESLLKRQQKKLpFIKNVSKNANDFVQS 243
                         170       180
                  ....*....|....*....|....
gi 530405409  268 ISSLDYftkpDYQLltSVFDNSIK 291
Cdd:PHA03390  244 MLKYNI----NYRL--TNYNEIIK 261
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
98-176 3.65e-03

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 40.67  E-value: 3.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   98 VVMQLQGRNLADlRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSN-FAMGRfpsTCRKCYMLDFGLARQF 176
Cdd:cd14193    79 VMEYVDGGELFD-RIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENiLCVSR---EANQVKIIDFGLARRY 154
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
129-233 3.66e-03

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 40.68  E-value: 3.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  129 RQILESIESIHSVGFLHRDIKPSNFAMGRfPSTCRKcyMLDFGlarqftnsCGDVRPPRAVAGFRGTVRYASINAHR-NR 207
Cdd:cd14005   114 RQVVEAVRHCHQRGVLHRDIKDENLLINL-RTGEVK--LIDFG--------CGALLKDSVYTDFDGTRVYSPPEWIRhGR 182
                          90       100
                  ....*....|....*....|....*.
gi 530405409  208 EMGRHDDLWSLFYMLVEFVVGQLPWR 233
Cdd:cd14005   183 YHGRPATVWSLGILLYDMLCGDIPFE 208
Pkinase pfam00069
Protein kinase domain;
81-266 3.67e-03

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 40.31  E-value: 3.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409    81 DHVCRFIGCGRNDRFNYVVMQL-QGRNLAD-LRRsqsRGTFTISTTLRLGRQILESIESihsvgflhrdikpsnfamgrf 158
Cdd:pfam00069   58 PNIVRLYDAFEDKDNLYLVLEYvEGGSLFDlLSE---KGAFSEREAKFIMKQILEGLES--------------------- 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   159 pstcrkcymldfglaRQFTNScgdvrppravagFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKDK 238
Cdd:pfam00069  114 ---------------GSSLTT------------FVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGN 166
                          170       180
                   ....*....|....*....|....*....
gi 530405409   239 EQVGS-IKERYDHRLMLKHLPPEFSIFLD 266
Cdd:pfam00069  167 EIYELiIDQPYAFPELPSNLSEEAKDLLK 195
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
142-303 3.73e-03

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 40.82  E-value: 3.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  142 GFLHRDIKPSNFAMGRfpSTCRKcyMLDFGLARQFTNScgdvrppRAVAGFRGTVRYAS---INAHRNREMGRHDDLWSL 218
Cdd:cd06618   135 GVIHRDVKPSNILLDE--SGNVK--LCDFGISGRLVDS-------KAKTRSAGCAAYMAperIDPPDNPKYDIRADVWSL 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  219 FYMLVEFVVGQLPWRKIKDKEQVGSI-----KERYDHRlmlKHLPPEFSIFLDHISSLDYFTKPDY-QLLTSVFdnsIKT 292
Cdd:cd06618   204 GISLVELATGQFPYRNCKTEFEVLTKilneePPSLPPN---EGFSPDFCSFVDLCLTKDHRYRPKYrELLQHPF---IRR 277
                         170
                  ....*....|.
gi 530405409  293 FGVIESDPFDW 303
Cdd:cd06618   278 YETAEVDVASW 288
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
130-255 3.89e-03

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


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 40.57  E-value: 3.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  130 QILESIESIHSVGFLHRDIKPSNFAMGrfpSTCRKCYMLDFGLARQFTNS-------CGDVRPpravagfrGTVRYASIN 202
Cdd:cd13991   106 QALEGLEYLHSRKILHGDVKADNVLLS---SDGSDAFLCDFGHAECLDPDglgkslfTGDYIP--------GTETHMAPE 174
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530405409  203 AHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIkdkeqvgsikerYDHRLMLK 255
Cdd:cd13991   175 VVLGKPCDAKVDVWSSCCMMLHMLNGCHPWTQY------------YSGPLCLK 215
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
119-184 4.02e-03

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 40.80  E-value: 4.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530405409  119 FTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAM-GRFPstCRKCYMLDFGLARQFTNSCgDVR 184
Cdd:cd14106   105 LTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLtSEFP--LGDIKLCDFGISRVIGEGE-EIR 168
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
110-260 4.02e-03

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


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 40.63  E-value: 4.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  110 LRRSQSRgtFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfpSTCRKcyMLDFGLAR-----QFTNSCGDVR 184
Cdd:cd05113    90 LREMRKR--FQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVND--QGVVK--VSDFGLSRyvlddEYTSSVGSKF 163
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530405409  185 PpravagfrgtVRYASINAHRNREMGRHDDLWSLFYMLVE-FVVGQLPWRKIKDKEQVGSIKEryDHRLMLKHLPPE 260
Cdd:cd05113   164 P----------VRWSPPEVLMYSKFSSKSDVWAFGVLMWEvYSLGKMPYERFTNSETVEHVSQ--GLRLYRPHLASE 228
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
112-177 4.05e-03

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


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 40.79  E-value: 4.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530405409  112 RSQSRG--TFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFA-MGRFPSTCRKcyMLDFGLARQFT 177
Cdd:cd14170    89 RIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLyTSKRPNAILK--LTDFGFAKETT 155
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
144-234 5.08e-03

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 40.43  E-value: 5.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  144 LHRDIKPSNFAMGRfpstcRKCYML-DFGLARQFTNSCGDVRPpravAGFRGTVRYASINAHRNREmgRHD---DLWSLF 219
Cdd:cd06616   132 IHRDVKPSNILLDR-----NGNIKLcDFGISGQLVDSIAKTRD----AGCRPYMAPERIDPSASRD--GYDvrsDVWSLG 200
                          90
                  ....*....|....*
gi 530405409  220 YMLVEFVVGQLPWRK 234
Cdd:cd06616   201 ITLYEVATGKFPYPK 215
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
78-173 5.35e-03

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


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 40.70  E-value: 5.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   78 SGKDHVCRFIgcgrnDRFNY-----VVMQLQGRNLADL-RRSQSRGtFTISTTLRLGRQILESIESIHSVGFLHRDIKPS 151
Cdd:cd14212    59 EDKHHIVRLL-----DHFMHhghlcIVFELLGVNLYELlKQNQFRG-LSLQLIRKFLQQLLDALSVLKDARIIHCDLKPE 132
                          90       100
                  ....*....|....*....|..
gi 530405409  152 NFAMGRFPSTCRKcyMLDFGLA 173
Cdd:cd14212   133 NILLVNLDSPEIK--LIDFGSA 152
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
114-272 5.63e-03

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 40.24  E-value: 5.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  114 QSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLDFGLARQFTNSCGDVRPPRAVAGfR 193
Cdd:cd05065    98 QNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILV----NSNLVCKVSDFGLSRFLEDDTSDPTYTSSLGG-K 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  194 GTVRYASINAHRNREMGRHDDLWSlfYMLVEFVV---GQLPWRKIKDKEQVGSIKERYD-----------HRLML----- 254
Cdd:cd05065   173 IPIRWTAPEAIAYRKFTSASDVWS--YGIVMWEVmsyGERPYWDMSNQDVINAIEQDYRlpppmdcptalHQLMLdcwqk 250
                         170
                  ....*....|....*....
gi 530405409  255 -KHLPPEFSiflDHISSLD 272
Cdd:cd05065   251 dRNLRPKFG---QIVNTLD 266
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
130-248 6.03e-03

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


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 40.38  E-value: 6.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  130 QILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLDFGLARQFTNScGDVRPPRAVagfrGTVRYASINAHRNREM 209
Cdd:cd05623   181 EMVLAIDSVHQLHYVHRDIKPDNILM----DMNGHIRLADFGSCLKLMED-GTVQSSVAV----GTPDYISPEILQAMED 251
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 530405409  210 GRHD-----DLWSLFYMLVEFVVGQLPWRKIKDKEQVGSI---KERY 248
Cdd:cd05623   252 GKGKygpecDWWSLGVCMYEMLYGETPFYAESLVETYGKImnhKERF 298
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
129-271 6.04e-03

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 40.12  E-value: 6.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  129 RQILESIESIHSVGFLHRDIKPSNFAMGrfPSTCRKCYML-DFGLARqftnscgDVRPPRAVAGFRGTVRYASINAHRNR 207
Cdd:cd13989   109 SDISSAISYLHENRIIHRDLKPENIVLQ--QGGGRVIYKLiDLGYAK-------ELDQGSLCTSFVGTLQYLAPELFESK 179
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530405409  208 EMGRHDDLWSLFYMLVEFVVGQLP---------W-RKIKDKEQvGSIKERYDHRLMLK---HLPPEfsiflDHISSL 271
Cdd:cd13989   180 KYTCTVDYWSFGTLAFECITGYRPflpnwqpvqWhGKVKQKKP-EHICAYEDLTGEVKfssELPSP-----NHLSSI 250
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
130-262 6.10e-03

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


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 40.20  E-value: 6.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  130 QILESIESIHSVGFLHRDIKPSNFAMGRFPStcrkCYMLDFGLARQFTNScgdvRPPRAVAgfrGTVRYASINAHRNREM 209
Cdd:cd05577   103 EIICGLEHLHNRFIVYRDLKPENILLDDHGH----VRISDLGLAVEFKGG----KKIKGRV---GTHGYMAPEVLQKEVA 171
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530405409  210 GRHD-DLWSLFYMLVEFVVGQLPWRKIKDKeqvgsiKERYDHRLMLKHLPPEFS 262
Cdd:cd05577   172 YDFSvDWFALGCMLYEMIAGRSPFRQRKEK------VDKEELKRRTLEMAVEYP 219
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
93-179 6.25e-03

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 39.50  E-value: 6.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409    93 DRFNYV-VMQ-LQGRNLADLRRSqsrgtftisTTLRLGRQILESIESIHSVGFLHRDIKPSNFamgRFPStcRKCYMLDF 170
Cdd:TIGR03724   68 DPDNKTiVMEyIEGKPLKDVIEE---------NGDELAREIGRLVGKLHKAGIVHGDLTTSNI---IVRD--DKVYLIDF 133

                   ....*....
gi 530405409   171 GLARqFTNS 179
Cdd:TIGR03724  134 GLGK-YSDE 141
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
130-247 6.54e-03

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 39.89  E-value: 6.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  130 QILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLDFGLARQFTnscgDVRPPRAVAGFRGtvrYASINAHRNREM 209
Cdd:cd05607   112 QITCGILHLHSLKIVYRDMKPENVLL----DDNGNCRLSDLGLAVEVK----EGKPITQRAGTNG---YMAPEILKEESY 180
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 530405409  210 GRHDDLWSLFYMLVEFVVGQLPWRKIKDKEQVGSIKER 247
Cdd:cd05607   181 SYPVDWFAMGCSIYEMVAGRTPFRDHKEKVSKEELKRR 218
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
129-179 6.61e-03

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 39.87  E-value: 6.61e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 530405409  129 RQILESIESIHSVGFLHRDIKPSNFAMgrFPSTCRKCYMLDFGLARQFTNS 179
Cdd:cd14107   105 QQVLEGIGYLHGMNILHLDIKPDNILM--VSPTREDIKICDFGFAQEITPS 153
PRK14879 PRK14879
Kae1-associated kinase Bud32;
99-174 7.32e-03

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 39.50  E-value: 7.32e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530405409   99 VMQ-LQGRNLADLRRSQSRGTFTISttLRLGRQIlesiESIHSVGFLHRDIKPSNFAMgrfpsTCRKCYMLDFGLAR 174
Cdd:PRK14879   77 VMEyIEGEPLKDLINSNGMEELELS--REIGRLV----GKLHSAGIIHGDLTTSNMIL-----SGGKIYLIDFGLAE 142
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
117-254 7.69e-03

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 39.85  E-value: 7.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  117 GTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMgrfpSTCRKCYMLDFGLARQFTNScgdvrpPRAVAGFRG-- 194
Cdd:cd05066   101 GQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILV----NSNLVCKVSDFGLSRVLEDD------PEAAYTTRGgk 170
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530405409  195 -TVRYASINAHRNREMGRHDDLWSLFYMLVEFV-VGQLPWRKIKDKEQVGSIKERYD-----------HRLML 254
Cdd:cd05066   171 iPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMsYGERPYWEMSNQDVIKAIEEGYRlpapmdcpaalHQLML 243
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
93-174 7.89e-03

bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 40.26  E-value: 7.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   93 DRFNYV-VMQ-LQGRNLADLrrsqsrgtftISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRfpstcRKCYMLDF 170
Cdd:PRK09605  407 DPEEKTiVMEyIGGKDLKDV----------LEGNPELVRKVGEIVAKLHKAGIVHGDLTTSNFIVRD-----DRLYLIDF 471

                  ....
gi 530405409  171 GLAR 174
Cdd:PRK09605  472 GLGK 475
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
98-177 7.89e-03

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


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 39.50  E-value: 7.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   98 VVMQLQGRNLadLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGrfPSTCRKCYMLDFGLARQFT 177
Cdd:cd14108    75 IVTELCHEEL--LERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMA--DQKTDQVRICDFGNAQELT 150
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
129-218 8.27e-03

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 39.84  E-value: 8.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  129 RQILESIESIHSVGFLHRDIKPSNFAMgrfpsTCRKCY---MLDFGLARQFTnscgdvrPPRAVAGFRGTVRYASINAHR 205
Cdd:cd14104   104 RQVCEALEFLHSKNIGHFDIRPENIIY-----CTRRGSyikIIEFGQSRQLK-------PGDKFRLQYTSAEFYAPEVHQ 171
                          90
                  ....*....|...
gi 530405409  206 NREMGRHDDLWSL 218
Cdd:cd14104   172 HESVSTATDMWSL 184
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
97-232 8.31e-03

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 39.46  E-value: 8.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   97 YVVMQLQGRNLadLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGrfpSTCRKCYMLDFGLARQF 176
Cdd:cd14164    77 YIVMEAAATDL--LQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLS---ADDRKIKIADFGFARFV 151
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530405409  177 TNscgdvrPPRAVAGFRGTVRYASinahrnREMGRHD-------DLWSLFYMLVEFVVGQLPW 232
Cdd:cd14164   152 ED------YPELSTTFCGSRAYTP------PEVILGTpydpkkyDVWSLGVVLYVMVTGTMPF 202
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
130-178 8.97e-03

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


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 39.76  E-value: 8.97e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 530405409  130 QILESIESIHSVGFLHRDIKPSNFAMGrfpSTCrKCYMLDFGLARQFTN 178
Cdd:cd07859   111 QLLRALKYIHTANVFHRDLKPKNILAN---ADC-KLKICDFGLARVAFN 155
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
69-184 9.49e-03

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


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 39.29  E-value: 9.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   69 WNPSER---KME-------SGKDHVCRFIGCGRNDRFNYVVMQLQGR-NLADLRRSQSRGT-FTISTTLRLGRQILESIE 136
Cdd:cd13997    38 RGPKERaraLREveahaalGQHPNIVRYYSSWEEGGHLYIQMELCENgSLQDALEELSPISkLSEAEVWDLLLQVALGLA 117
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 530405409  137 SIHSVGFLHRDIKPSNFamgrFPSTCRKCYMLDFGLARQFTNScGDVR 184
Cdd:cd13997   118 FIHSKGIVHLDIKPDNI----FISNKGTCKIGDFGLATRLETS-GDVE 160
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
82-232 9.75e-03

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 39.66  E-value: 9.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409   82 HVCRFIGCGRNDRFNYVVMQ-LQGRNLADLRRSQSRGTFTISTTLRlgrQILESIESIHSVGFLHRDIKPSNFAMgrfpS 160
Cdd:cd06642    63 YITRYYGSYLKGTKLWIIMEyLGGGSALDLLKPGPLEETYIATILR---EILKGLDYLHSERKIHRDIKAANVLL----S 135
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530405409  161 TCRKCYMLDFGLARQFTnscgDVRPPRAVagFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPW 232
Cdd:cd06642   136 EQGDVKLADFGVAGQLT----DTQIKRNT--FVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPN 201
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
129-223 9.76e-03

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


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 39.52  E-value: 9.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530405409  129 RQILESIESIHSVGFLHRDIKPSNFAMgrFPSTCRKCYMLDFGLARQFtnscgdvRPPRAVAGFRGTVRYASINAHRNRE 208
Cdd:cd14190   109 RQICEGIQFMHQMRVLHLDLKPENILC--VNRTGHQVKIIDFGLARRY-------NPREKLKVNFGTPEFLSPEVVNYDQ 179
                          90
                  ....*....|....*...
gi 530405409  209 MGRHDDLWSL---FYMLV 223
Cdd:cd14190   180 VSFPTDMWSMgviTYMLL 197
 
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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