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Conserved domains on  [gi|767912019|ref|XP_011542316|]
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RAC-gamma serine/threonine-protein kinase isoform X4 [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 ...
40-249 3.98e-157

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 cd05593:

Pssm-ID: 451246 [Multi-domain]  Cd Length: 348  Bit Score: 439.90  E-value: 3.98e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd05593  139 RDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 120 DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSE 199
Cdd:cd05593  219 DHEKLFELILMEDIKFPRTLSADAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFTGVNWQDVYDKKLVPPFKPQVTSE 298
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767912019 200 TDTRYFDEEFTAQTITITPPEKYDEDGMDCMDNERRPHFPQFSYSASGRE 249
Cdd:cd05593  299 TDTRYFDEEFTAQTITITPPEKYDEDGMDCMDNERRPHFPQFSYSASGRE 348
 
Name Accession Description Interval E-value
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
40-249 3.98e-157

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: 439.90  E-value: 3.98e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd05593  139 RDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 120 DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSE 199
Cdd:cd05593  219 DHEKLFELILMEDIKFPRTLSADAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFTGVNWQDVYDKKLVPPFKPQVTSE 298
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767912019 200 TDTRYFDEEFTAQTITITPPEKYDEDGMDCMDNERRPHFPQFSYSASGRE 249
Cdd:cd05593  299 TDTRYFDEEFTAQTITITPPEKYDEDGMDCMDNERRPHFPQFSYSASGRE 348
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
45-206 5.54e-56

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 181.94  E-value: 5.54e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKEgITDAATmkTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL 124
Cdd:PTZ00263 147 ENLLLDNKGHVKVTDFGFAKK-VPDRTF--TLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRI 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 125 FELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRY 204
Cdd:PTZ00263 224 YEKILAGRLKFPNWFDGRARDLVKGLLQTDHTKRLGTLKGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSN 303

                 ..
gi 767912019 205 FD 206
Cdd:PTZ00263 304 FE 305
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
42-175 9.78e-54

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 173.87  E-value: 9.78e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019    42 ISLENLMLDKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH 121
Cdd:smart00220 123 LKPENILLDEDGHVKLADFGLARQ-LDPGEKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQ 201
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 767912019   122 E-KLFELILMEDIKFPR---TLSSDAKSLLSGLLIKDPNKRLGggpddAKEIMRHSFF 175
Cdd:smart00220 202 LlELFKKIGKPKPPFPPpewDISPEAKDLIRKLLVKDPEKRLT-----AEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
42-175 6.77e-53

Protein kinase domain;


Pssm-ID: 425449 [Multi-domain]  Cd Length: 254  Bit Score: 171.64  E-value: 6.77e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019   42 ISLENLMLDKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH 121
Cdd:pfam00069 124 LKPENILIDEDGNLKITDFGLARQ-LNSGSSLTTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGING 202
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767912019  122 EKLFELILMEDIKFPR---TLSSDAKSLLSGLLIKDPNKRLGggpddAKEIMRHSFF 175
Cdd:pfam00069 203 NEIYELIIDQPYAFPElpsNLSEEAKDLLKKLLKKDPSKRLT-----ATEALQHPWF 254
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
42-246 1.93e-22

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 94.42  E-value: 1.93e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  42 ISLENLMLDKDGH-IKITDFGLCKE------GITDAATMKTFCGTPEYLAPEVLEDN---DYGRAVDWWGLGVVMYEMMC 111
Cdd:COG0515  127 IKPENILLDRDGRvVKLIDFGLAKLlpdpgsTSSIPALPSTSVGTPGYMAPEVLLGLslaYASSSSDIWSLGITLYELLT 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 112 GRLPFYNQDHEKLFELIL-------------MEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGV 178
Cdd:COG0515  207 GLPPFEGEKNSSATSQTLkiilelptpslasPLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKES 286
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912019 179 NWQD-------VYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEKYDEDGMDCMDNERRPHFPQFSYSAS 246
Cdd:COG0515  287 DLSDllkpddsAPLRLSLPPSLEALISSLNSLAISGSDLKLDDSNFSKELAPNGVSSSPHNSSSLLLSTASSKRS 361
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
45-116 2.40e-10

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 59.81  E-value: 2.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCK----EGITDAATMktfCGTPEYLAPEVLEdndyGRAV----DWWGLGVVMYEMMCGRLPF 116
Cdd:NF033483 136 QNILITKDGRVKVTDFGIARalssTTMTQTNSV---LGTVHYLSPEQAR----GGTVdarsDIYSLGIVLYEMLTGRPPF 208
 
Name Accession Description Interval E-value
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
40-249 3.98e-157

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: 439.90  E-value: 3.98e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd05593  139 RDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 120 DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSE 199
Cdd:cd05593  219 DHEKLFELILMEDIKFPRTLSADAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFTGVNWQDVYDKKLVPPFKPQVTSE 298
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767912019 200 TDTRYFDEEFTAQTITITPPEKYDEDGMDCMDNERRPHFPQFSYSASGRE 249
Cdd:cd05593  299 TDTRYFDEEFTAQTITITPPEKYDEDGMDCMDNERRPHFPQFSYSASGRE 348
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
40-246 6.57e-153

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


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 428.31  E-value: 6.57e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd05571  119 RDLKLENLLLDKDGHIKITDFGLCKEEISYGATTKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNR 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 120 DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSE 199
Cdd:cd05571  199 DHEVLFELILMEEVRFPSTLSPEAKSLLAGLLKKDPKKRLGGGPRDAKEIMEHPFFASINWDDLYQKKIPPPFKPQVTSE 278
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767912019 200 TDTRYFDEEFTAQTITITPPekyDEDGMDCMDNERRPHFPQFSYSAS 246
Cdd:cd05571  279 TDTRYFDEEFTAESVELTPP---DRGDLLGLEEEERPHFEQFSYSAS 322
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
40-246 1.86e-151

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: 424.80  E-value: 1.86e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd05595  119 RDIKLENLMLDKDGHIKITDFGLCKEGITDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 120 DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSE 199
Cdd:cd05595  199 DHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLGGGPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSE 278
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767912019 200 TDTRYFDEEFTAQTITITPPEKYdeDGMDCMDNERRPHFPQFSYSAS 246
Cdd:cd05595  279 VDTRYFDDEFTAQSITITPPDRY--DSLDLLESDQRTHFPQFSYSAS 323
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
40-247 2.01e-135

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 385.15  E-value: 2.01e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd05594  150 RDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 229
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 120 DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSE 199
Cdd:cd05594  230 DHEKLFELILMEEIRFPRTLSPEAKSLLSGLLKKDPKQRLGGGPDDAKEIMQHKFFAGIVWQDVYEKKLVPPFKPQVTSE 309
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 767912019 200 TDTRYFDEEFTAQTITITPPEKydEDGMDCMDNERRPHFPQFSYSASG 247
Cdd:cd05594  310 TDTRYFDEEFTAQMITITPPDQ--DDSMETVDNERRPHFPQFSYSASA 355
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
44-243 1.02e-94

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


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 280.64  E-value: 1.02e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  44 LENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEK 123
Cdd:cd05570  124 LDNVLLDAEGHIKIADFGMCKEGIWGGNTTSTFCGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDE 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 124 LFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTR 203
Cdd:cd05570  204 LFEAILNDEVLYPRWLSREAVSILKGLLTKDPARRLGCGPKGEADIKAHPFFRNIDWDKLEKKEVEPPFKPKVKSPRDTS 283
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 767912019 204 YFDEEFTAQTITITPPEKYDEDGMDCMDnerrphFPQFSY 243
Cdd:cd05570  284 NFDPEFTSESPRLTPVDSDLLTNIDQEE------FRGFSY 317
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
45-243 1.35e-83

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 252.24  E-value: 1.35e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL 124
Cdd:cd05575  125 ENILLDSQGHVVLTDFGLCKEGIEPSDTTSTFCGTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEM 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 125 FELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGpDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRY 204
Cdd:cd05575  205 YDNILHKPLRLRTNVSPSARDLLEGLLQKDRTKRLGSG-NDFLEIKNHSFFRPINWDDLEAKKIPPPFNPNVSGPLDLRN 283
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767912019 205 FDEEFTAQTITITPPEKYDEDGMDCMDNERRPHFPQFSY 243
Cdd:cd05575  284 IDPEFTREPVPASVGKSADSVAVSASVQEADNAFDGFSY 322
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
40-245 9.08e-83

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 250.30  E-value: 9.08e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd05589  125 RDLKLDNLLLDTEGYVKIADFGLCKEGMGFGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGD 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 120 DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSE 199
Cdd:cd05589  205 DEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRKNPERRLGASERDAEDVKKQPFFRNIDWEALLARKIKPPFVPTIKSP 284
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767912019 200 TDTRYFDEEFTAQTITITPPEkydedgmdcmdnERRP-------HFPQFSYSA 245
Cdd:cd05589  285 EDVSNFDEEFTSEKPVLTPPK------------EPRPlteeeqaLFKDFDYVA 325
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
40-243 8.19e-76

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 232.28  E-value: 8.19e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd05592  120 RDLKLDNVLLDREGHIKIADFGMCKENIYGENKASTFCGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGE 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 120 DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSE 199
Cdd:cd05592  200 DEDELFWSICNDTPHYPRWLTKEAASCLSLLLERNPEKRLGVPECPAGDIRDHPFFKTIDWDKLERREIDPPFKPKVKSA 279
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 767912019 200 TDTRYFDEEFTAQTITITPPekyDEDGMDCMDNERrphFPQFSY 243
Cdd:cd05592  280 NDVSNFDPDFTMEKPVLTPV---DKKLLASMDQEQ---FKGFSF 317
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
45-220 2.91e-74

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


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 228.44  E-value: 2.91e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL 124
Cdd:cd05584  129 ENILLDAQGHVKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKT 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 125 FELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRY 204
Cdd:cd05584  209 IDKILKGKLNLPPYLTNEARDLLKKLLKRNVSSRLGSGPGDAEEIKAHPFFRHINWDDLLAKKVEPPFKPLLQSEEDVSQ 288
                        170
                 ....*....|....*.
gi 767912019 205 FDEEFTAQTITITPPE 220
Cdd:cd05584  289 FDSKFTKQTPVDSPDD 304
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
40-243 6.67e-73

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 224.96  E-value: 6.67e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd05587  121 RDLKLDNVMLDAEGHIKIADFGMCKEGIFGGKTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGE 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 120 DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSE 199
Cdd:cd05587  201 DEDELFQSIMEHNVSYPKSLSKEAVSICKGLLTKHPAKRLGCGPTGERDIKEHPFFRRIDWEKLERREIQPPFKPKIKSP 280
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 767912019 200 TDTRYFDEEFTAQTITITPPEKydedgmDCMDNERRPHFPQFSY 243
Cdd:cd05587  281 RDAENFDKEFTKEPPVLTPTDK------LVIMNIDQSEFEGFSF 318
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
44-175 2.53e-72

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: 221.24  E-value: 2.53e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  44 LENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEK 123
Cdd:cd05123  121 PENILLDSDGHIKLTDFGLAKELSSDGDRTYTFCGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKE 200
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767912019 124 LFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPddAKEIMRHSFF 175
Cdd:cd05123  201 IYEKILKSPLKFPEYVSPEAKSLISGLLQKDPTKRLGSGG--AEEIKAHPFF 250
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
40-243 2.66e-67

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 211.01  E-value: 2.66e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd05616  125 RDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGE 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 120 DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSE 199
Cdd:cd05616  205 DEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKACGR 284
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 767912019 200 tDTRYFDEEFTAQTITITPPEKydedgmDCMDNERRPHFPQFSY 243
Cdd:cd05616  285 -NAENFDRFFTRHPPVLTPPDQ------EVIRNIDQSEFEGFSF 321
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
40-243 3.19e-66

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


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 208.11  E-value: 3.19e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd05591  120 RDLKLDNILLDAEGHCKLADFGMCKEGILNGKTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEAD 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 120 DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLG--GGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVT 197
Cdd:cd05591  200 NEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPAKRLGcvASQGGEDAIRQHPFFREIDWEALEQRKVKPPFKPKIK 279
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767912019 198 SETDTRYFDEEFTAQTITITPpekYDEDGMDCMDNErrpHFPQFSY 243
Cdd:cd05591  280 TKRDANNFDQDFTKEEPVLTP---VDPAVIKQINQE---EFRGFSF 319
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
45-206 7.19e-65

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: 203.58  E-value: 7.19e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKEgITDAAtmKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL 124
Cdd:cd05580  130 ENLLLDSDGHIKITDFGFAKR-VKDRT--YTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKI 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 125 FELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRY 204
Cdd:cd05580  207 YEKILEGKIRFPSFFDPDAKDLIKRLLVVDLTKRLGNLKNGVEDIKNHPWFAGIDWDALLQRKIPAPYVPKVRGPGDTSN 286

                 ..
gi 767912019 205 FD 206
Cdd:cd05580  287 FD 288
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
45-218 1.83e-64

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


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 203.40  E-value: 1.83e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL 124
Cdd:cd05582  126 ENILLDEDGHIKLTDFGLSKESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKET 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 125 FELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRY 204
Cdd:cd05582  206 MTMILKAKLGMPQFLSPEAQSLLRALFKRNPANRLGAGPDGVEEIKRHPFFATIDWNKLYRKEIKPPFKPAVSRPDDTFY 285
                        170
                 ....*....|....
gi 767912019 205 FDEEFTAQTITITP 218
Cdd:cd05582  286 FDPEFTSRTPKDSP 299
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
40-245 2.02e-64

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 203.60  E-value: 2.02e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd05590  120 RDLKLDNVLLDHEGHCKLADFGMCKEGIFNGKTTSTFCGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAE 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 120 DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKE-IMRHSFFSGVNWQDVYDKKLVPPFKPQVTS 198
Cdd:cd05590  200 NEDDLFEAILNDEVVYPTWLSQDAVDILKAFMTKNPTMRLGSLTLGGEEaILRHPFFKELDWEKLNRRQIEPPFRPRIKS 279
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767912019 199 ETDTRYFDEEFTAQTITITPPekydEDGMDCMDNERrpHFPQFSYSA 245
Cdd:cd05590  280 REDVSNFDPDFIKEDPVLTPI----EESLLPMINQD--EFRNFSYTA 320
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
40-218 4.73e-64

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 202.51  E-value: 4.73e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd05603  120 RDLKPENILLDCQGHVVLTDFGLCKEGMEPEETTSTFCGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSR 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 120 DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPdDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSE 199
Cdd:cd05603  200 DVSQMYDNILHKPLHLPGGKTVAACDLLQGLLHKDQRRRLGAKA-DFLEIKNHVFFSPINWDDLYHKRITPPYNPNVAGP 278
                        170       180
                 ....*....|....*....|...
gi 767912019 200 TDTRYFDEEFTAQ----TITITP 218
Cdd:cd05603  279 ADLRHFDPEFTQEavphSVGRTP 301
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
40-218 3.88e-63

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


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 200.34  E-value: 3.88e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF--- 116
Cdd:cd05588  120 RDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFdiv 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 117 -----YNQDHEK-LFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDA-KEIMRHSFFSGVNWQDVYDKKLV 189
Cdd:cd05588  200 gssdnPDQNTEDyLFQVILEKPIRIPRSLSVKAASVLKGFLNKNPAERLGCHPQTGfADIQSHPFFRTIDWEQLEQKQVT 279
                        170       180
                 ....*....|....*....|....*....
gi 767912019 190 PPFKPQVTSETDTRYFDEEFTAQTITITP 218
Cdd:cd05588  280 PPYKPRIESERDLENFDPQFTNEPVQLTP 308
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
40-214 4.25e-62

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 197.49  E-value: 4.25e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd05604  121 RDLKPENILLDSQGHIVLTDFGLCKEGISNSDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCR 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 120 DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGpDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSE 199
Cdd:cd05604  201 DTAEMYENILHKPLVLRPGISLTAWSILEELLEKDRQLRLGAK-EDFLEIKNHPFFESINWTDLVQKKIPPPFNPNVNGP 279
                        170
                 ....*....|....*
gi 767912019 200 TDTRYFDEEFTAQTI 214
Cdd:cd05604  280 DDISNFDAEFTEEMV 294
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
40-212 7.43e-61

Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 193.94  E-value: 7.43e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd05585  118 RDLKPENILLDYTGHIALCDFGLCKLNMKDDDKTNTFCGTPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDE 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 120 DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGpdDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSE 199
Cdd:cd05585  198 NTNEMYRKILQEPLRFPDGFDRDAKDLLIGLLNRDPTKRLGYN--GAQEIKNHPFFDQIDWKRLLMKKIQPPFKPAVENA 275
                        170
                 ....*....|...
gi 767912019 200 TDTRYFDEEFTAQ 212
Cdd:cd05585  276 IDTSNFDEEFTRE 288
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
40-241 4.95e-60

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 192.90  E-value: 4.95e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd05615  135 RDLKLDNVMLDSEGHIKIADFGMCKEHMVEGVTTRTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGE 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 120 DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSE 199
Cdd:cd05615  215 DEDELFQSIMEHNVSYPKSLSKEAVSICKGLMTKHPAKRLGCGPEGERDIREHAFFRRIDWDKLENREIQPPFKPKVCGK 294
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 767912019 200 tDTRYFDEEFTAQTITITPPEKYDEDGMDCMDNERRPHF-PQF 241
Cdd:cd05615  295 -GAENFDKFFTRGQPVLTPPDQLVIANIDQADFEGFSYVnPQF 336
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
40-244 6.39e-60

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 192.54  E-value: 6.39e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd05602  132 RDLKPENILLDSQGHIVLTDFGLCKENIEPNGTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSR 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 120 DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLgGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSE 199
Cdd:cd05602  212 NTAEMYDNILNKPLQLKPNITNSARHLLEGLLQKDRTKRL-GAKDDFTEIKNHIFFSPINWDDLINKKITPPFNPNVSGP 290
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767912019 200 TDTRYFDEEFTAQTITITPPEKYDEDGMDCMDNERRPHFPQFSYS 244
Cdd:cd05602  291 NDLRHFDPEFTDEPVPNSIGQSPDSILVTASIKEAAEAFLGFSYA 335
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
45-210 1.91e-59

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


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 190.86  E-value: 1.91e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEK 123
Cdd:cd05586  125 ENILLDANGHIALCDFGLSKADLTDNKTTNTFCGTTEYLAPEVLlDEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQ 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 124 LFELILMEDIKFPR-TLSSDAKSLLSGLLIKDPNKRLGGgPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDT 202
Cdd:cd05586  205 MYRNIAFGKVRFPKdVLSDEGRSFVKGLLNRNPKHRLGA-HDDAVELKEHPFFADIDWDLLSKKKITPPFKPIVDSDTDV 283

                 ....*...
gi 767912019 203 RYFDEEFT 210
Cdd:cd05586  284 SNFDPEFT 291
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
40-228 3.96e-58

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: 187.44  E-value: 3.96e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd05619  130 RDLKLDNILLDKDGHIKIADFGMCKENMLGDAKTSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQ 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 120 DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDdakeIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSE 199
Cdd:cd05619  210 DEEELFQSIRMDNPFYPRWLEKEAKDILVKLFVREPERRLGVRGD----IRQHPFFREINWEALEEREIEPPFKPKVKSP 285
                        170       180
                 ....*....|....*....|....*....
gi 767912019 200 TDTRYFDEEFTAQTITITPPEKYDEDGMD 228
Cdd:cd05619  286 FDCSNFDKEFLNEKPRLSFADRALINSMD 314
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
40-243 1.29e-57

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 187.15  E-value: 1.29e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF--- 116
Cdd:cd05617  140 RDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFdii 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 117 -YNQD---HEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDA-KEIMRHSFFSGVNWQDVYDKKLVPP 191
Cdd:cd05617  220 tDNPDmntEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNKDPKERLGCQPQTGfSDIKSHTFFRSIDWDLLEKKQVTPP 299
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767912019 192 FKPQVTSETDTRYFDEEFTAQTITITPPekyDEDGMDCMDnerRPHFPQFSY 243
Cdd:cd05617  300 FKPQITDDYGLENFDTQFTSEPVQLTPD---DEDVIKRID---QSEFEGFEY 345
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
40-219 8.15e-57

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


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 184.35  E-value: 8.15e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGIT-DAATMKTFCGTPEYLAPEVLEDND-YGRAVDWWGLGVVMYEMMCGRLPFY 117
Cdd:cd05614  129 RDIKLENILLDSEGHVVLTDFGLSKEFLTeEKERTYSFCGTIEYMAPEIIRGKSgHGKAVDWWSLGILMFELLTGASPFT 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 118 ----NQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFK 193
Cdd:cd05614  209 legeKNTQSEVSRRILKCDPPFPSFIGPVARDLLQKLLCKDPKKRLGAGPQGAQEIKEHPFFKGLDWEALALRKVNPPFR 288
                        170       180
                 ....*....|....*....|....*.
gi 767912019 194 PQVTSETDTRYFDEEFTAQTITITPP 219
Cdd:cd05614  289 PSIRSELDVGNFAEEFTNLEPVYSPA 314
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
40-228 2.00e-56

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: 182.84  E-value: 2.00e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd05620  120 RDLKLDNVMLDRDGHIKIADFGMCKENVFGDNRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGD 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 120 DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGggpdDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSE 199
Cdd:cd05620  200 DEDELFESIRVDTPHYPRWITKESKDILEKLFERDPTRRLG----VVGNIRGHPFFKTINWTALEKRELDPPFKPKVKSP 275
                        170       180
                 ....*....|....*....|....*....
gi 767912019 200 TDTRYFDEEFTAQTITITPPEKYDEDGMD 228
Cdd:cd05620  276 SDYSNFDREFLSEKPRLSYSDKNLIDSMD 304
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
45-206 5.54e-56

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 181.94  E-value: 5.54e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKEgITDAATmkTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL 124
Cdd:PTZ00263 147 ENLLLDNKGHVKVTDFGFAKK-VPDRTF--TLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRI 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 125 FELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRY 204
Cdd:PTZ00263 224 YEKILAGRLKFPNWFDGRARDLVKGLLQTDHTKRLGTLKGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSN 303

                 ..
gi 767912019 205 FD 206
Cdd:PTZ00263 304 FE 305
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
45-206 3.14e-54

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: 176.09  E-value: 3.14e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKEGITDAATMktfCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL 124
Cdd:cd05612  130 ENILLDKEGHIKLTDFGFAKKLRDRTWTL---CGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGI 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 125 FELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRY 204
Cdd:cd05612  207 YEKILAGKLEFPRHLDLYAKDLIKKLLVVDRTRRLGNMKNGADDVKNHRWFKSVDWDDVPQRKLKPPIVPKVSHDGDTSN 286

                 ..
gi 767912019 205 FD 206
Cdd:cd05612  287 FD 288
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
40-243 8.39e-54

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 177.53  E-value: 8.39e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF--- 116
Cdd:cd05618  145 RDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFdiv 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 117 -----YNQDHEK-LFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDA-KEIMRHSFFSGVNWQDVYDKKLV 189
Cdd:cd05618  225 gssdnPDQNTEDyLFQVILEKQIRIPRSLSVKAASVLKSFLNKDPKERLGCHPQTGfADIQGHPFFRNVDWDLMEQKQVV 304
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767912019 190 PPFKPQVTSETDTRYFDEEFTAQTITITPPekyDEDGMDCMDnerRPHFPQFSY 243
Cdd:cd05618  305 PPFKPNISGEFGLDNFDSQFTNEPVQLTPD---DDDIVRKID---QSEFEGFEY 352
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
42-175 9.78e-54

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 173.87  E-value: 9.78e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019    42 ISLENLMLDKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH 121
Cdd:smart00220 123 LKPENILLDEDGHVKLADFGLARQ-LDPGEKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQ 201
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 767912019   122 E-KLFELILMEDIKFPR---TLSSDAKSLLSGLLIKDPNKRLGggpddAKEIMRHSFF 175
Cdd:smart00220 202 LlELFKKIGKPKPPFPPpewDISPEAKDLIRKLLVKDPEKRLT-----AEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
42-175 6.77e-53

Protein kinase domain;


Pssm-ID: 425449 [Multi-domain]  Cd Length: 254  Bit Score: 171.64  E-value: 6.77e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019   42 ISLENLMLDKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH 121
Cdd:pfam00069 124 LKPENILIDEDGNLKITDFGLARQ-LNSGSSLTTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGING 202
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767912019  122 EKLFELILMEDIKFPR---TLSSDAKSLLSGLLIKDPNKRLGggpddAKEIMRHSFF 175
Cdd:pfam00069 203 NEIYELIIDQPYAFPElpsNLSEEAKDLLKKLLKKDPSKRLT-----ATEALQHPWF 254
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
40-194 3.18e-52

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


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 170.95  E-value: 3.18e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMK-TFCGTPEYLAPEVLEDNDYG--RAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd05613  129 RDIKLENILLDSSGHVVLTDFGLSKEFLLDENERAySFCGTIEYMAPEIVRGGDSGhdKAVDWWSLGVLMYELLTGASPF 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 117 Y----NQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPF 192
Cdd:cd05613  209 TvdgeKNSQAEISRRILKSEPPYPQEMSALAKDIIQRLLMKDPKKRLGCGPNGADEIKKHPFFQKINWDDLAAKKVPAPF 288

                 ..
gi 767912019 193 KP 194
Cdd:cd05613  289 KP 290
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
45-207 1.68e-50

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 166.43  E-value: 1.68e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKEgiTDAATMkTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL 124
Cdd:cd14209  130 ENLLIDQQGYIKVTDFGFAKR--VKGRTW-TLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQI 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 125 FELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRY 204
Cdd:cd14209  207 YEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKLKGPGDTSN 286

                 ...
gi 767912019 205 FDE 207
Cdd:cd14209  287 FDD 289
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
42-172 3.82e-50

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: 164.61  E-value: 3.82e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  42 ISLENLMLDKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQD 120
Cdd:cd14003  125 LKLENILLDKNGNLKIIDFGLSNE-FRGGSLLKTFCGTPAYAAPEVLLGRKYdGPKADVWSLGVILYAMLTGYLPFDDDN 203
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767912019 121 HEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGggpddAKEIMRH 172
Cdd:cd14003  204 DSKLFRKILKGKYPIPSHLSPDARDLIRRMLVVDPSKRIT-----IEEILNH 250
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
40-178 7.46e-48

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


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 159.10  E-value: 7.46e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDA-ATMKTFCGTPEYLAPEVLEDNDYG--RAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd05583  123 RDIKLENILLDSEGHVVLTDFGLSKEFLPGEnDRAYSFCGTIEYMAPEVVRGGSDGhdKAVDWWSLGVLTYELLTGASPF 202
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912019 117 YNQD----HEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGV 178
Cdd:cd05583  203 TVDGernsQSEISKRILKSHPPIPKTFSAEAKDFILKLLEKDPKKRLGAGPRGAHEIKEHPFFKGL 268
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
46-243 1.09e-47

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: 160.47  E-value: 1.09e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCKeGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLF 125
Cdd:cd05599  131 NLLLDARGHIKLSDFGLCT-GLKKSHLAYSTVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETC 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 126 ELIL--MEDIKFPR--TLSSDAKSLLSGLLIkDPNKRLGGGpdDAKEIMRHSFFSGVNWQDVYDKKlvPPFKPQVTSETD 201
Cdd:cd05599  210 RKIMnwRETLVFPPevPISPEAKDLIERLLC-DAEHRLGAN--GVEEIKSHPFFKGVDWDHIRERP--APILPEVKSILD 284
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767912019 202 TRYFDEEFTAQTITITPPEKYDEDGmdcMDNERRPHFPQFSY 243
Cdd:cd05599  285 TSNFDEFEEVDLQIPSSPEAGKDSK---ELKSKDWVFIGYTY 323
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
45-244 2.76e-46

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: 157.45  E-value: 2.76e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKEGITDAATM-----------------------------KTFCGTPEYLAPEVLEDNDYGR 95
Cdd:cd05573  130 DNILLDADGHIKLADFGLCTKMNKSGDREsylndsvntlfqdnvlarrrphkqrrvraYSAVGTPDYIAPEVLRGTGYGP 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  96 AVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL--MEDIKFPR--TLSSDAKSLLSGLLIkDPNKRLGggpdDAKEIMR 171
Cdd:cd05573  210 ECDWWSLGVILYEMLYGFPPFYSDSLVETYSKIMnwKESLVFPDdpDVSPEAIDLIRRLLC-DPEDRLG----SAEEIKA 284
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912019 172 HSFFSGVNWQDVYDkkLVPPFKPQVTSETDTRYFDEeftaqTITITPPEKYDEDGMDCMDNERRPHFPQFSYS 244
Cdd:cd05573  285 HPFFKGIDWENLRE--SPPPFVPELSSPTDTSNFDD-----FEDDLLLSEYLSNGSPLLGKGKQLAFVGFTFK 350
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
45-180 2.60e-45

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: 152.76  E-value: 2.60e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKEGITDAATM---------------KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEM 109
Cdd:cd05579  122 DNILIDANGHLKLTDFGLSKVGLVRRQIKlsiqkksngapekedRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEF 201
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912019 110 MCGRLPFYNQDHEKLFELILMEDIKFPR--TLSSDAKSLLSGLLIKDPNKRLGGGPddAKEIMRHSFFSGVNW 180
Cdd:cd05579  202 LVGIPPFHAETPEEIFQNILNGKIEWPEdpEVSDEAKDLISKLLTPDPEKRLGAKG--IEEIKNHPFFKGIDW 272
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
45-174 4.88e-45

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: 151.47  E-value: 4.88e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKEgiTDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL 124
Cdd:cd14007  129 ENILLGSNGELKLADFGWSVH--APSNRRKTFCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQET 206
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767912019 125 FELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSF 174
Cdd:cd14007  207 YKRIQNVDIKFPSSVSPEAKDLISKLLQKDPSKRL-----SLEQVLNHPW 251
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
44-174 6.93e-45

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: 151.09  E-value: 6.93e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  44 LENLML---DKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD 120
Cdd:cd05117  127 PENILLaskDPDSPIKIIDFGLAKI-FEEGEKLKTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGET 205
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767912019 121 HEKLFELILMEDIKFP----RTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSF 174
Cdd:cd05117  206 EQELFEKILKGKYSFDspewKNVSEEAKDLIKRLLVVDPKKRL-----TAAEALNHPW 258
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
45-182 6.95e-45

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: 151.22  E-value: 6.95e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHE-- 122
Cdd:cd05572  122 ENLLLDSNGYVKLVDFGFAKK-LGSGRKTWTFCGTPEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEDpm 200
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912019 123 KLFELILME--DIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQD 182
Cdd:cd05572  201 KIYNIILKGidKIEFPKYIDKNAKNLIKQLLRRNPEERLGYLKGGIRDIKKHKWFEGFDWEG 262
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
45-196 6.03e-40

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 140.06  E-value: 6.03e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCK------------------------------EGITDAATMkTFCGTPEYLAPEVLEDNDYG 94
Cdd:cd05574  132 ENILLHESGHIMLTDFDLSKqssvtpppvrkslrkgsrrssvksieketfVAEPSARSN-SFVGTEEYIAPEVIKGDGHG 210
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  95 RAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPR--TLSSDAKSLLSGLLIKDPNKRLG--GGpddAKEIM 170
Cdd:cd05574  211 SAVDWWTLGILLYEMLYGTTPFKGSNRDETFSNILKKELTFPEspPVSSEAKDLIRKLLVKDPSKRLGskRG---ASEIK 287
                        170       180
                 ....*....|....*....|....*.
gi 767912019 171 RHSFFSGVNWQDVydKKLVPPFKPQV 196
Cdd:cd05574  288 RHPFFRGVNWALI--RNMTPPIIPRP 311
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
45-180 1.12e-39

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


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 138.31  E-value: 1.12e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKEGITDAATM---------------KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEM 109
Cdd:cd05609  129 DNLLITSMGHIKLTDFGLSKIGLMSLTTNlyeghiekdtrefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEF 208
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912019 110 MCGRLPFYNQDHEKLFELILMEDIKFPR---TLSSDAKSLLSGLLIKDPNKRLGGGpdDAKEIMRHSFFSGVNW 180
Cdd:cd05609  209 LVGCVPFFGDTPEELFGQVISDEIEWPEgddALPDDAQDLITRLLQQNPLERLGTG--GAEEVKQHPFFQDLDW 280
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
40-207 5.05e-39

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: 137.83  E-value: 5.05e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFG-LCKEGITDAATMKTFCGTPEYLAPEVLE--DND----YGRAVDWWGLGVVMYEMMCG 112
Cdd:cd05601  126 RDIKPENILIDRTGHIKLADFGsAAKLSSDKTVTSKMPVGTPDYIAPEVLTsmNGGskgtYGVECDWWSLGIVAYEMLYG 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 113 RLPFYNQDHEKLFELIL--MEDIKFP--RTLSSDAKSLLSGLLiKDPNKRLGGgpddaKEIMRHSFFSGVNWQDVYDKkl 188
Cdd:cd05601  206 KTPFTEDTVIKTYSNIMnfKKFLKFPedPKVSESAVDLIKGLL-TDAKERLGY-----EGLCCHPFFSGIDWNNLRQT-- 277
                        170
                 ....*....|....*....
gi 767912019 189 VPPFKPQVTSETDTRYFDE 207
Cdd:cd05601  278 VPPFVPTLTSDDDTSNFDE 296
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
40-243 9.72e-39

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: 137.06  E-value: 9.72e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKeGITDAATMKTFC-----GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRL 114
Cdd:cd05598  125 RDIKPDNILIDRDGHIKLTDFGLCT-GFRWTHDSKYYLahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQP 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 115 PFYNQ--DHEKLFELILMEDIKFPRT--LSSDAKSLLSGlLIKDPNKRLGGGpdDAKEIMRHSFFSGVNWQdvYDKKLVP 190
Cdd:cd05598  204 PFLAQtpAETQLKVINWRTTLKIPHEanLSPEAKDLILR-LCCDAEDRLGRN--GADEIKAHPFFAGIDWE--KLRKQKA 278
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767912019 191 PFKPQVTSETDTRYFDEefTAQTITITPPEKyDEDGMDCMDNERRPH-FPQFSY 243
Cdd:cd05598  279 PYIPTIRHPTDTSNFDP--VDPEKLRSSDEE-PTTPNDPDNGKHPEHaFYEFTF 329
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
40-219 3.61e-38

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: 135.55  E-value: 3.61e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLC----KEGITDAATMktfCGTPEYLAPEVLEDND-----YGRAVDWWGLGVVMYEMM 110
Cdd:cd05597  126 RDIKPDNVLLDRNGHIRLADFGSClklrEDGTVQSSVA---VGTPDYISPEILQAMEdgkgrYGPECDWWSLGVCMYEML 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 111 CGRLPFYNQ----------DHEKLFELILMEDikfprTLSSDAKSLLSGlLIKDPNKRLG-GGPDDakeIMRHSFFSGVN 179
Cdd:cd05597  203 YGETPFYAEslvetygkimNHKEHFSFPDDED-----DVSEEAKDLIRR-LICSRERRLGqNGIDD---FKKHPFFEGID 273
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 767912019 180 WQDVYDkkLVPPFKPQVTSETDTRYFDEEFTAQTITITPP 219
Cdd:cd05597  274 WDNIRD--STPPYIPEVTSPTDTSNFDVDDDDLRHTDSLP 311
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
45-194 7.33e-38

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


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 133.63  E-value: 7.33e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH--- 121
Cdd:cd05605  131 ENILLDDHGHVRISDLGLAVE-IPEGETIRGRVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEkvk 209
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912019 122 -EKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKP 194
Cdd:cd05605  210 rEEVDRRVKEDQEEYSEKFSEEAKSICSQLLQKDPKTRLGCRGEGAEDVKSHPFFKSINFKRLEAGLLEPPFVP 283
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
45-194 2.00e-37

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: 132.27  E-value: 2.00e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ---- 119
Cdd:cd05577  124 ENILLDDHGHVRISDLGLAVE-FKGGKKIKGRVGTHGYMAPEVLqKEVAYDFSVDWFALGCMLYEMIAGRSPFRQRkekv 202
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912019 120 DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKP 194
Cdd:cd05577  203 DKEELKRRTLEMAVEYPDSFSPEARSLCEGLLQKDPERRLGCRGGSADEVKEHPFFRSLNWQRLEAGMLEPPFVP 277
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
40-223 2.82e-37

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: 134.04  E-value: 2.82e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLC-KEGITDAATMKTFCGTPEYLAPEVLE----DNDYGRAVDWWGLGVVMYEMMCGRL 114
Cdd:cd05596  149 RDVKPDNMLLDASGHLKLADFGTCmKMDKDGLVRSDTAVGTPDYISPEVLKsqggDGVYGRECDWWSVGVFLYEMLVGDT 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 115 PFYNQDHEKLFELIL--MEDIKFPR--TLSSDAKSLLSGLLIkDPNKRLGGGPDDakEIMRHSFFSGVNWQDVYDKKLVP 190
Cdd:cd05596  229 PFYADSLVGTYGKIMnhKNSLQFPDdvEISKDAKSLICAFLT-DREVRLGRNGIE--EIKAHPFFKNDQWTWDNIRETVP 305
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767912019 191 PFKPQVTSETDTRYFD--EEFTAQTITITPPEKYD 223
Cdd:cd05596  306 PVVPELSSDIDTSNFDdiEEDETPEETFPVPKAFV 340
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
45-207 1.31e-36

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: 132.85  E-value: 1.31e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKEGITDA--------------------------ATMKTF-----------CGTPEYLAPEV 87
Cdd:cd05600  140 ENFLIDSSGHIKLTDFGLASGTLSPKkiesmkirleevkntafleltakerrNIYRAMrkedqnyansvVGSPDYMAPEV 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  88 LEDNDYGRAVDWWGLGVVMYEMMCGRLPFY---------NQDH-EKLFELILMEDIKFPRTLSSDAKSLLSgLLIKDPNK 157
Cdd:cd05600  220 LRGEGYDLTVDYWSLGCILFECLVGFPPFSgstpnetwaNLYHwKKTLQRPVYTDPDLEFNLSDEAWDLIT-KLITDPQD 298
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767912019 158 RLGGgpddAKEIMRHSFFSGVNWqDVYDKKLVPPFKPQVTSETDTRYFDE 207
Cdd:cd05600  299 RLQS----PEQIKNHPFFKNIDW-DRLREGSKPPFIPELESEIDTSYFDD 343
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
45-175 2.47e-36

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: 129.64  E-value: 2.47e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFG----LCKEGITDAATMK-------------TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMY 107
Cdd:cd05581  130 ENILLDEDMHIKITDFGtakvLGPDSSPESTKGDadsqiaynqaraaSFVGTAEYVSPELLNEKPAGKSSDLWALGCIIY 209
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912019 108 EMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPD-DAKEIMRHSFF 175
Cdd:cd05581  210 QMLTGKPPFRGSNEYLTFQKIVKLEYEFPENFPPDAKDLIQKLLVLDPSKRLGVNENgGYDELKAHPFF 278
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
40-180 3.02e-36

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: 129.14  E-value: 3.02e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATmKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd05611  121 RDIKPENLLIDQTGHLKLTDFGLSRNGLEKRHN-KKFVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAE 199
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912019 120 DHEKLFELILMEDIKFPR----TLSSDAKSLLSGLLIKDPNKRLGGgpDDAKEIMRHSFFSGVNW 180
Cdd:cd05611  200 TPDAVFDNILSRRINWPEevkeFCSPEAVDLINRLLCMDPAKRLGA--NGYQEIKSHPFFKSINW 262
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
40-206 5.89e-36

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 130.10  E-value: 5.89e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKegITDAATMkTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:PTZ00426 155 RDLKPENLLLDKDGFIKMTDFGFAK--VVDTRTY-TLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYAN 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 120 DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSE 199
Cdd:PTZ00426 232 EPLLIYQKILEGIIYFPKFLDNNCKHLMKKLLSHDLTKRYGNLKKGAQNVKEHPWFGNIDWVSLLHKNVEVPYKPKYKNV 311

                 ....*..
gi 767912019 200 TDTRYFD 206
Cdd:PTZ00426 312 FDSSNFE 318
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
40-194 1.65e-34

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


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 124.99  E-value: 1.65e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd05608  129 RDLKPENVLLDDDGNVRISDLGLAVELKDGQTKTKGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRAR 208
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912019 120 ----DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKP 194
Cdd:cd05608  209 gekvENKELKQRILNDSVTYSEKFSPASKSICEALLAKDPEKRLGFRDGNCDGLRTHPFFRDINWRKLEAGILPPPFVP 287
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
40-219 4.70e-34

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


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 126.66  E-value: 4.70e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFC-GTPEYLAPEVL---EDN--DYGRAVDWWGLGVVMYEMMCGR 113
Cdd:cd05624  197 RDIKPDNVLLDMNGHIRLADFGSCLKMNDDGTVQSSVAvGTPDYISPEILqamEDGmgKYGPECDWWSLGVCMYEMLYGE 276
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 114 LPFYNQDHEKLFELIL--MEDIKFPR---TLSSDAKSLLSgLLIKDPNKRLG-GGPDDAKeimRHSFFSGVNWQDVydKK 187
Cdd:cd05624  277 TPFYAESLVETYGKIMnhEERFQFPShvtDVSEEAKDLIQ-RLICSRERRLGqNGIEDFK---KHAFFEGLNWENI--RN 350
                        170       180       190
                 ....*....|....*....|....*....|...
gi 767912019 188 LVPPFKPQVTSETDTRYFD-EEFTAQTITITPP 219
Cdd:cd05624  351 LEAPYIPDVSSPSDTSNFDvDDDVLRNPEILPP 383
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
40-174 1.31e-33

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 121.74  E-value: 1.31e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLC--KEGITDAATMKTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd14663  124 RDLKPENLLLDEDGNLKISDFGLSalSEQFRQDGLLHTTCGTPNYVAPEVLARRGYdGAKADIWSCGVILFVLLAGYLPF 203
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767912019 117 YNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSF 174
Cdd:cd14663  204 DDENLMALYRKIMKGEFEYPRWFSPGAKSLIKRILDPNPSTRI-----TVEQIMASPW 256
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
40-219 7.40e-33

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


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 122.65  E-value: 7.40e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCK---------------EG---------------------ITDAATMKTF------- 76
Cdd:cd05629  125 RDIKPDNILIDRGGHIKLSDFGLSTgfhkqhdsayyqkllQGksnknridnrnsvavdsinltMSSKDQIATWkknrrlm 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  77 ----CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL--MEDIKFPR--TLSSDAKSLLS 148
Cdd:cd05629  205 aystVGTPDYIAPEIFLQQGYGQECDWWSLGAIMFECLIGWPPFCSENSHETYRKIInwRETLYFPDdiHLSVEAEDLIR 284
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912019 149 GlLIKDPNKRLGGGpdDAKEIMRHSFFSGVNWQDVydKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPP 219
Cdd:cd05629  285 R-LITNAENRLGRG--GAHEIKSHPFFRGVDWDTI--RQIRAPFIPQLKSITDTSYFPTDELEQVPEAPAL 350
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
45-175 8.05e-33

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


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 119.67  E-value: 8.05e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL 124
Cdd:cd05578  129 DNILLDEQGHVHITDFNIATK-LTDGTLATSTSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSRTSI 207
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767912019 125 FELILME---DIKFPRTLSSDAKSLLSGLLIKDPNKRLGggpdDAKEIMRHSFF 175
Cdd:cd05578  208 EEIRAKFetaSVLYPAGWSEEAIDLINKLLERDPQKRLG----DLSDLKNHPYF 257
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
40-212 1.19e-32

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


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 121.52  E-value: 1.19e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCK----------EGITDAATMKT---------------------------------- 75
Cdd:cd05610  128 RDLKPDNMLISNEGHIKLTDFGLSKvtlnrelnmmDILTTPSMAKPkndysrtpgqvlslisslgfntptpyrtpksvrr 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  76 ---------FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFP---RTLSSDA 143
Cdd:cd05610  208 gaarvegerILGTPDYLAPELLLGKPHGPAVDWWALGVCLFEFLTGIPPFNDETPQQVFQNILNRDIPWPegeEELSVNA 287
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912019 144 KSLLSGLLIKDPNKRLGggpddAKEIMRHSFFSGVNWQDVYDKKlvPPFKPQVTSETDTRYFDEEFTAQ 212
Cdd:cd05610  288 QNAIEILLTMDPTKRAG-----LKELKQHPLFHGVDWENLQNQT--MPFIPQPDDETDTSYFEARNNAQ 349
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
40-194 1.39e-32

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: 120.13  E-value: 1.39e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd05630  126 RDLKPENILLDDHGHIRISDLGLAVH-VPEGQTIKGRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQR 204
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912019 120 ----DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKP 194
Cdd:cd05630  205 kkkiKREEVERLVKEVPEEYSEKFSPQARSLCSMLLCKDPAERLGCRGGGAREVKEHPLFKKLNFKRLGAGMLEPPFKP 283
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
45-158 1.57e-32

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: 119.01  E-value: 1.57e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLM---LDKDGHIKITDFGLCKegITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH 121
Cdd:cd14083  130 ENLLyysPDEDSKIMISDFGLSK--MEDSGVMSTACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDEND 207
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767912019 122 EKLFELILMEDIKFPR----TLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd14083  208 SKLFAQILKAEYEFDSpywdDISDSAKDFIRHLMEKDPNKR 248
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
46-175 1.60e-32

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: 119.10  E-value: 1.60e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCK--EGITDAAtmKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEK 123
Cdd:cd08215  133 NIFLTKDGVVKLGDFGISKvlESTTDLA--KTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPA 210
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767912019 124 LFELILMEDI-KFPRTLSSDAKSLLSGLLIKDPNKRlgggPdDAKEIMRHSFF 175
Cdd:cd08215  211 LVYKIVKGQYpPIPSQYSSELRDLVNSMLQKDPEKR----P-SANEILSSPFI 258
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
45-160 1.92e-31

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: 116.20  E-value: 1.92e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL 124
Cdd:cd14002  128 QNILIGKGGVVKLCDFGFARAMSCNTLVLTSIKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQL 207
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767912019 125 FELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLG 160
Cdd:cd14002  208 VQMIVKDPVKWPSNMSPEFKSFLQGLLNKDPSKRLS 243
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
45-175 1.97e-31

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: 116.50  E-value: 1.97e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDY---GRAVDWWGLGVVMYEMMCGRLPFYNQDH 121
Cdd:cd14008  137 ENLLLTADGTVKISDFGVSEMFEDGNDTLQKTAGTPAFLAPELCDGDSKtysGKAADIWALGVTLYCLVFGRLPFNGDNI 216
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767912019 122 EKLFELILME--DIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd14008  217 LELYEAIQNQndEFPIPPELSPELKDLLRRMLEKDPEKRI-----TLKEIKEHPWV 267
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
40-194 2.26e-31

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: 116.63  E-value: 2.26e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd05631  126 RDLKPENILLDDRGHIRISDLGLAVQ-IPEGETVRGRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKR 204
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912019 120 DH----EKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKP 194
Cdd:cd05631  205 KErvkrEEVDRRVKEDQEEYSEKFSEDAKSICRMLLTKNPKERLGCRGNGAAGVKQHPIFKNINFKRLEANMLEPPFCP 283
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
46-194 3.72e-31

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 116.00  E-value: 3.72e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCkegiTDAATMK--TFCGTPEYLAPEVLEDN-DYGRAVDWWGLGVVMYEMMCGRLPFYNQ--- 119
Cdd:cd05606  128 NILLDEHGHVRISDLGLA----CDFSKKKphASVGTHGYMAPEVLQKGvAYDSSADWFSLGCMLYKLLKGHSPFRQHktk 203
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912019 120 DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKP 194
Cdd:cd05606  204 DKHEIDRMTLTMNVELPDSFSPELKSLLEGLLQRDVSKRLGCLGRGATEVKEHPFFKGVDWQQVYLQKYPPPLIP 278
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
44-175 4.22e-31

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: 115.34  E-value: 4.22e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  44 LENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLE-DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHE 122
Cdd:cd14099  129 LGNLFLDENMNVKIGDFGLAARLEYDGERKKTLCGTPNYIAPEVLEkKKGHSFEVDIWSLGVILYTLLVGKPPFETSDVK 208
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767912019 123 KLFELILMEDIKFPRTL--SSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd14099  209 ETYKRIKKNEYSFPSHLsiSDEAKDLIRSMLQPDPTKRP-----SLDEILSHPFF 258
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
40-194 1.17e-30

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: 115.45  E-value: 1.17e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd05632  128 RDLKPENILLDDYGHIRISDLGLAVK-IPEGESIRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGR 206
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912019 120 DH----EKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKP 194
Cdd:cd05632  207 KEkvkrEEVDRRVLETEEVYSAKFSEEAKSICKMLLTKDPKQRLGCQEEGAGEVKRHPFFRNMNFKRLEAGMLDPPFVP 285
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
29-177 1.54e-30

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: 113.97  E-value: 1.54e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  29 IRFRFDLQAPPKNISLENLM---LDKDGHIKITDFGLCK-EGitDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGV 104
Cdd:cd14167  114 VKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSKiEG--SGSVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGV 191
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912019 105 VMYEMMCGRLPFYNQDHEKLFELILMEDIKFPR----TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFSG 177
Cdd:cd14167  192 IAYILLCGYPPFYDENDAKLFEQILKAEYEFDSpywdDISDSAKDFIQHLMEKDPEKRF-----TCEQALQHPWIAG 263
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
40-174 2.69e-30

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: 113.31  E-value: 2.69e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLckEGITDAAT-MKTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFY 117
Cdd:cd14077  137 RDLKIENILISKSGNIKIIDFGL--SNLYDPRRlLRTFCGSLYFAAPELLQAQPYtGPEVDVWSFGVVLYVLVCGKVPFD 214
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767912019 118 NQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGggpddAKEIMRHSF 174
Cdd:cd14077  215 DENMPALHAKIKKGKVEYPSYLSSECKSLISRMLVVDPKKRAT-----LEQVLNHPW 266
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
40-219 4.88e-30

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: 115.88  E-value: 4.88e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFC-GTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGR 113
Cdd:cd05623  197 RDIKPDNILMDMNGHIRLADFGSCLKLMEDGTVQSSVAvGTPDYISPEILQamedgKGKYGPECDWWSLGVCMYEMLYGE 276
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 114 LPFYNQDHEKLFELIL--MEDIKFPRTL---SSDAKSLLSGLLIKDPNKRLGGGPDDAKeimRHSFFSGVNWQDVydKKL 188
Cdd:cd05623  277 TPFYAESLVETYGKIMnhKERFQFPTQVtdvSENAKDLIRRLICSREHRLGQNGIEDFK---NHPFFVGIDWDNI--RNC 351
                        170       180       190
                 ....*....|....*....|....*....|...
gi 767912019 189 VPPFKPQVTSETDTRYF--DEEFTAQTITITPP 219
Cdd:cd05623  352 EAPYIPEVSSPTDTSNFdvDDDCLKNCETMPPP 384
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
45-175 5.11e-30

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: 112.61  E-value: 5.11e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCK--EGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHE 122
Cdd:cd06606  128 ANILVDSDGVVKLADFGCAKrlAEIATGEGTKSLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSELGNP 207
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767912019 123 K--LFELILMEDI-KFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd06606  208 VaaLFKIGSSGEPpPIPEHLSEEAKDFLRKCLQRDPKKRP-----TADELLQHPFL 258
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
44-175 2.14e-29

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: 110.81  E-value: 2.14e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  44 LENLMLDKDGHIKITDFG---LCKEGITdaatMKTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd14081  129 PENLLLDEKNNIKIADFGmasLQPEGSL----LETSCGSPHYACPEVIKGEKYdGRKADIWSCGVILYALLVGALPFDDD 204
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767912019 120 DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd14081  205 NLRQLLEKVKRGVFHIPHFISPDAQDLLRRMLEVNPEKRI-----TIEEIKKHPWF 255
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
40-175 6.82e-29

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


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 109.75  E-value: 6.82e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDN------DYGRAVDWWGLGVVMYEMMCGR 113
Cdd:cd14093  133 RDLKPENILLDDNLNVKISDFGFATR-LDEGEKLRELCGTPGYLAPEVLKCSmydnapGYGKEVDMWACGVIMYTLLAGC 211
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912019 114 LPFYNQDHEKLFELILMEDIKFPR----TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd14093  212 PPFWHRKQMVMLRNIMEGKYEFGSpewdDISDTAKDLISKLLVVDPKKRL-----TAEEALEHPFF 272
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
46-174 1.34e-28

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


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 108.92  E-value: 1.34e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGL-CKEGITDAATMKTFC---------------GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEM 109
Cdd:cd14010  124 NILLDGNGTLKLSDFGLaRREGEILKELFGQFSdegnvnkvskkqakrGTPYYMAPELFQGGVHSFASDLWALGCVLYEM 203
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 110 MCGRLPFYNQDHEKLFELILMEDIKFPRT-----LSSDAKSLLSGLLIKDPNKRLGGGpddakEIMRHSF 174
Cdd:cd14010  204 FTGKPPFVAESFTELVEKILNEDPPPPPPkvsskPSPDFKSLLKGLLEKDPAKRLSWD-----ELVKHPF 268
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
40-172 1.53e-28

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: 108.57  E-value: 1.53e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDG----HIKITDFGLckegitdAATMK----TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC 111
Cdd:cd14095  122 RDIKPENLLVVEHEdgskSLKLADFGL-------ATEVKeplfTVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLC 194
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912019 112 GRLPFY--NQDHEKLFELILMEDIKFPR----TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRH 172
Cdd:cd14095  195 GFPPFRspDRDQEELFDLILAGEFEFLSpywdNISDSAKDLISRMLVVDPEKRY-----SAGQVLDH 256
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
40-207 1.59e-28

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: 111.64  E-value: 1.59e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLC----KEGITDAATMktfCGTPEYLAPEVLE----DNDYGRAVDWWGLGVVMYEMMC 111
Cdd:cd05622  196 RDVKPDNMLLDKSGHLKLADFGTCmkmnKEGMVRCDTA---VGTPDYISPEVLKsqggDGYYGRECDWWSVGVFLYEMLV 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 112 GRLPFYNQDHEKLFELIL--MEDIKFPR--TLSSDAKSLLSGLLiKDPNKRLggGPDDAKEIMRHSFFSGVNWQDVYDKK 187
Cdd:cd05622  273 GDTPFYADSLVGTYSKIMnhKNSLTFPDdnDISKEAKNLICAFL-TDREVRL--GRNGVEEIKRHLFFKNDQWAWETLRD 349
                        170       180
                 ....*....|....*....|
gi 767912019 188 LVPPFKPQVTSETDTRYFDE 207
Cdd:cd05622  350 TVAPVVPDLSSDIDTSNFDD 369
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
45-175 2.66e-28

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 108.12  E-value: 2.66e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLcKEGITDAATMKTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEK 123
Cdd:cd14079  131 ENLLLDSNMNVKIADFGL-SNIMRDGEFLKTSCGSPNYAAPEVISGKLYaGPEVDVWSCGVILYALLCGSLPFDDEHIPN 209
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767912019 124 LFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd14079  210 LFKKIKSGIYTIPSHLSPGARDLIKRMLVVDPLKRI-----TIPEIRQHPWF 256
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
53-172 3.88e-28

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 108.29  E-value: 3.88e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  53 GHIKITDFGLCKegITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMED 132
Cdd:cd14096  176 GIVKLADFGLSK--QVWDSNTKTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPFYDESIETLTEKISRGD 253
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 767912019 133 IKFPR----TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRH 172
Cdd:cd14096  254 YTFLSpwwdEISKSAKDLISHLLTVDPAKRY-----DIDEFLAH 292
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
40-210 5.43e-28

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


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 109.00  E-value: 5.43e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCkegiTDAATMKTFC--GTPEYLAPEVLEDND-YGRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd05633  132 RDLKPANILLDEHGHVRISDLGLA----CDFSKKKPHAsvGTHGYMAPEVLQKGTaYDSSADWFSLGCMLFKLLRGHSPF 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 117 YN---QDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFK 193
Cdd:cd05633  208 RQhktKDKHEIDRMTLTVNVELPDSFSPELKSLLEGLLQRDVSKRLGCHGRGAQEVKEHSFFKGIDWQQVYLQKYPPPLI 287
                        170       180
                 ....*....|....*....|..
gi 767912019 194 P-----QVTSETDTRYFDEEFT 210
Cdd:cd05633  288 PprgevNAADAFDIGSFDEEDT 309
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
40-177 5.54e-28

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: 107.77  E-value: 5.54e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLML---DKDGHIKITDFGLCKegITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd14166  124 RDLKPENLLYltpDENSKIMITDFGLSK--MEQNGIMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPF 201
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912019 117 YNQDHEKLFELILMEDIKFPR----TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFSG 177
Cdd:cd14166  202 YEETESRLFEKIKEGYYEFESpfwdDISESAKDFIRHLLEKNPSKRY-----TCEKALSHPWIIG 261
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
40-177 6.01e-28

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: 107.67  E-value: 6.01e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLD---KDGHIKITDFGLCKegITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd14169  125 RDLKPENLLYAtpfEDSKIMISDFGLSK--IEAQGMLSTACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPF 202
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912019 117 YNQDHEKLFELILMEDIKFPR----TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFSG 177
Cdd:cd14169  203 YDENDSELFNQILKAEYEFDSpywdDISESAKDFIRHLLERDPEKRF-----TCEQALQHPWISG 262
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
45-159 7.48e-28

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 106.70  E-value: 7.48e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLC---KEGITDAatMKTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQD 120
Cdd:cd14078  130 ENLLLDEDQNLKLIDFGLCakpKGGMDHH--LETCCGSPAYAAPELIQGKPYiGSEADVWSMGVLLYALLCGFLPFDDDN 207
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 767912019 121 HEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRL 159
Cdd:cd14078  208 VMALYRKIQSGKYEEPEWLSPSSKLLLDQMLQVDPKKRI 246
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
21-175 7.73e-28

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: 106.79  E-value: 7.73e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  21 EDIA------LPYKIRFRFDLQAPPKNISLENLMLDKDGHIKITDFGLCKEGITDA----ATMKTFCGTPEYLAPEVLED 90
Cdd:cd14165  101 EDVArkmfhqLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRDEngriVLSKTFCGSAAYAAPEVLQG 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  91 NDYG-RAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRT--LSSDAKSLLSGLLIKDPNKRLgggpdDAK 167
Cdd:cd14165  181 IPYDpRIYDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFPRSknLTSECKDLIYRLLQPDVSQRL-----CID 255

                 ....*...
gi 767912019 168 EIMRHSFF 175
Cdd:cd14165  256 EVLSHPWL 263
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
45-175 2.12e-27

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: 105.73  E-value: 2.12e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKE-GITDAATM-KTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDH 121
Cdd:cd14080  131 ENILLDSNNNVKLSDFGFARLcPDDDGDVLsKTFCGSAAYAAPEILQGIPYdPKKYDIWSLGVILYIMLCGSMPFDDSNI 210
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767912019 122 EKLFELILMEDIKFPRT---LSSDAKSLLSGLLIKDPNKRLGggpddAKEIMRHSFF 175
Cdd:cd14080  211 KKMLKDQQNRKVRFPSSvkkLSPECKDLIDQLLEPDPTKRAT-----IEEILNHPWL 262
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
40-207 2.60e-27

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: 107.78  E-value: 2.60e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLC-KEGITDAATMKTFCGTPEYLAPEVLE----DNDYGRAVDWWGLGVVMYEMMCGRL 114
Cdd:cd05621  175 RDVKPDNMLLDKYGHLKLADFGTCmKMDETGMVHCDTAVGTPDYISPEVLKsqggDGYYGRECDWWSVGVFLFEMLVGDT 254
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 115 PFYNQDHEKLFELIL--MEDIKFPR--TLSSDAKSLLSGLLiKDPNKRLggGPDDAKEIMRHSFFSGVNWQDVYDKKLVP 190
Cdd:cd05621  255 PFYADSLVGTYSKIMdhKNSLNFPDdvEISKHAKNLICAFL-TDREVRL--GRNGVEEIKQHPFFRNDQWNWDNIRETAA 331
                        170
                 ....*....|....*..
gi 767912019 191 PFKPQVTSETDTRYFDE 207
Cdd:cd05621  332 PVVPELSSDIDTSNFDD 348
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
42-171 3.18e-27

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: 105.36  E-value: 3.18e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  42 ISLENLMLDKDGHIKITDFGLCK-EGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD 120
Cdd:cd14014  126 IKPANILLTEDGRVKLTDFGIARaLGDSGLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDS 205
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767912019 121 HEKLFELILMEDIKFPRT----LSSDAKSLLSGLLIKDPNKRlgggPDDAKEIMR 171
Cdd:cd14014  206 PAAVLAKHLQEAPPPPSPlnpdVPPALDAIILRALAKDPEER----PQSAAELLA 256
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
40-159 9.39e-27

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: 104.36  E-value: 9.39e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVL---EDNDYGRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd14118  139 RDIKPSNLLLGDDGHVKIADFGVSNEFEGDDALLSSTAGTPAFMAPEALsesRKKFSGKALDIWAMGVTLYCFVFGRCPF 218
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767912019 117 YNQDHEKLFELILMEDIKFPR--TLSSDAKSLLSGLLIKDPNKRL 159
Cdd:cd14118  219 EDDHILGLHEKIKTDPVVFPDdpVVSEQLKDLILRMLDKNPSERI 263
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
40-172 1.08e-26

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


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 104.17  E-value: 1.08e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDG-------HIKITDFGLC--KEGITDAATMKTfCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMM 110
Cdd:cd14097  124 RDLKLENILVKSSIidnndklNIKVTDFGLSvqKYGLGEDMLQET-CGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLL 202
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912019 111 CGRLPFYNQDHEKLFELILMEDIKFP----RTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRH 172
Cdd:cd14097  203 CGEPPFVAKSEEKLFEEIRKGDLTFTqsvwQSVSDAAKNVLQQLLKVDPAHRM-----TASELLDN 263
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
46-175 2.48e-26

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: 102.67  E-value: 2.48e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLF 125
Cdd:cd05122  128 NILLTSDGEVKLIDFGLSAQ-LSDGKTRNTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKAL 206
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767912019 126 ELILMED---IKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd05122  207 FLIATNGppgLRNPKKWSKEFKDFLKKCLQKDPEKRP-----TAEQLLKHPFI 254
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
40-175 2.49e-26

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: 102.70  E-value: 2.49e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd14189  125 RDLKLGNFFINENMELKVGDFGLAARLEPPEQRKKTICGTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETL 204
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767912019 120 DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd14189  205 DLKETYRCIKQVKYTLPASLSLPARHLLAGILKRNPGDRL-----TLDQILEHEFF 255
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
40-175 5.95e-26

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: 101.99  E-value: 5.95e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATM----KTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRL 114
Cdd:cd14162  124 RDLKCENLLLDKNNNLKITDFGFARGVMKTKDGKpklsETYCGSYAYASPEILRGIPYdPFLSDIWSMGVVLYTMVYGRL 203
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912019 115 PFYNQDHEKLFELIlMEDIKFPR--TLSSDAKSLLSGLLIKDPnKRLgggpdDAKEIMRHSFF 175
Cdd:cd14162  204 PFDDSNLKVLLKQV-QRRVVFPKnpTVSEECKDLILRMLSPVK-KRI-----TIEEIKRDPWF 259
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
40-158 6.86e-26

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: 101.44  E-value: 6.86e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYN 118
Cdd:cd14072  123 RDLKAENLLLDADMNIKIADFGFSNE-FTPGNKLDTFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDG 201
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767912019 119 QDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd14072  202 QNLKELRERVLRGKYRIPFYMSTDCENLLKKFLVLNPSKR 241
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
40-194 7.87e-26

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: 102.29  E-value: 7.87e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd05607  128 RDMKPENVLLDDNGNCRLSDLGLAVE-VKEGKPITQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDH 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 120 ----DHEKLFELILMEDIKFPR-TLSSDAKSLLSGLLIKDPNKRLGGGPDDaKEIMRHSFFSGVNWQDVYDKKLVPPFKP 194
Cdd:cd05607  207 kekvSKEELKRRTLEDEVKFEHqNFTEEAKDICRLFLAKKPENRLGSRTND-DDPRKHEFFKSINFPRLEAGLIDPPFVP 285
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
46-176 8.57e-26

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: 101.13  E-value: 8.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLF 125
Cdd:cd06614  127 NILLSKDGSVKLADFGFAAQLTKEKSKRNSVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRAL 206
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767912019 126 ELILME---DIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFS 176
Cdd:cd06614  207 FLITTKgipPLKNPEKWSPEFKDFLNKCLVKDPEKRP-----SAEELLQHPFLK 255
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
40-177 1.23e-25

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: 102.05  E-value: 1.23e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLML---DKDGHIKITDFGLCK-EGITDaaTMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLP 115
Cdd:cd14168  132 RDLKPENLLYfsqDEESKIMISDFGLSKmEGKGD--VMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPP 209
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912019 116 FYNQDHEKLFELILMEDIKFPR----TLSSDAKSLLSGLLIKDPNKRlgggpDDAKEIMRHSFFSG 177
Cdd:cd14168  210 FYDENDSKLFEQILKADYEFDSpywdDISDSAKDFIRNLMEKDPNKR-----YTCEQALRHPWIAG 270
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
45-174 1.70e-25

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: 101.34  E-value: 1.70e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLML---DKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH 121
Cdd:cd14086  129 ENLLLaskSKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQ 208
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767912019 122 EKLFELILMEDIKFPR----TLSSDAKSLLSGLLIKDPNKRLGggpddAKEIMRHSF 174
Cdd:cd14086  209 HRLYAQIKAGAYDYPSpewdTVTPEAKDLINQMLTVNPAKRIT-----AAEALKHPW 260
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
42-175 2.80e-25

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: 100.00  E-value: 2.80e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  42 ISLENLMLDKD-GHIKITDFGlCKEGITDAAtMKTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd14005  133 IKDENLLINLRtGEVKLIDFG-CGALLKDSV-YTDFDGTRVYSPPEWIRHGRYhGRPATVWSLGILLYDMLCGDIPFEND 210
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767912019 120 dheklfELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd14005  211 ------EQILRGNVLFRPRLSKECCDLISRCLQFDPSKRP-----SLEQILSHPWF 255
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
34-172 5.80e-25

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 99.00  E-value: 5.80e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  34 DLQAppknislENLMLDKDGHIKITDFGLcKEGITDAATMKTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCG 112
Cdd:cd14071  124 DLKA-------ENLLLDANMNIKIADFGF-SNFFKPGELLKTWCGSPPYAAPEVFEGKEYeGPQLDIWSLGVVLYVLVCG 195
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 113 RLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGggpddAKEIMRH 172
Cdd:cd14071  196 ALPFDGSTLQTLRDRVLSGRFRIPFFMSTDCEHLIRRMLVLDPSKRLT-----IEQIKKH 250
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
45-160 7.18e-25

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: 98.83  E-value: 7.18e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGH---IKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH 121
Cdd:cd14009  121 QNLLLSTSGDdpvLKIADFGFARS-LQPASMAETLCGSPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNH 199
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767912019 122 EKLFELILMED--IKFP--RTLSSDAKSLLSGLLIKDPNKRLG 160
Cdd:cd14009  200 VQLLRNIERSDavIPFPiaAQLSPDCKDLLRRLLRRDPAERIS 242
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
40-174 1.22e-24

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: 98.18  E-value: 1.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFG---LCKEGitdaATMKTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLP 115
Cdd:cd14075  125 RDLKAENVFYASNNCVKVGDFGfstHAKRG----ETLNTFCGSPPYAAPELFKDEHYiGIYVDIWALGVLLYFMVTGVMP 200
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767912019 116 FYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSF 174
Cdd:cd14075  201 FRAETVAKLKKCILEGTYTIPSYVSEPCQELIRGILQPVPSDRY-----SIDEIKNSEW 254
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
46-158 1.29e-24

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: 97.99  E-value: 1.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFynQDHEKLF 125
Cdd:cd13999  121 NILLDENFTVKIADFGLSRIKNSTTEKMTGVVGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPF--KELSPIQ 198
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767912019 126 ELILMEDIKFPRTLSSDAKSLLSGLLIK----DPNKR 158
Cdd:cd13999  199 IAAAVVQKGLRPPIPPDCPPELSKLIKRcwneDPEKR 235
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
45-173 1.74e-24

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: 98.23  E-value: 1.74e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLML---DKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLE---DNDYGRAVDWWGLGVVMYEMMCGRLPFYN 118
Cdd:cd14084  140 ENVLLssqEEECLIKITDFGLSKI-LGETSLMKTLCGTPTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPFSE 218
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 119 Q-DHEKLFELILMEDIKF----PRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHS 173
Cdd:cd14084  219 EyTQMSLKEQILSGKYTFipkaWKNVSEEAKDLVKKMLVVDPSRRP-----SIEEALEHP 273
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
40-174 1.89e-24

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: 97.94  E-value: 1.89e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKE-GITDAATMKTFCGTPEYLAPE-VLEDNDY-GRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd14076  130 RDLKLENLLLDKNRNLVITDFGFANTfDHFNGDLMSTSCGSPCYAAPElVVSDSMYaGRKADIWSCGVILYAMLAGYLPF 209
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912019 117 yNQDHE--------KLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSF 174
Cdd:cd14076  210 -DDDPHnpngdnvpRLYRYICNTPLIFPEYVTPKARDLLRRILVPNPRKRI-----RLSAIMRHAW 269
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
40-172 3.58e-24

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: 97.16  E-value: 3.58e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDG--HIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVL------EDNDYGRAVDWWGLGVVMYEMMC 111
Cdd:cd14098  125 RDLKPENILITQDDpvIVKISDFGLAKV-IHTGTFLVTFCGTMAYLAPEILmskeqnLQGGYSNLVDMWSVGCLVYVMLT 203
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912019 112 GRLPFYNQDHEKLFELIlmEDIKFPR------TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRH 172
Cdd:cd14098  204 GALPFDGSSQLPVEKRI--RKGRYTQpplvdfNISEEAIDFILRLLDVDPEKRM-----TAAQALDH 263
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
40-158 4.26e-24

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


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 96.69  E-value: 4.26e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYN 118
Cdd:cd14073  125 RDLKLENILLDQNGNAKIADFGLSNL-YSKDKLLQTFCGSPLYASPEIVNGTPYqGPEVDCWSLGVLLYTLVYGTMPFDG 203
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767912019 119 QDHEKLFELILMEDIKFPRTLsSDAKSLLSGLLIKDPNKR 158
Cdd:cd14073  204 SDFKRLVKQISSGDYREPTQP-SDASGLIRWMLTVNPKRR 242
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
40-158 4.34e-24

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: 96.69  E-value: 4.34e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGlckegitDAATMK-----TFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGR 113
Cdd:cd14004  133 RDIKDENVILDGNGTIKLIDFG-------SAAYIKsgpfdTFVGTIDYAAPEVLRGNPYgGKEQDIWALGVLLYTLVFKE 205
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767912019 114 LPFYNQDHeklfelILMEDIKFPRTLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd14004  206 NPFYNIEE------ILEADLRIPYAVSEDLIDLISRMLNRDVGDR 244
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
16-172 5.18e-24

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: 96.56  E-value: 5.18e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  16 QRTAKEDIALPYKIRFRFDLQAPPKNISLENLMLDKDGHIKITDFGLCKEgiTDAATMKTFCGTPEYLAPEVLEDNDYGR 95
Cdd:cd14116  105 QRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVH--APSSRRTTLCGTLDYLPPEMIEGRMHDE 182
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912019  96 AVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRH 172
Cdd:cd14116  183 KVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKHNPSQRP-----MLREVLEH 254
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
45-175 6.23e-24

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 96.46  E-value: 6.23e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL 124
Cdd:cd08217  139 ANIFLDSDNNVKLGDFGLARVLSHDSSFAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLEL 218
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767912019 125 FELIlmEDIKFPR---TLSSDAKSLLSGLLIKDPNKRlgggPdDAKEIMRHSFF 175
Cdd:cd08217  219 AKKI--KEGKFPRipsRYSSELNEVIKSMLNVDPDKR----P-SVEELLQLPLI 265
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
40-174 6.36e-24

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: 96.56  E-value: 6.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLML----DKDGHIKITDFGLCKEGItdaATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLP 115
Cdd:cd14185  122 RDLKPENLLVqhnpDKSTTLKLADFGLAKYVT---GPIFTVCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPP 198
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912019 116 FYNQ--DHEKLFELILMEDIKF--P--RTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSF 174
Cdd:cd14185  199 FRSPerDQEELFQIIQLGHYEFlpPywDNISEAAKDLISRLLVVDPEKRY-----TAKQVLQHPW 258
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
40-172 6.60e-24

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


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 96.59  E-value: 6.60e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLML---DKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd14089  124 RDLKPENLLYsskGPNAILKLTDFGFAKE-TTTKKSLQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPF 202
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912019 117 YNQDHEKLF----ELILMEDIKFPRT----LSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRH 172
Cdd:cd14089  203 YSNHGLAISpgmkKRIRNGQYEFPNPewsnVSEEAKDLIRGLLKTDPSERL-----TIEEVMNH 261
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
40-175 1.18e-23

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: 95.85  E-value: 1.18e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd14188  125 RDLKLGNFFINENMELKVGDFGLAARLEPLEHRRRTICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETT 204
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767912019 120 DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRlgggpDDAKEIMRHSFF 175
Cdd:cd14188  205 NLKETYRCIREARYSLPSSLLAPAKHLIASMLSKNPEDR-----PSLDEIIRHDFF 255
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
42-174 1.30e-23

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: 95.74  E-value: 1.30e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  42 ISLENLMLDKDGHIKITDFGLCKeGITDAATMK-TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD 120
Cdd:cd06623  126 IKPSNLLINSKGEVKIADFGISK-VLENTLDQCnTFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPG 204
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767912019 121 HEKLFEL---ILMEDIKFPR--TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSF 174
Cdd:cd06623  205 QPSFFELmqaICDGPPPSLPaeEFSPEFRDFISACLQKDPKKRP-----SAAELLQHPF 258
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
40-175 1.91e-23

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: 95.02  E-value: 1.91e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFG----LCKegITDAATMKTFCGTPEYLAPEVLEDNDY--GRAVDWWGLGVVMYEMMCGR 113
Cdd:cd14119  121 KDIKPGNLLLTTDGTLKISDFGvaeaLDL--FAEDDTCTTSQGSPAFQPPEIANGQDSfsGFKVDIWSAGVTLYNMTTGK 198
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912019 114 LPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd14119  199 YPFEGDNIYKLFENIGKGEYTIPDDVDPDLQDLLRGMLEKDPEKRF-----TIEQIRQHPWF 255
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
40-158 2.45e-23

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


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 94.64  E-value: 2.45e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAaTMKTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYN 118
Cdd:cd14161  126 RDLKLENILLDANGNIKIADFGLSNLYNQDK-FLQTYCGSPLYASPEIVNGRPYiGPEVDSWSLGVLLYILVHGTMPFDG 204
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767912019 119 QDHEKLFELILMEDIKFPrTLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd14161  205 HDYKILVKQISSGAYREP-TKPSDACGLIRWLLMVNPERR 243
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
45-179 2.48e-23

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


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 95.66  E-value: 2.48e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLM---LDKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH 121
Cdd:cd14085  127 ENLLyatPAPDAPLKIADFGLSKI-VDQQVTMKTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDERG 205
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912019 122 EK-LFELILMEDIKFPR----TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFSGVN 179
Cdd:cd14085  206 DQyMFKRILNCDYDFVSpwwdDVSLNAKDLVKKLIVLDPKKRL-----TTQQALQHPWVTGKA 263
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
40-175 2.76e-23

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


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 94.98  E-value: 2.76e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLE----DND--YGRAVDWWGLGVVMYEMMCGR 113
Cdd:cd14182  134 RDLKPENILLDDDMNIKLTDFGFSCQ-LDPGEKLREVCGTPGYLAPEIIEcsmdDNHpgYGKEVDMWSTGVIMYTLLAGS 212
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912019 114 LPFYNQDHEKLFELILMEDIKFPR----TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd14182  213 PPFWHRKQMLMLRMIMSGNYQFGSpewdDRSDTVKDLISRFLVVQPQKRY-----TAEEALAHPFF 273
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
40-210 3.16e-23

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


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 95.88  E-value: 3.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCkegiTDAATMKTFC--GTPEYLAPEVLEDN-DYGRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd14223  127 RDLKPANILLDEFGHVRISDLGLA----CDFSKKKPHAsvGTHGYMAPEVLQKGvAYDSSADWFSLGCMLFKLLRGHSPF 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 117 YN---QDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFK 193
Cdd:cd14223  203 RQhktKDKHEIDRMTLTMAVELPDSFSPELRSLLEGLLQRDVNRRLGCMGRGAQEVKEEPFFRGLDWQMVFLQKYPPPLI 282
                        170       180
                 ....*....|....*....|..
gi 767912019 194 P-----QVTSETDTRYFDEEFT 210
Cdd:cd14223  283 PprgevNAADAFDIGSFDEEDT 304
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
40-174 4.72e-23

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 94.32  E-value: 4.72e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLD---KDGHIKITDFGLCKegiTDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd14088  123 RNLKLENLVYYnrlKNSKIVISDFHLAK---LENGLIKEPCGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPF 199
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 117 YN-------QDHEK-LFELILMEDIKFPR----TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSF 174
Cdd:cd14088  200 YDeaeeddyENHDKnLFRKILAGDYEFDSpywdDISQAAKDLVTRLMEVEQDQRI-----TAEEAISHEW 264
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
41-173 1.62e-22

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: 91.56  E-value: 1.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  41 NISLENLMLDKDGHIKITDFGLCK--EGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMmcgrlpfyn 118
Cdd:cd00180  117 DLKPENILLDSDGTVKLADFGLAKdlDSDDSLLKTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL--------- 187
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767912019 119 qdheklfelilmedikfprtlsSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHS 173
Cdd:cd00180  188 ----------------------EELKDLIRRMLQYDPKKRP-----SAKELLEHL 215
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
16-159 1.66e-22

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 92.75  E-value: 1.66e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  16 QRTAKE---DIALpyKIRFRFDLQAPPKNISLENLML---DKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLE 89
Cdd:cd14172  102 EREASEimrDIGT--AIQYLHSMNIAHRDVKPENLLYtskEKDAVLKLTDFGFAKE-TTVQNALQTPCYTPYYVAPEVLG 178
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912019  90 DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLF----ELILMEDIKFPR----TLSSDAKSLLSGLLIKDPNKRL 159
Cdd:cd14172  179 PEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAISpgmkRRIRMGQYGFPNpewaEVSEEAKQLIRHLLKTDPTERM 256
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
16-191 1.85e-22

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 92.62  E-value: 1.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  16 QRTAKEDIALPYKIRFRFDLQAPPKNISLENLMLDKDGHIKITDFGLCKEgiTDAATMKTFCGTPEYLAPEVLEDNDYGR 95
Cdd:cd14117  106 QRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSVH--APSLRRRTMCGTLDYLPPEMIEGRTHDE 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  96 AVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSff 175
Cdd:cd14117  184 KVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFPPFLSDGSRDLISKLLRYHPSERL-----PLKGVMEHP-- 256
                        170
                 ....*....|....*.
gi 767912019 176 sgvnWQDVYDKKLVPP 191
Cdd:cd14117  257 ----WVKANSRRVLPP 268
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
42-246 1.93e-22

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 94.42  E-value: 1.93e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  42 ISLENLMLDKDGH-IKITDFGLCKE------GITDAATMKTFCGTPEYLAPEVLEDN---DYGRAVDWWGLGVVMYEMMC 111
Cdd:COG0515  127 IKPENILLDRDGRvVKLIDFGLAKLlpdpgsTSSIPALPSTSVGTPGYMAPEVLLGLslaYASSSSDIWSLGITLYELLT 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 112 GRLPFYNQDHEKLFELIL-------------MEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGV 178
Cdd:COG0515  207 GLPPFEGEKNSSATSQTLkiilelptpslasPLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKES 286
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912019 179 NWQD-------VYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEKYDEDGMDCMDNERRPHFPQFSYSAS 246
Cdd:COG0515  287 DLSDllkpddsAPLRLSLPPSLEALISSLNSLAISGSDLKLDDSNFSKELAPNGVSSSPHNSSSLLLSTASSKRS 361
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
45-172 4.17e-22

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: 91.44  E-value: 4.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGH---IKITDFGLCKEGI-TDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD 120
Cdd:cd14087  126 ENLLYYHPGPdskIMITDFGLASTRKkGPNCLMKTTCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDN 205
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767912019 121 HEKLFELILMEDIKFP----RTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRH 172
Cdd:cd14087  206 RTRLYRQILRAKYSYSgepwPSVSNLAKDFIDRLLTVNPGERL-----SATQALKH 256
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
40-207 1.03e-21

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 92.43  E-value: 1.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKeGITDAATMKTF------------------------------------CGTPEYL 83
Cdd:cd05627  126 RDIKPDNLLLDAKGHVKLSDFGLCT-GLKKAHRTEFYrnlthnppsdfsfqnmnskrkaetwkknrrqlaystVGTPDYI 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  84 APEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL--MEDIKFPRT--LSSDAKSLLSGLLIkDPNKRL 159
Cdd:cd05627  205 APEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQETYRKVMnwKETLVFPPEvpISEKAKDLILRFCT-DAENRI 283
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 767912019 160 GGGPDDakEIMRHSFFSGVNWQDVYDKKLVPPFkpQVTSETDTRYFDE 207
Cdd:cd05627  284 GSNGVE--EIKSHPFFEGVDWEHIRERPAAIPI--EIKSIDDTSNFDD 327
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
46-175 1.58e-21

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: 90.11  E-value: 1.58e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFG----LCKEGITDAATMKTFCGTPEYLAPEVLE-DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD 120
Cdd:cd06610  132 NILLGEDGSVKIADFGvsasLATGGDRTRKVRKTFVGTPCWMAPEVMEqVRGYDFKADIWSFGITAIELATGAAPYSKYP 211
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912019 121 HEKLFELILMEDikfPRTLSSDA---------KSLLSGLLIKDPNKRlgggPdDAKEIMRHSFF 175
Cdd:cd06610  212 PMKVLMLTLQND---PPSLETGAdykkysksfRKMISLCLQKDPSKR----P-TAEELLKHKFF 267
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
40-175 1.96e-21

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 90.03  E-value: 1.96e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGL-CKegITDAATMKTFCGTPEYLAPEVLE------DNDYGRAVDWWGLGVVMYEMMCG 112
Cdd:cd14181  140 RDLKPENILLDDQLHIKLSDFGFsCH--LEPGEKLRELCGTPGYLAPEILKcsmdetHPGYGKEVDLWACGVILFTLLAG 217
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912019 113 RLPFYNQDHEKLFELILMEDIKFPR----TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd14181  218 SPPFWHRRQMLMLRMIMEGRYQFSSpewdDRSSTVKDLISRLLVVDPEIRL-----TAEQALQHPFF 279
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
42-176 2.03e-21

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 89.92  E-value: 2.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  42 ISLENLMLD-KDGHIKITDFGLCK----EGITDaatmktfcGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:PHA03390 135 IKLENVLYDrAKDRIYLCDYGLCKiigtPSCYD--------GTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPF 206
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912019 117 YNqDHEKLFELILME-----DIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpDDAKEIMRHSFFS 176
Cdd:PHA03390 207 KE-DEDEELDLESLLkrqqkKLPFIKNVSKNANDFVQSMLKYNINYRL----TNYNEIIKHPFLK 266
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
40-159 2.28e-21

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


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 90.48  E-value: 2.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLML---DKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd14179  126 RDLKPENLLFtdeSDNSEIKIIDFGFARLKPPDNQPLKTPCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPF 205
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767912019 117 YNQDH-------EKLFELILMEDIKFP----RTLSSDAKSLLSGLLIKDPNKRL 159
Cdd:cd14179  206 QCHDKsltctsaEEIMKKIKQGDFSFEgeawKNVSQEAKDLIQGLLTVDPNKRI 259
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
42-175 3.84e-21

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: 88.90  E-value: 3.84e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  42 ISLENLMLDKDGHIKITDFGLCkEGITDAATMKT-----FCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLP 115
Cdd:cd13994  124 LKPENILLDEDGVLKLTDFGTA-EVFGMPAEKESpmsagLCGSEPYMAPEVFTSGSYdGRAVDVWSCGIVLFALFTGRFP 202
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912019 116 F-YNQDHEKLFELILMEDIKFPRTLS-------SDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd13994  203 WrSAKKSDSAYKAYEKSGDFTNGPYEpienllpSECRRLIYRMLHPDPEKRI-----TIDEALNDPWV 265
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
33-159 6.64e-21

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 88.11  E-value: 6.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  33 FDLQapPKNI---SLENLMLdkdghiKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEM 109
Cdd:cd14121  119 MDLK--PQNLllsSRYNPVL------KLADFGFAQH-LKPNDEAHSLRGSPLYMAPEMILKKKYDARVDLWSVGVILYEC 189
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767912019 110 MCGRLPFYNQDHEKLFELILMED-IKFPRT--LSSDAKSLLSGLLIKDPNKRL 159
Cdd:cd14121  190 LFGRAPFASRSFEELEEKIRSSKpIEIPTRpeLSADCRDLLLRLLQRDPDRRI 242
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
40-175 7.98e-21

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 88.27  E-value: 7.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd06648  127 RDIKSDSILLTSDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNE 206
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767912019 120 DHEKLFELI---LMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd06648  207 PPLQAMKRIrdnEPPKLKNLHKVSPRLRSFLDRMLVRDPAQRA-----TAAELLNHPFL 260
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
40-207 1.16e-20

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 89.33  E-value: 1.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKeGITDAATMKTF------------------------------------CGTPEYL 83
Cdd:cd05628  125 RDIKPDNLLLDSKGHVKLSDFGLCT-GLKKAHRTEFYrnlnhslpsdftfqnmnskrkaetwkrnrrqlafstVGTPDYI 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  84 APEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL--MEDIKFPRT--LSSDAKSLLSGLLIKDPNKRl 159
Cdd:cd05628  204 APEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQETYKKVMnwKETLIFPPEvpISEKAKDLILRFCCEWEHRI- 282
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 767912019 160 ggGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFkpQVTSETDTRYFDE 207
Cdd:cd05628  283 --GAPGVEEIKTNPFFEGVDWEHIRERPAAIPI--EIKSIDDTSNFDE 326
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
40-159 1.27e-20

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: 87.61  E-value: 1.27e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd14186  126 RDLTLSNLLLTRNMNIKIADFGLATQLKMPHEKHFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTD 205
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767912019 120 DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRL 159
Cdd:cd14186  206 TVKNTLNKVVLADYEMPAFLSREAQDLIHQLLRKNPADRL 245
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
45-159 1.73e-20

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: 88.13  E-value: 1.73e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLML---DKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVL----EDNDYGRAVDWWGLGVVMYEMMCGRLPF- 116
Cdd:cd14092  128 ENLLFtdeDDDAEIKIVDFGFARL-KPENQPLKTPCFTLPYAAPEVLkqalSTQGYDESCDLWSLGVILYTMLSGQVPFq 206
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767912019 117 ---YNQDHEKLFELILMEDIKFP----RTLSSDAKSLLSGLLIKDPNKRL 159
Cdd:cd14092  207 spsRNESAAEIMKRIKSGDFSFDgeewKNVSSEAKSLIQGLLTVDPSKRL 256
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
29-175 2.49e-20

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: 87.47  E-value: 2.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  29 IRFRFDLQAPPKNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYE 108
Cdd:cd06654  129 LEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIE 208
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 109 MMCGRLPFYNQDHEKLFELILME---DIKFPRTLSSDAKSLLSGLLIKDPNKRlgggpDDAKEIMRHSFF 175
Cdd:cd06654  209 MIEGEPPYLNENPLRALYLIATNgtpELQNPEKLSAIFRDFLNRCLEMDVEKR-----GSAKELLQHQFL 273
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
40-175 2.76e-20

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: 86.90  E-value: 2.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd06647  127 RDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNE 206
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767912019 120 DHEKLFELILME---DIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd06647  207 NPLRALYLIATNgtpELQNPEKLSAIFRDFLNRCLEMDVEKRG-----SAKELLQHPFL 260
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
34-200 3.77e-20

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: 86.92  E-value: 3.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  34 DLQapPKNIslenLMLDKDGH---IKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMM 110
Cdd:cd14091  119 DLK--PSNI----LYADESGDpesLRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKKQGYDAACDIWSLGVLLYTML 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 111 CGRLPFYNQDHEKLfELIL--MEDIKFP------RTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFsgVNWQD 182
Cdd:cd14091  193 AGYTPFASGPNDTP-EVILarIGSGKIDlsggnwDHVSDSAKDLVRKMLHVDPSQRP-----TAAQVLQHPWI--RNRDS 264
                        170
                 ....*....|....*...
gi 767912019 183 VYDKKLVPPFKPQVTSET 200
Cdd:cd14091  265 LPQRQLTDPQDAALVKGA 282
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
40-160 5.33e-20

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: 86.54  E-value: 5.33e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDY---GRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd14200  148 RDIKPSNLLLGDDGHVKIADFGVSNQFEGNDALLSSTAGTPAFMAPETLSDSGQsfsGKALDVWAMGVTLYCFVYGKCPF 227
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767912019 117 YNQDHEKLFELILMEDIKFPR--TLSSDAKSLLSGLLIKDPNKRLG 160
Cdd:cd14200  228 IDEFILALHNKIKNKPVEFPEepEISEELKDLILKMLDKNPETRIT 273
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
40-158 5.77e-20

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 86.02  E-value: 5.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCK----EGITDAatMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLP 115
Cdd:cd14070  127 RDLKIENLLLDENDNIKLIDFGLSNcagiLGYSDP--FSTQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLP 204
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767912019 116 F------YNQDHEKlfeLILMEDIKFPRTLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd14070  205 FtvepfsLRALHQK---MVDKEMNPLPTDLSPGAISFLRSLLEPDPLKR 250
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
46-175 6.13e-20

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: 85.86  E-value: 6.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCKEGITDAAtmKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEK-- 123
Cdd:cd06605  130 NILVNSRGQVKLCDFGVSGQLVDSLA--KTFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPPPNAKPsm 207
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912019 124 -LFEL---ILMEDikfPRTL-----SSDAKSLLSGLLIKDPNKRlgggpDDAKEIMRHSFF 175
Cdd:cd06605  208 mIFELlsyIVDEP---PPLLpsgkfSPDFQDFVSQCLQKDPTER-----PSYKELMEHPFI 260
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
40-174 6.42e-20

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: 85.53  E-value: 6.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVL--EDNDYGRAVDWWGLGVVMYEMMCGRLPFY 117
Cdd:cd06632  126 RDIKGANILVDTNGVVKLADFGMAKH-VEAFSFAKSFKGSPYWMAPEVImqKNSGYGLAVDIWSLGCTVLEMATGKPPWS 204
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767912019 118 N-QDHEKLFELILMEDI-KFPRTLSSDAKSLLSGLLIKDPNKRlgggPdDAKEIMRHSF 174
Cdd:cd06632  205 QyEGVAAIFKIGNSGELpPIPDHLSPDAKDFIRLCLQRDPEDR----P-TASQLLEHPF 258
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
40-174 8.41e-20

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: 85.43  E-value: 8.41e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGlCKEGITDAATM------KTFCGTPEYLAPEVLEDND---YGRAVDWWGLGVVMYEMM 110
Cdd:cd06626  123 RDIKPANIFLDSNGLIKLGDFG-SAVKLKNNTTTmapgevNSLVGTPAYMAPEVITGNKgegHGRAADIWSLGCVVLEMA 201
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912019 111 CGRLPFYNQDHE--KLFELILMEDIKFPRTL--SSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSF 174
Cdd:cd06626  202 TGKRPWSELDNEwaIMYHVGMGHKPPIPDSLqlSPEGKDFLSRCLESDPKKRP-----TASELLDHPF 264
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
36-175 8.95e-20

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: 85.93  E-value: 8.95e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  36 QAPPKNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLP 115
Cdd:cd06656  135 QVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPP 214
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912019 116 FYNQDHEKLFELILME---DIKFPRTLSSDAKSLLSGLLIKDPNKRlgggpDDAKEIMRHSFF 175
Cdd:cd06656  215 YLNENPLRALYLIATNgtpELQNPERLSAVFRDFLNRCLEMDVDRR-----GSAKELLQHPFL 272
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
33-159 1.16e-19

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: 84.63  E-value: 1.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  33 FDLQapPKNIslenLMLDK-DGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC 111
Cdd:cd14006  113 LDLK--PENI----LLADRpSPQIKIIDFGLARK-LNPGEELKEIFGTPEFVAPEIVNGEPVSLATDMWSIGVLTYVLLS 185
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767912019 112 GRLPFYNQDHEKLFELILMEDIKFPRT----LSSDAKSLLSGLLIKDPNKRL 159
Cdd:cd14006  186 GLSPFLGEDDQETLANISACRVDFSEEyfssVSQEAKDFIRKLLVKEPRKRP 237
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
40-176 1.50e-19

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: 84.98  E-value: 1.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd14187  131 RDLKLGNLFLNDDMEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETS 210
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767912019 120 DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRlgggpDDAKEIMRHSFFS 176
Cdd:cd14187  211 CLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTAR-----PTINELLNDEFFT 262
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
34-158 1.69e-19

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 84.39  E-value: 1.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  34 DLQapPKNIslenLMLDKDGHIKITDFGLCKEGITdAATMKTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCG 112
Cdd:cd14074  128 DLK--PENV----VFFEKQGLVKLTDFGFSNKFQP-GEKLETSCGSLAYSAPEILLGDEYdAPAVDIWSLGVILYMLVCG 200
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767912019 113 RLPFYN-QDHEKlfeLILMEDIKF--PRTLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd14074  201 QPPFQEaNDSET---LTMIMDCKYtvPAHVSPECKDLIRRMLIRDPKKR 246
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
40-158 1.78e-19

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 86.61  E-value: 1.78e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEgITDAATM---KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:PTZ00267 193 RDLKSANIFLMPTGIIKLGDFGFSKQ-YSDSVSLdvaSSFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRPF 271
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767912019 117 YNQDHEKLFELILMEDIK-FPRTLSSDAKSLLSGLLIKDPNKR 158
Cdd:PTZ00267 272 KGPSQREIMQQVLYGKYDpFPCPVSSGMKALLDPLLSKNPALR 314
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
25-158 1.87e-19

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 84.66  E-value: 1.87e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  25 LPYKIRFRFDLQAPPKNISLENLML----DKDGHIKITDFGLCKegITDAAtMKTFCGTPEYLAPEVLEDNDYGRAVDWW 100
Cdd:cd14183  113 LASAIKYLHSLNIVHRDIKPENLLVyehqDGSKSLKLGDFGLAT--VVDGP-LYTVCGTPTYVAPEIIAETGYGLKVDIW 189
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912019 101 GLGVVMYEMMCGRLPF--YNQDHEKLFELILMEDIKFPR----TLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd14183  190 AAGVITYILLCGFPPFrgSGDDQEVLFDQILMGQVDFPSpywdNVSDSAKELITMMLQVDVDQR 253
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
33-174 2.47e-19

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 84.46  E-value: 2.47e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  33 FDLQapPKNIslenLMLDKD---GHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEM 109
Cdd:cd14105  132 FDLK--PENI----MLLDKNvpiPRIKLIDFGLAHK-IEDGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYIL 204
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 110 MCGRLPFYNQDHEKLFELIL-----MEDIKFPRTlSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSF 174
Cdd:cd14105  205 LSGASPFLGDTKQETLANITavnydFDDEYFSNT-SELAKDFIRQLLVKDPRKRM-----TIQESLRHPW 268
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
40-172 2.51e-19

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: 84.31  E-value: 2.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLML----DKDGHIKITDFGLCK--EGitdaaTMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGR 113
Cdd:cd14184  123 RDIKPENLLVceypDGTKSLKLGDFGLATvvEG-----PLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGF 197
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912019 114 LPFYNQDH--EKLFELILMEDIKFPR----TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRH 172
Cdd:cd14184  198 PPFRSENNlqEDLFDQILLGKLEFPSpywdNITDSAKELISHMLQVNVEARY-----TAEQILSH 257
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
46-175 6.13e-19

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: 83.17  E-value: 6.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCK--EGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN-QDHE 122
Cdd:cd06625  132 NILRDSNGNVKLGDFGASKrlQTICSSTGMKSVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEfEPMA 211
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767912019 123 KLFElILMEDIKF--PRTLSSDAKSLLSGLLIKDPNKRlgggPdDAKEIMRHSFF 175
Cdd:cd06625  212 AIFK-IATQPTNPqlPPHVSEDARDFLSLIFVRNKKQR----P-SAEELLSHSFV 260
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
36-175 6.98e-19

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: 83.62  E-value: 6.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  36 QAPPKNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLP 115
Cdd:cd06655  135 QVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPP 214
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912019 116 FYNQDHEKLFELILME---DIKFPRTLSSDAKSLLSGLLIKDPNKRlgggpDDAKEIMRHSFF 175
Cdd:cd06655  215 YLNENPLRALYLIATNgtpELQNPEKLSPIFRDFLNRCLEMDVEKR-----GSAKELLQHPFL 272
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
40-159 7.68e-19

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 83.22  E-value: 7.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNI-----SLENLMLDKDGH-IKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCG 112
Cdd:cd13974  151 KNIvhrdlKLGNMVLNKRTRkITITNFCLGKHLVSEDDLLKDQRGSPAYISPDVLSGKPYlGKPSDMWALGVVLFTMLYG 230
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767912019 113 RLPFYNQDHEKLFELILMEDIKFPRT--LSSDAKSLLSGLLIKDPNKRL 159
Cdd:cd13974  231 QFPFYDSIPQELFRKIKAAEYTIPEDgrVSENTVCLIRKLLVLNPQKRL 279
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
40-171 8.49e-19

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 82.46  E-value: 8.49e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd08529  125 RDIKSMNIFLDKGDNVKIGDLGVAKILSDTTNFAQTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQ 204
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767912019 120 DHEKLFELILMEDIK-FPRTLSSDAKSLLSGLLIKDPNKRlgggpDDAKEIMR 171
Cdd:cd08529  205 NQGALILKIVRGKYPpISASYSQDLSQLIDSCLTKDYRQR-----PDTTELLR 252
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
34-174 8.69e-19

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 82.47  E-value: 8.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  34 DLQAppKNISLENLMldkdghIKITDFGLCK--EGITDAATmkTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC 111
Cdd:cd08222  131 DLKA--KNIFLKNNV------IKVGDFGISRilMGTSDLAT--TFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCC 200
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912019 112 GRLPFYNQDHEKLFELILMEDI-KFPRTLSSDAKSLLSGLLIKDPNKRlgggpDDAKEIMRHSF 174
Cdd:cd08222  201 LKHAFDGQNLLSVMYKIVEGETpSLPDKYSKELNAIYSRMLNKDPALR-----PSAAEILKIPF 259
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
40-206 1.37e-18

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 83.56  E-value: 1.37e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLC------------------KEGITD-----------------------AATMKTFC- 77
Cdd:cd05625  125 RDIKPDNILIDRDGHIKLTDFGLCtgfrwthdskyyqsgdhlRQDSMDfsnewgdpencrcgdrlkplerrAARQHQRCl 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  78 -----GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKlfelILMEDIKFPRTLSSDAKSLL----S 148
Cdd:cd05625  205 ahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPPFLAQTPLE----TQMKVINWQTSLHIPPQAKLspeaS 280
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912019 149 GLLIK---DPNKRLggGPDDAKEIMRHSFFSGVNWQDvyDKKLVP-PFKPQVTSETDTRYFD 206
Cdd:cd05625  281 DLIIKlcrGPEDRL--GKNGADEIKAHPFFKTIDFSS--DLRQQSaPYIPKITHPTDTSNFD 338
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
40-160 1.42e-18

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 82.05  E-value: 1.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAAtmKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd08530  127 RDLKSANILLSAGDLVKIGDLGISKVLKKNLA--KTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEAR 204
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 767912019 120 DHEKLFELILMEdiKFPR---TLSSDAKSLLSGLLIKDPNKRLG 160
Cdd:cd08530  205 TMQELRYKVCRG--KFPPippVYSQDLQQIIRSLLQVNPKKRPS 246
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
40-206 1.57e-18

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 83.52  E-value: 1.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCK----------------------------------------EGITDAATMK----- 74
Cdd:cd05626  125 RDIKPDNILIDLDGHIKLTDFGLCTgfrwthnskyyqkgshirqdsmepsdlwddvsncrcgdrlKTLEQRATKQhqrcl 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  75 --TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN-QDHEKLFELILMED-IKFPR--TLSSDAKSLLS 148
Cdd:cd05626  205 ahSLVGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEMLVGQPPFLApTPTETQLKVINWENtLHIPPqvKLSPEAVDLIT 284
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767912019 149 GLLIKdPNKRLGGgpDDAKEIMRHSFFSGVNWQDvyDKKLVP-PFKPQVTSETDTRYFD 206
Cdd:cd05626  285 KLCCS-AEERLGR--NGADDIKAHPFFSEVDFSS--DIRTQPaPYVPKISHPMDTSNFD 338
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
40-176 1.61e-18

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


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 82.38  E-value: 1.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd06657  140 RDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNE 219
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 120 DHEKLFELI---LMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFS 176
Cdd:cd06657  220 PPLKAMKMIrdnLPPKLKNLHKVSPSLKGFLDRLLVRDPAQRA-----TAAELLKHPFLA 274
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
65-175 2.59e-18

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


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 80.94  E-value: 2.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  65 EGITDAATMKTFCgtPEYLAPEVLEDNDY--GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSD 142
Cdd:cd13976  137 EGEDDSLSDKHGC--PAYVSPEILNSGATysGKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRRGQFAIPETLSPR 214
                         90       100       110
                 ....*....|....*....|....*....|...
gi 767912019 143 AKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd13976  215 ARCLIRSLLRREPSERL-----TAEDILLHPWL 242
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
45-175 4.42e-18

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: 80.36  E-value: 4.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLD-KDGHIKITDFGLCKEGITDAATmkTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRlPFYNQDHE 122
Cdd:cd05118  130 ENILINlELGQLKLADFGLARSFTSPPYT--PYVATRWYRAPEVlLGAKPYGSSIDIWSLGCILAELLTGR-PLFPGDSE 206
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767912019 123 kLFELILMEDIKFPrtlsSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd05118  207 -VDQLAKIVRLLGT----PEALDLLSKMLKYDPAKRI-----TASQALAHPYF 249
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
29-159 4.92e-18

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: 81.23  E-value: 4.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  29 IRFRFDLQAPPKNISLENLMLDK---DGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVV 105
Cdd:cd14170  114 IQYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFGFAKE-TTSHNSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVI 192
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912019 106 MYEMMCGRLPFYNQD----HEKLFELILMEDIKFPRT----LSSDAKSLLSGLLIKDPNKRL 159
Cdd:cd14170  193 MYILLCGYPPFYSNHglaiSPGMKTRIRMGQYEFPNPewseVSEEVKMLIRNLLKTEPTQRM 254
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
34-172 5.54e-18

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: 80.92  E-value: 5.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  34 DLQapPKNISLENLmlDKDGHIKITDFGL---CKEGITDAATMKTF-----CGTPEYLAPEVL-----EDNDYGRAVDWW 100
Cdd:cd14090  125 DLK--PENILCESM--DKVSPVKICDFDLgsgIKLSSTSMTPVTTPelltpVGSAEYMAPEVVdafvgEALSYDKRCDLW 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 101 GLGVVMYEMMCGRLPFYN--------------QD-HEKLFELILMEDIKFPRT----LSSDAKSLLSGLLIKDPNKRLgg 161
Cdd:cd14090  201 SLGVILYIMLCGYPPFYGrcgedcgwdrgeacQDcQELLFHSIQEGEYEFPEKewshISAEAKDLISHLLVRDASQRY-- 278
                        170
                 ....*....|.
gi 767912019 162 gpdDAKEIMRH 172
Cdd:cd14090  279 ---TAEQVLQH 286
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
45-175 8.85e-18

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: 80.09  E-value: 8.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLML---DKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH 121
Cdd:cd14106  137 QNILLtseFPLGDIKLCDFGISRV-IGEGEEIREILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDK 215
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767912019 122 EKLFELILMEDIKFPRTL----SSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd14106  216 QETFLNISQCNLDFPEELfkdvSPLAIDFIKRLLVKDPEKRL-----TAKECLEHPWL 268
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
33-174 1.15e-17

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 79.62  E-value: 1.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  33 FDLQapPKNIslenLMLDKDG---HIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEM 109
Cdd:cd14196  132 FDLK--PENI----MLLDKNIpipHIKLIDFGLAHE-IEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYIL 204
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912019 110 MCGRLPFYNQD-HEKLFELILME---DIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSF 174
Cdd:cd14196  205 LSGASPFLGDTkQETLANITAVSydfDEEFFSHTSELAKDFIRKLLVKETRKRL-----TIQEALRHPW 268
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
35-158 1.19e-17

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: 79.58  E-value: 1.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  35 LQAPPKNISLENLmlDKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRL 114
Cdd:cd14198  134 LDLKPQNILLSSI--YPLGDIKIVDFGMSRK-IGHACELREIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHES 210
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767912019 115 PFYNQDHEKLFELILMEDIKFPR----TLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd14198  211 PFVGEDNQETFLNISQVNVDYSEetfsSVSQLATDFIQKLLVKNPEKR 258
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
40-175 1.25e-17

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 80.08  E-value: 1.25e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd06658  142 RDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNE 221
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767912019 120 DHEKLFELI---LMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd06658  222 PPLQAMRRIrdnLPPRVKDSHKVSSVLRGFLDLMLVREPSQRA-----TAQELLQHPFL 275
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
40-159 1.42e-17

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: 79.62  E-value: 1.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLED---NDYGRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd14199  150 RDVKPSNLLVGEDGHIKIADFGVSNEFEGSDALLTNTVGTPAFMAPETLSEtrkIFSGKALDVWAMGVTLYCFVFGQCPF 229
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767912019 117 YNQDHEKLFELILMEDIKFPRT--LSSDAKSLLSGLLIKDPNKRL 159
Cdd:cd14199  230 MDERILSLHSKIKTQPLEFPDQpdISDDLKDLLFRMLDKNPESRI 274
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
39-183 1.99e-17

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: 79.30  E-value: 1.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  39 PKNIslenLMLDKDGH---IKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLP 115
Cdd:cd14175  123 PSNI----LYVDESGNpesLRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTP 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 116 FYNQDHEKLFELIL-MEDIKFP------RTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF--------SGVNW 180
Cdd:cd14175  199 FANGPSDTPEEILTrIGSGKFTlsggnwNTVSDAAKDLVSKMLHVDPHQRL-----TAKQVLQHPWItqkdklpqSQLNH 273

                 ...
gi 767912019 181 QDV 183
Cdd:cd14175  274 QDV 276
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
35-174 2.79e-17

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


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 78.27  E-value: 2.79e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  35 LQAPPKNISLENLMLDKD--GHIKITDFGLCKEGITDAATmKTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMC 111
Cdd:cd14662  115 MQICHRDLKLENTLLDGSpaPRLKICDFGYSKSSVLHSQP-KSTVGTPAYIAPEVLSRKEYdGKVADVWSCGVTLYVMLV 193
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912019 112 GRLPFYNQDHEKLF----ELILMEDIKFPR--TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSF 174
Cdd:cd14662  194 GAYPFEDPDDPKNFrktiQRIMSVQYKIPDyvRVSQDCRHLLSRIFVANPAKRI-----TIPEIKNHPW 257
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
50-172 2.99e-17

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: 79.12  E-value: 2.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  50 DKDGHIKITDFGLCKE--GITDAATMKTfcGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDhEKLFEL 127
Cdd:cd14094  146 ENSAPVKLGGFGVAIQlgESGLVAGGRV--GTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEG 222
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767912019 128 ILMEDIKF-PR---TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRH 172
Cdd:cd14094  223 IIKGKYKMnPRqwsHISESAKDLVRRMLMLDPAERI-----TVYEALNH 266
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
39-172 3.48e-17

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: 78.04  E-value: 3.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  39 PKNIslenLMLDKDGH-IKITDFGLCKEGITDAaTMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY 117
Cdd:cd14103  119 PENI----LCVSRTGNqIKIIDFGLARKYDPDK-KLKVLFGTPEFVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFM 193
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 118 NQDHEKLFELILM-----EDIKFpRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRH 172
Cdd:cd14103  194 GDNDAETLANVTRakwdfDDEAF-DDISDEAKDFISKLLVKDPRKRM-----SAAQCLQH 247
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
78-175 5.35e-17

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 77.38  E-value: 5.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  78 GTPEYLAPEVLEDNDY--GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDP 155
Cdd:cd14022  148 GCPAYVSPEILNTSGSysGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREP 227
                         90       100
                 ....*....|....*....|
gi 767912019 156 NKRLgggpdDAKEIMRHSFF 175
Cdd:cd14022  228 SERL-----TSQEILDHPWF 242
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
54-174 6.46e-17

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: 77.41  E-value: 6.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  54 HIKITDFGLCK--EGITDAATMktfCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL---FELI 128
Cdd:cd14120  139 RLKIADFGFARflQDGMMAATL---CGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQELkafYEKN 215
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767912019 129 LMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSF 174
Cdd:cd14120  216 ANLRPNIPSGTSPALKDLLLGLLKRNPKDRI-----DFEDFFSHPF 256
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
40-175 7.49e-17

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: 77.37  E-value: 7.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLC-------KEGITDAAtmktfCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMC 111
Cdd:cd14069  124 RDIKPENLLLDENDNLKISDFGLAtvfrykgKERLLNKM-----CGTLPYVAPELLAKKKYrAEPVDVWSCGIVLFAMLA 198
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912019 112 GRLPfYNQDHEKLFE-LILMEDIKFPRT----LSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd14069  199 GELP-WDQPSDSCQEySDWKENKKTYLTpwkkIDTAALSLLRKILTENPNKRI-----TIEDIKKHPWY 261
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
46-175 8.57e-17

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 76.92  E-value: 8.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQdheKLF 125
Cdd:cd06612  129 NILLNEEGQAKLADFGVSGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDI---HPM 205
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767912019 126 ELILMEDIKFPRTL------SSDAKSLLSGLLIKDPNKRlgggpDDAKEIMRHSFF 175
Cdd:cd06612  206 RAIFMIPNKPPPTLsdpekwSPEFNDFVKKCLVKDPEER-----PSAIQLLQHPFI 256
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
45-175 1.23e-16

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: 77.14  E-value: 1.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKE-GItdaaTMKTFcgTPE-----YLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRLPFY 117
Cdd:cd07829  127 QNLLINRDGVLKLADFGLARAfGI----PLRTY--THEvvtlwYRAPEILlGSKHYSTAVDIWSVGCIFAELITGKPLFP 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 118 NQDHE----KLFElIL---------------MEDIKFPR-----------TLSSDAKSLLSGLLIKDPNKRLgggpdDAK 167
Cdd:cd07829  201 GDSEIdqlfKIFQ-ILgtpteeswpgvtklpDYKPTFPKwpkndlekvlpRLDPEGIDLLSKMLQYNPAKRI-----SAK 274

                 ....*...
gi 767912019 168 EIMRHSFF 175
Cdd:cd07829  275 EALKHPYF 282
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
39-176 1.24e-16

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: 77.36  E-value: 1.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  39 PKNIslenLMLDKDGH---IKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLP 115
Cdd:cd14177  126 PSNI----LYMDDSANadsIRICDFGFAKQLRGENGLLLTPCYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTP 201
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912019 116 FYNQDHEKLFELIL-MEDIKFP------RTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFS 176
Cdd:cd14177  202 FANGPNDTPEEILLrIGSGKFSlsggnwDTVSDAAKDLLSHMLHVDPHQRY-----TAEQVLKHSWIA 264
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
46-175 1.31e-16

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 76.49  E-value: 1.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLckegitdAATMK-------TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN 118
Cdd:cd06627  129 NILTTKDGLVKLADFGV-------ATKLNevekdenSVVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYD 201
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767912019 119 QD-HEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRlgggpDDAKEIMRHSFF 175
Cdd:cd06627  202 LQpMAALFRIVQDDHPPLPENISPELRDFLLQCFQKDPTLR-----PSAKELLKHPWL 254
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
39-172 2.01e-16

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: 77.37  E-value: 2.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  39 PKNIslenLMLDKDGH---IKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLP 115
Cdd:cd14176  141 PSNI----LYVDESGNpesIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTP 216
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912019 116 FYNQDHEKLFELIL-MEDIKFPRT------LSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRH 172
Cdd:cd14176  217 FANGPDDTPEEILArIGSGKFSLSggywnsVSDTAKDLVSKMLHVDPHQRL-----TAALVLRH 275
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
33-159 2.03e-16

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 76.21  E-value: 2.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  33 FDLQapPKNIslenLMLDKDG---HIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEM 109
Cdd:cd14194  132 FDLK--PENI----MLLDRNVpkpRIKIIDFGLAHK-IDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYIL 204
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767912019 110 MCGRLPFYNQDHEKLFELILMEDIKFPRTLSSD----AKSLLSGLLIKDPNKRL 159
Cdd:cd14194  205 LSGASPFLGDTKQETLANVSAVNYEFEDEYFSNtsalAKDFIRRLLVKDPKKRM 258
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
40-175 2.21e-16

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 76.56  E-value: 2.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd06659  141 RDIKSDSILLTLDGRVKLSDFGFCAQISKDVPKRKSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSD 220
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767912019 120 DHEKLFELILME---DIKFPRTLSSDAKSLLSGLLIKDPNKRlgggpDDAKEIMRHSFF 175
Cdd:cd06659  221 SPVQAMKRLRDSpppKLKNSHKASPVLRDFLERMLVRDPQER-----ATAQELLDHPFL 274
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
45-159 3.13e-16

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: 76.45  E-value: 3.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGH---IKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD- 120
Cdd:cd14180  130 ENILYADESDgavLKVIDFGFARLRPQGSRPLQTPCFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRg 209
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767912019 121 ---HEKLFEliLMEDIKFPR---------TLSSDAKSLLSGLLIKDPNKRL 159
Cdd:cd14180  210 kmfHNHAAD--IMHKIKEGDfslegeawkGVSEEAKDLVRGLLTVDPAKRL 258
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
35-159 8.93e-16

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


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 74.25  E-value: 8.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  35 LQAPPKNISLENLMLDKDG--HIKITDFGLCKEGITDAATmKTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMC 111
Cdd:cd14665  115 MQICHRDLKLENTLLDGSPapRLKICDFGYSKSSVLHSQP-KSTVGTPAYIAPEVLLKKEYdGKIADVWSCGVTLYVMLV 193
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767912019 112 GRLPFYN----QDHEKLFELILMEDIKFPRT--LSSDAKSLLSGLLIKDPNKRL 159
Cdd:cd14665  194 GAYPFEDpeepRNFRKTIQRILSVQYSIPDYvhISPECRHLISRIFVADPATRI 247
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
42-174 1.10e-15

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: 74.20  E-value: 1.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  42 ISLENLMLDKDGHIKITDFGLCKEgITDAAT-MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD 120
Cdd:cd06609  124 IKAANILLSEEGDVKLADFGVSGQ-LTSTMSkRNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLH 202
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 121 HEKLFELI------LMEDIKFprtlSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSF 174
Cdd:cd06609  203 PMRVLFLIpknnppSLEGNKF----SKPFKDFVELCLNKDPKERP-----SAKELLKHKF 253
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
40-172 1.13e-15

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 74.42  E-value: 1.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDK---DGHIKITDFGLCKEgitDAATMKTFCGTPEYLAPEVLEDND-----------------YGRAVDW 99
Cdd:cd14171  133 RDLKPENLLLKDnseDAPIKLCDFGFAKV---DQGDLMTPQFTPYYVAPQVLEAQRrhrkersgiptsptpytYDKSCDM 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 100 WGLGVVMYEMMCGRLPFYNQDHEK-----LFELILMEDIKFP----RTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIM 170
Cdd:cd14171  210 WSLGVIIYIMLCGYPPFYSEHPSRtitkdMKRKIMTGSYEFPeeewSQISEMAKDIVRKLLCVDPEERM-----TIEEVL 284

                 ..
gi 767912019 171 RH 172
Cdd:cd14171  285 HH 286
S_TK_X smart00133
Extension to Ser/Thr-type protein kinases;
176-245 1.30e-15

Extension to Ser/Thr-type protein kinases;


Pssm-ID: 214529  Cd Length: 64  Bit Score: 68.93  E-value: 1.30e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019   176 SGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEKYDEDGMDcmdnerRPHFPQFSYSA 245
Cdd:smart00133   1 RGIDWDKLENKEIEPPFVPKIKSPTDTSNFDPEFTEETPVLTPVDSPLSGGIQ------QEPFRGFSYVF 64
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
53-174 1.47e-15

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: 73.98  E-value: 1.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  53 GHIKITDFGLCKE--GITDAAtmKTFCGTPEYLAPEVLEDN--DYGRAVDWWGLGVVMYEMMCGRLPFYN--QDHEKLFE 126
Cdd:cd06624  146 GVVKISDFGTSKRlaGINPCT--ETFTGTLQYMAPEVIDKGqrGYGPPADIWSLGCTIIEMATGKPPFIElgEPQAAMFK 223
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767912019 127 LILME---DIkfPRTLSSDAKSLLSGLLIKDPNKRLGggpddAKEIMRHSF 174
Cdd:cd06624  224 VGMFKihpEI--PESLSEEAKSFILRCFEPDPDKRAT-----ASDLLQDPF 267
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
40-158 2.03e-15

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 74.91  E-value: 2.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKegiTDAATM-----KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRL 114
Cdd:PTZ00283 167 RDIKSANILLCSNGLVKLGDFGFSK---MYAATVsddvgRTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKR 243
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767912019 115 PFYNQDHEKLFELILMEDIK-FPRTLSSDAKSLLSGLLIKDPNKR 158
Cdd:PTZ00283 244 PFDGENMEEVMHKTLAGRYDpLPPSISPEMQEIVTALLSSDPKRR 288
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
14-175 2.84e-15

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: 73.12  E-value: 2.84e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  14 LLQRTAKEDIALPYKIRFRFDLQapPKNISLENLMLDKDG----HIKITDFGLCK--EGITDAATMktfCGTPEYLAPEV 87
Cdd:cd14202  106 FLQQIAGAMKMLHSKGIIHRDLK--PQNILLSYSGGRKSNpnniRIKIADFGFARylQNNMMAATL---CGSPMYMAPEV 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  88 LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN---QDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpd 164
Cdd:cd14202  181 IMSQHYDAKADLWSIGTIIYQCLTGKAPFQAsspQDLRLFYEKNKSLSPNIPRETSSHLRQLLLGLLQRNQKDRM----- 255
                        170
                 ....*....|.
gi 767912019 165 DAKEIMRHSFF 175
Cdd:cd14202  256 DFDEFFHHPFL 266
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
42-175 3.16e-15

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 72.77  E-value: 3.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  42 ISLENLmldKDGHIKitdfglckEGITDAATMKTFCgtPEYLAPEVLEDNDY--GRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd14023  125 LRLESL---EDTHIM--------KGEDDALSDKHGC--PAYVSPEILNTTGTysGKSADVWSLGVMLYTLLVGRYPFHDS 191
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767912019 120 DHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd14023  192 DPSALFSKIRRGQFCIPDHVSPKARCLIRSLLRREPSERL-----TAPEILLHPWF 242
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
39-174 3.84e-15

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: 73.14  E-value: 3.84e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  39 PKNISLENLmlDKDGHIKITDFGL---------CKEGITDAATmkTFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGV 104
Cdd:cd14174  128 PENILCESP--DKVSPVKICDFDLgsgvklnsaCTPITTPELT--TPCGSAEYMAPEVVEvftdeATFYDKRCDLWSLGV 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 105 VMYEMMCGRLPFYNQ---------------DHEKLFELILMEDIKFPRT----LSSDAKSLLSGLLIKDPNKRLgggpdD 165
Cdd:cd14174  204 ILYIMLSGYPPFVGHcgtdcgwdrgevcrvCQNKLFESIQEGKYEFPDKdwshISSEAKDLISKLLVRDAKERL-----S 278

                 ....*....
gi 767912019 166 AKEIMRHSF 174
Cdd:cd14174  279 AAQVLQHPW 287
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
46-210 4.02e-15

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: 73.33  E-value: 4.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCKEGITD-AATMKTfcgtpEYL------APEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFY 117
Cdd:cd07834  133 NILVNSNCDLKICDFGLARGVDPDeDKGFLT-----EYVvtrwyrAPELlLSSKKYTKAIDIWSVGCIFAELLTRKPLFP 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 118 NQDHEKLFELIL-------MEDIKFPR------------------------TLSSDAKSLLSGLLIKDPNKRLgggpdDA 166
Cdd:cd07834  208 GRDYIDQLNLIVevlgtpsEEDLKFISsekarnylkslpkkpkkplsevfpGASPEAIDLLEKMLVFNPKKRI-----TA 282
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 767912019 167 KEIMRHSFFsgvnwQDVYDKKLVPPFKPQVTSEtdtRYFDEEFT 210
Cdd:cd07834  283 DEALAHPYL-----AQLHDPEDEPVAKPPFDFP---FFDDEELT 318
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
45-172 4.49e-15

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


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 72.66  E-value: 4.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKD---GHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH 121
Cdd:cd14197  140 QNILLTSEsplGDIKIVDFGLSRI-LKNSEELREIMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDK 218
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767912019 122 EKLFELILMEDIKFPRT----LSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRH 172
Cdd:cd14197  219 QETFLNISQMNVSYSEEefehLSESAIDFIKTLLIKKPENRA-----TAEDCLKH 268
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
40-158 6.98e-15

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 71.77  E-value: 6.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd08218  125 RDIKSQNIFLTKDGIIKLGDFGIARVLNSTVELARTCIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAG 204
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767912019 120 DHEKL-FELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd08218  205 NMKNLvLKIIRGSYPPVPSRYSYDLRSLVSQLFKRNPRDR 244
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
39-174 8.62e-15

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: 71.97  E-value: 8.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  39 PKNIslenLMLDKDGH---IKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLP 115
Cdd:cd14178  125 PSNI----LYMDESGNpesIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTP 200
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912019 116 FYNQDHEKLFELIL-MEDIKFPRT------LSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSF 174
Cdd:cd14178  201 FANGPDDTPEEILArIGSGKYALSggnwdsISDAAKDIVSKMLHVDPHQRL-----TAPQVLRHPW 261
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
35-162 1.02e-14

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: 71.49  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  35 LQAPPKNIslenLMLDKDGH-IKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGR 113
Cdd:cd14190  126 LDLKPENI----LCVNRTGHqVKIIDFGLARR-YNPREKLKVNFGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGL 200
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767912019 114 LPFYNQDHEKLFELILMEDIKFP----RTLSSDAKSLLSGLLIKDPNKRLGGG 162
Cdd:cd14190  201 SPFLGDDDTETLNNVLMGNWYFDeetfEHVSDEAKDFVSNLIIKERSARMSAT 253
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
45-159 1.05e-14

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: 71.57  E-value: 1.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLM-LDKDG-HIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY-NQDH 121
Cdd:cd14191  129 ENIMcVNKTGtKIKLIDFGLARR-LENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMgDNDN 207
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767912019 122 EKLFELIL----MEDIKFPRtLSSDAKSLLSGLLIKDPNKRL 159
Cdd:cd14191  208 ETLANVTSatwdFDDEAFDE-ISDDAKDFISNLLKKDMKARL 248
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
40-174 1.10e-14

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: 71.74  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFyn 118
Cdd:cd06917  125 RDIKAANILVTNTGNVKLCDFGVAASLNQNSSKRSTFVGTPYWMAPEViTEGKYYDTKADIWSLGITTYEMATGNPPY-- 202
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 119 QDHEKLFELILMEDIKFPR----TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSF 174
Cdd:cd06917  203 SDVDALRAVMLIPKSKPPRlegnGYSPLLKEFVAACLDEEPKDRL-----SADELLKSKW 257
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
46-175 1.40e-14

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: 71.31  E-value: 1.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDG-HIKITDFGLCKE---GITDAATMK-TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD 120
Cdd:cd06630  133 NLLVDSTGqRLRIADFGAAARlasKGTGAGEFQgQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEK 212
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 121 HEKLFELIL-----MEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGggpddAKEIMRHSFF 175
Cdd:cd06630  213 ISNHLALIFkiasaTTPPPIPEHLSPGLRDVTLRCLELQPEDRPP-----ARELLKHPVF 267
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
46-187 1.89e-14

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 70.93  E-value: 1.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVL-----EDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD 120
Cdd:cd06611  133 NILLTLDGDVKLADFGVSAKNKSTLQKRDTFIGTPYWMAPEVVacetfKDNPYDYKADIWSLGITLIELAQMEPPHHELN 212
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 121 HEKLFELILMED---IKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFSgvnwqDVYDKK 187
Cdd:cd06611  213 PMRVLLKILKSEpptLDQPSKWSSSFNDFLKSCLVKDPDDRP-----TAAELLKHPFVS-----DQSDNK 272
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
46-174 2.25e-14

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: 70.54  E-value: 2.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFG----LCKEG--ITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLP---- 115
Cdd:cd06631  133 NIMLMPNGVIKLIDFGcakrLCINLssGSQSQLLKSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPwadm 212
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912019 116 ------FYNQDHEKLFElilmediKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSF 174
Cdd:cd06631  213 npmaaiFAIGSGRKPVP-------RLPDKFSPEARDFVHACLTRDQDERP-----SAEQLLKHPF 265
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
46-175 2.85e-14

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 70.03  E-value: 2.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDND---YGRAVDWWGLGVVMYEMMCGRLPFYNQDHE 122
Cdd:cd06613  127 NILLTEDGDVKLADFGVSAQLTATIAKRKSFIGTPYWMAPEVAAVERkggYDGKCDIWALGITAIELAELQPPMFDLHPM 206
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767912019 123 KLFELILMEDIKfPRTL------SSDAKSLLSGLLIKDPNKRlgggPdDAKEIMRHSFF 175
Cdd:cd06613  207 RALFLIPKSNFD-PPKLkdkekwSPDFHDFIKKCLTKNPKKR----P-TATKLLQHPFV 259
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
78-172 4.69e-14

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB3 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 69.14  E-value: 4.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  78 GTPEYLAPEVLED--NDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDP 155
Cdd:cd14024  148 GCPAYVGPEILSSrrSYSGKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIRRGAFSLPAWLSPGARCLVSCMLRRSP 227
                         90
                 ....*....|....*..
gi 767912019 156 NKRLgggpdDAKEIMRH 172
Cdd:cd14024  228 AERL-----KASEILLH 239
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
40-164 5.21e-14

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: 69.45  E-value: 5.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY-- 117
Cdd:cd08528  138 RDLKPNNIMLGEDDKVTITDFGLAKQKGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYst 217
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767912019 118 ----------NQDHEKLFELILMEDIKFprtlssdaksLLSGLLIKDPNKRlgggPD 164
Cdd:cd08528  218 nmltlatkivEAEYEPLPEGMYSDDITF----------VIRSCLTPDPEAR----PD 260
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
40-174 5.89e-14

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: 69.49  E-value: 5.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKT------FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGR 113
Cdd:cd06628  130 RDIKGANILVDNKGGIKISDFGISKKLEANSLSTKNngarpsLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGT 209
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912019 114 LPFYNQDH-EKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRlgggpDDAKEIMRHSF 174
Cdd:cd06628  210 HPFPDCTQmQAIFKIGENASPTIPSNISSEARDFLEKTFEIDHNKR-----PTADELLKHPF 266
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
27-120 8.59e-14

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 68.68  E-value: 8.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  27 YKIRFRfDLQAPpknisleNLMLDKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVM 106
Cdd:cd14059  100 HKIIHR-DLKSP-------NVLVTYNDVLKISDFGTSKE-LSEKSTKMSFAGTVAWMAPEVIRNEPCSEKVDIWSFGVVL 170
                         90
                 ....*....|....
gi 767912019 107 YEMMCGRLPFYNQD 120
Cdd:cd14059  171 WELLTGEIPYKDVD 184
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
45-151 8.89e-14

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: 68.98  E-value: 8.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDG---HIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFyNQDh 121
Cdd:cd14082  132 ENVLLASAEpfpQVKLCDFGFARI-IGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF-NED- 208
                         90       100       110
                 ....*....|....*....|....*....|....
gi 767912019 122 EKLFELILMEDIKFPRT----LSSDAKSLLSGLL 151
Cdd:cd14082  209 EDINDQIQNAAFMYPPNpwkeISPDAIDLINNLL 242
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
40-158 9.18e-14

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: 69.01  E-value: 9.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAAtmKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY-- 117
Cdd:cd06620  129 RDIKPSNILVNSKGQIKLCDFGVSGELINSIA--DTFVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAgs 206
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767912019 118 NQDH------EKLFELI----------LMEDIKFPRtlssDAKSLLSGLLIKDPNKR 158
Cdd:cd06620  207 NDDDdgyngpMGILDLLqrivneppprLPKDRIFPK----DLRDFVDRCLLKDPRER 259
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
29-158 9.96e-14

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: 68.73  E-value: 9.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  29 IRFRFDLQAPPKNISLENLMLDKDG-HIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVM 106
Cdd:cd14164  113 VNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFARFVEDYPELSTTFCGSRAYTPPEVILGTPYdPKKYDVWSLGVVL 192
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767912019 107 YEMMCGRLPFynqdHEKLFELILMED--IKFPR--TLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd14164  193 YVMVTGTMPF----DETNVRRLRLQQrgVLYPSgvALEEPCRALIRTLLQFNPSTR 244
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
46-128 1.33e-13

Protein tyrosine kinase;


Pssm-ID: 429616 [Multi-domain]  Cd Length: 258  Bit Score: 68.29  E-value: 1.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019   46 NLMLDKDGHIKITDFGLCKEgITDAATMKTFCGTPE---YLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDH 121
Cdd:pfam07714 132 NCLVSENLVVKISDFGLSRD-IYDDDYYRKRGGGKLpikWMAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSN 210

                  ....*..
gi 767912019  122 EKLFELI 128
Cdd:pfam07714 211 EEVLEYL 217
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
40-128 1.49e-13

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 68.33  E-value: 1.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEG-ITDAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 116
Cdd:cd00192  129 RDLAARNCLVGEDLVVKISDFGLSRDIyDDDYYRKKTGGKLPiRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATPY 208
                         90
                 ....*....|..
gi 767912019 117 YNQDHEKLFELI 128
Cdd:cd00192  209 PGLSNEEVLEYL 220
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
46-176 1.77e-13

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: 68.74  E-value: 1.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCK-----EGITDAATMKTFCGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRLPF--- 116
Cdd:cd07852  137 NILLNSDCRVKLADFGLARslsqlEEDDENPVLTDYVATRWYRAPEILlGSTRYTKGVDMWSVGCILGEMLLGKPLFpgt 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 117 --YNQdHEKLFELILM---EDI-------------------------KFPRTlSSDAKSLLSGLLIKDPNKRLgggpdDA 166
Cdd:cd07852  217 stLNQ-LEKIIEVIGRpsaEDIesiqspfaatmleslppsrpksldeLFPKA-SPDALDLLKKLLVFNPNKRL-----TA 289
                        170
                 ....*....|
gi 767912019 167 KEIMRHSFFS 176
Cdd:cd07852  290 EEALRHPYVA 299
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
35-175 3.08e-13

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 67.29  E-value: 3.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  35 LQAPPKNIslenLMLDKDGH-IKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGR 113
Cdd:cd14192  126 LDLKPENI----LCVNSTGNqIKIIDFGLARR-YKPREKLKVNFGTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGL 200
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912019 114 LPFYNQDHEKLFELILMEDIKFP----RTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd14192  201 SPFLGETDAETMNNIVNCKWDFDaeafENLSEEAKDFISRLLVKEKSCRM-----SATQCLKHEWL 261
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
33-159 3.49e-13

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


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 67.34  E-value: 3.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  33 FDLQapPKNIslenLMLDKDG---HIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEM 109
Cdd:cd14195  132 FDLK--PENI----MLLDKNVpnpRIKLIDFGIAHK-IEAGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYIL 204
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767912019 110 MCGRLPFYNQDHEKLFELILMEDIKFPRTLSSD----AKSLLSGLLIKDPNKRL 159
Cdd:cd14195  205 LSGASPFLGETKQETLTNISAVNYDFDEEYFSNtselAKDFIRRLLVKDPKKRM 258
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
46-175 4.65e-13

Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RPK118 contains an N-terminal Phox homology (PX) domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain containing a long uncharacterized insert. Also included in the family is human RPK60 (or ribosomal protein S6 kinase-like 1), which also contains MIT and kinase domains but lacks a PX domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. RPK118 also binds the antioxidant peroxiredoxin-3. RPK118 may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. The RPK118-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: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 66.80  E-value: 4.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCKEgITDA----ATMKTFCgtpeylAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRL-----PF 116
Cdd:cd05576  143 NILLNDRGHIQLTYFSRWSE-VEDScdsdAIENMYC------APEVGGISEETEACDWWSLGALLFELLTGKAlvechPA 215
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767912019 117 YNQDHEKLfelilmediKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFF 175
Cdd:cd05576  216 GINTHTTL---------NIPEWVSEEARSLLQQLLQFNPTERLGAGVAGVEDIKSHPFF 265
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
39-116 5.22e-13

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: 67.09  E-value: 5.22e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912019  39 PKNISLENlMLDKDGHiKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd13989  130 PENIVLQQ-GGGRVIY-KLIDLGYAKE-LDQGSLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPF 204
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
33-158 5.65e-13

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


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 66.57  E-value: 5.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  33 FDLQapPKNISLENLMLDkdGHIKITDFGLCK---EGITDAATM---KTFCGTPEYLAPEVLEDNDYGR----AVDWWGL 102
Cdd:cd13990  131 YDLK--PGNILLHSGNVS--GEIKITDFGLSKimdDESYNSDGMeltSQGAGTYWYLPPECFVVGKTPPkissKVDVWSV 206
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912019 103 GVVMYEMMCGRLPF-YNQDHEK-LFELILME--DIKFPR--TLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd13990  207 GVIFYQMLYGRKPFgHNQSQEAiLEENTILKatEVEFPSkpVVSSEAKDFIRRCLTYRKEDR 268
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
55-175 6.88e-13

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: 66.45  E-value: 6.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  55 IKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHE----KLFELILM 130
Cdd:cd14107  139 IKICDFGFAQE-ITPSEHQFSKYGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRatllNVAEGVVS 217
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767912019 131 EDIKFPRTLSSDAKSLLSGLLIKDPNKRLGggpddAKEIMRHSFF 175
Cdd:cd14107  218 WDTPEITHLSEDAKDFIKRVLQPDPEKRPS-----ASECLSHEWF 257
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
40-193 7.57e-13

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: 66.61  E-value: 7.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPfyNQ 119
Cdd:cd06640  125 RDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPP--NS 202
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912019 120 DHEKLFELILMEDIKFPR---TLSSDAKSLLSGLLIKDPNKRlgggpDDAKEIMRHSFFSGVNWQDVYDKKLVPPFK 193
Cdd:cd06640  203 DMHPMRVLFLIPKNNPPTlvgDFSKPFKEFIDACLNKDPSFR-----PTAKELLKHKFIVKNAKKTSYLTELIDRFK 274
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
41-120 8.19e-13

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


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 66.00  E-value: 8.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  41 NISLENLMLDKDGHIKITDFGLCKEGITDAATMKT-FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd14111  124 DIKPDNIMVTNLNAIKIVDFGSAQSFNPLSLRQLGrRTGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQ 203

                 .
gi 767912019 120 D 120
Cdd:cd14111  204 D 204
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
35-172 8.93e-13

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: 66.09  E-value: 8.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  35 LQAPPKNIslenLMLDKDGH-IKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGR 113
Cdd:cd14193  126 LDLKPENI----LCVSREANqVKIIDFGLARR-YKPREKLRVNFGTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGL 200
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912019 114 LPFYNQDHEKLFELIL-----MEDIKFpRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRH 172
Cdd:cd14193  201 SPFLGEDDNETLNNILacqwdFEDEEF-ADISEEAKDFISKLLIKEKSWRM-----SASEALKH 258
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
45-158 1.21e-12

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: 65.83  E-value: 1.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKD-GHIKITDFGLckeGITDAATMKTFCGTPEYLAPEVLEDND------YGRAVDWWGLGVVMYEMMCGRLPF- 116
Cdd:cd13993  136 ENILLSQDeGTVKLCDFGL---ATTEKISMDFGVGSEFYMAPECFDEVGrslkgyPCAAGDIWSLGIILLNLTFGRNPWk 212
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767912019 117 -----------YNQDHEKLFELILmedikfprTLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd13993  213 iasesdpifydYYLNSPNLFDVIL--------PMSDDFYNLLRQIFTVNPNNR 257
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
45-175 1.41e-12

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 65.77  E-value: 1.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKE-GITdaatMKTFcgTPE-----YLAPEVL-EDNDYGRAVDWWGLGVVMYEmMCGRLPFY 117
Cdd:cd07835  128 QNLLIDTEGALKLADFGLARAfGVP----VRTY--THEvvtlwYRAPEILlGSKHYSTPVDIWSVGCIFAE-MVTRRPLF 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 118 NQDHE-----KLFELI------------LMEDIK--FPR-----------TLSSDAKSLLSGLLIKDPNKRLgggpdDAK 167
Cdd:cd07835  201 PGDSEidqlfRIFRTLgtpdedvwpgvtSLPDYKptFPKwarqdlskvvpSLDEDGLDLLSQMLVYDPAKRI-----SAK 275

                 ....*...
gi 767912019 168 EIMRHSFF 175
Cdd:cd07835  276 AALQHPYF 283
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
40-174 1.45e-12

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 65.15  E-value: 1.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCK--EGITDAATmkTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY 117
Cdd:cd08223  126 RDLKTQNIFLTKSNIIKVGDLGIARvlESSSDMAT--TLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFN 203
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767912019 118 NQDHEKLFELILMEDI-KFPRTLSSDAKSLLSGLLIKDPNKRlgggpDDAKEIMRHSF 174
Cdd:cd08223  204 AKDMNSLVYKILEGKLpPMPKQYSPELGELIKAMLHQDPEKR-----PSVKRILRQPY 256
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
46-175 1.93e-12

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: 65.28  E-value: 1.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLckegitdAATM-KTFCG-------TPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd07840  134 NILINNDGVLKLADFGL-------ARPYtKENNAdytnrviTLWYRPPELLlGATRYGPEVDMWSVGCILAELFTGKPIF 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 117 -----YNQdHEKLFELI---------------LMEDIKFPRT------------LSSDAKSLLSGLLIKDPNKRLgggpd 164
Cdd:cd07840  207 qgkteLEQ-LEKIFELCgspteenwpgvsdlpWFENLKPKKPykrrlrevfknvIDPSALDLLDKLLTLDPKKRI----- 280
                        170
                 ....*....|.
gi 767912019 165 DAKEIMRHSFF 175
Cdd:cd07840  281 SADQALQHEYF 291
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
40-154 2.21e-12

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: 65.01  E-value: 2.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLdKDGHIKITDFGLCKEGITDAATM-KTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFY 117
Cdd:cd14163  125 RDLKCENALL-QGFTLKLTDFGFAKQLPKGGRELsQTFCGSTAYAAPEVLQGVPHdSRKGDIWSMGVVLYVMLCAQLPFD 203
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 767912019 118 NQDHEKLFeLILMEDIKFPRTL--SSDAKSLLSGLLIKD 154
Cdd:cd14163  204 DTDIPKML-CQQQKGVSLPGHLgvSRTCQDLLKRLLEPD 241
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
45-175 2.66e-12

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 64.83  E-value: 2.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDND-YGRAVDWWGLGVVMYEMMCGRLPFY-NQDHE 122
Cdd:cd07860  129 QNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKyYSTAVDIWSLGCIFAEMVTRRALFPgDSEID 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 123 KLFELIL---------------MEDIK--FPR-----------TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSF 174
Cdd:cd07860  209 QLFRIFRtlgtpdevvwpgvtsMPDYKpsFPKwarqdfskvvpPLDEDGRDLLSQMLHYDPNKRI-----SAKAALAHPF 283

                 .
gi 767912019 175 F 175
Cdd:cd07860  284 F 284
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
45-158 2.82e-12

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: 64.33  E-value: 2.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCkegitdaATMKTFC----GTPEYLAPEVLEDN-DYGRAVDWWGLGVVMYEMMCG-RLPFYN 118
Cdd:cd13997  132 DNIFISNKGTCKIGDFGLA-------TRLETSGdveeGDSRYLAPELLNENyTHLPKADIFSLGVTVYEAATGePLPRNG 204
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767912019 119 QDHEKLFELILmedIKFPR-TLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd13997  205 QQWQQLRQGKL---PLPPGlVLSQELTRLLKVMLDPDPTRR 242
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
40-158 3.27e-12

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: 64.22  E-value: 3.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd08219  124 RDIKSKNIFLTQNGKVKLGDFGSARLLTSPGAYACTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQAN 203
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767912019 120 DHEKLFELILMEDIK-FPRTLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd08219  204 SWKNLILKVCQGSYKpLPSHYSYELRSLIKQMFKRNPRSR 243
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
52-174 4.29e-12

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: 64.16  E-value: 4.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  52 DGHIKITDFGLCKEGITDAA--TMKTFCGTPEYLAPEVLEDNDY----------GRAVDWWGLGVVMYEMMCGRLPFY-- 117
Cdd:cd14131  138 KGRLKLIDFGIAKAIQNDTTsiVRDSQVGTLNYMSPEAIKDTSAsgegkpkskiGRPSDVWSLGCILYQMVYGKTPFQhi 217
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912019 118 -----------NQDHEklfelilmedIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSF 174
Cdd:cd14131  218 tnpiaklqaiiDPNHE----------IEFPDIPNPDLIDVMKRCLQRDPKKRP-----SIPELLNHPF 270
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
40-158 4.61e-12

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: 63.82  E-value: 4.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLD-KDGHIKITDFG---LCKEGI-TDaatmktFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGR 113
Cdd:cd14102  129 RDIKDENLLVDlRTGELKLIDFGsgaLLKDTVyTD------FDGTRVYSPPEWIRYHRYhGRSATVWSLGVLLYDMVCGD 202
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767912019 114 LPFyNQDHEklfelILMEDIKFPRTLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd14102  203 IPF-EQDEE-----ILRGRLYFRRRVSPECQQLIKWCLSLRPSDR 241
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
46-128 5.21e-12

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: 63.72  E-value: 5.21e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019    46 NLMLDKDGHIKITDFGLCKEgITDAATMKTFCGT-P-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMM-CGRLPFYNQDHE 122
Cdd:smart00221 133 NCLVGENLVVKISDFGLSRD-LYDDDYYKVKGGKlPiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFtLGEEPYPGMSNA 211

                   ....*.
gi 767912019   123 KLFELI 128
Cdd:smart00221 212 EVLEYL 217
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
40-158 7.69e-12

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: 63.51  E-value: 7.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNq 119
Cdd:cd08228  130 RDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYG- 208
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 767912019 120 DHEKLFELIL-MEDIKFP----RTLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd08228  209 DKMNLFSLCQkIEQCDYPplptEHYSEKLRELVSMCIYPDPDQR 252
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
40-179 7.94e-12

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 63.51  E-value: 7.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEV-----LEDNDYGRAVDWWGLGVVMYEMMCGRL 114
Cdd:cd06644  134 RDLKAGNVLLTLDGDIKLADFGVSAKNVKTLQRRDSFIGTPYWMAPEVvmcetMKDTPYDYKADIWSLGITLIEMAQIEP 213
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912019 115 PFYNQDHEKLFELILMEDikfPRTLSSDAK------SLLSGLLIKDPNKRlgggpDDAKEIMRHSFFSGVN 179
Cdd:cd06644  214 PHHELNPMRVLLKIAKSE---PPTLSQPSKwsmefrDFLKTALDKHPETR-----PSAAQLLEHPFVSSVT 276
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
39-168 8.18e-12

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


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 63.40  E-value: 8.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  39 PKNISLEnlmlDKDGHI--KITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd14039  127 PENIVLQ----EINGKIvhKIIDLGYAKD-LDQGSLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPF 201
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912019 117 Y-------------NQDHEKLFELILME-DIKF------PRTLSS----DAKSLLSGLLIKDPNKRLGGGPDDAKE 168
Cdd:cd14039  202 LhnlqpftwhekikKKDPKHIFAVEEMNgEVRFsthlpqPNNLCSlivePMEGWLQLMLNWDPVQRGGGLDTDSKQ 277
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
39-172 8.36e-12

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


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 63.51  E-value: 8.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  39 PKNISLENLmlDKDGHIKITDFGLcKEGI---TDAATMKTF-----CGTPEYLAPEVLEDND-----YGRAVDWWGLGVV 105
Cdd:cd14173  128 PENILCEHP--NQVSPVKICDFDL-GSGIklnSDCSPISTPelltpCGSAEYMAPEVVEAFNeeasiYDKRCDLWSLGVI 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 106 MYEMMCGRLPFYNQ---------------DHEKLFELILMEDIKFPRT----LSSDAKSLLSGLLIKDPNKRLgggpdDA 166
Cdd:cd14173  205 LYIMLSGYPPFVGRcgsdcgwdrgeacpaCQNMLFESIQEGKYEFPEKdwahISCAAKDLISKLLVRDAKQRL-----SA 279

                 ....*.
gi 767912019 167 KEIMRH 172
Cdd:cd14173  280 AQVLQH 285
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
46-128 9.38e-12

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 62.93  E-value: 9.38e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019    46 NLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMM-CGRLPFYNQDHEK 123
Cdd:smart00219 132 NCLVGENLVVKISDFGLSRDLYDDDYYRKRGGKLPiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFtLGEQPYPGMSNEE 211

                   ....*
gi 767912019   124 LFELI 128
Cdd:smart00219 212 VLEYL 216
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
46-176 1.07e-11

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: 63.36  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCgRLPFYNQDHE-- 122
Cdd:cd07841  132 NLLIASDGVLKLADFGLARSFGSPNRKMTHQVVTRWYRAPELLfGARHYGVGVDMWSVGCIFAELLL-RVPFLPGDSDid 210
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 123 ---KLFELI-------------LMEDIKF-PRT----------LSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd07841  211 qlgKIFEALgtpteenwpgvtsLPDYVEFkPFPptplkqifpaASDDALDLLQRLLTLNPNKRI-----TARQALEHPYF 285

                 .
gi 767912019 176 S 176
Cdd:cd07841  286 S 286
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
45-175 1.12e-11

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: 63.29  E-value: 1.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLD-KDGHIKITDFGLCKEGITDAATMKTFCgTPEYLAPEVLEDN-DYGRAVDWWGLGVVMYEMMCGRlPFYNQDH- 121
Cdd:cd14137  135 QNLLVDpETGVLKLCDFGSAKRLVPGEPNVSYIC-SRYYRAPELIFGAtDYTTAIDIWSAGCVLAELLLGQ-PLFPGESs 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 122 -EKLFELILM------EDIK----------------------FPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRH 172
Cdd:cd14137  213 vDQLVEIIKVlgtptrEQIKamnpnytefkfpqikphpwekvFPKRTPPDAIDLLSKILVYNPSKRL-----TALEALAH 287

                 ...
gi 767912019 173 SFF 175
Cdd:cd14137  288 PFF 290
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
55-175 1.16e-11

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: 63.10  E-value: 1.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  55 IKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN---QDHEKLFELILME 131
Cdd:cd14201  153 IKIADFGFARY-LQSNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQAnspQDLRMFYEKNKNL 231
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 767912019 132 DIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd14201  232 QPSIPRETSPYLADLLLGLLQRNQKDRM-----DFEAFFSHPFL 270
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
40-158 1.18e-11

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: 63.21  E-value: 1.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAAtmKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd06621  129 RDIKPSNILLTRKGQVKLCDFGVSGELVNSLA--GTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPE 206
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767912019 120 DHEKL--FELI----------LMEDIKFPRTLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd06621  207 GEPPLgpIELLsyivnmpnpeLKDEPENGIKWSESFKDFIEKCLEKDGTRR 257
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
46-158 1.27e-11

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 62.67  E-value: 1.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY--NQDHEK 123
Cdd:cd08224  134 NVFITANGVVKLGDLGLGRFFSSKTTAAHSLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYgeKMNLYS 213
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 767912019 124 LFELIlmEDIKFP----RTLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd08224  214 LCKKI--EKCEYPplpaDLYSQELRDLVAACIQPDPEKR 250
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
40-158 1.37e-11

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: 62.67  E-value: 1.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHI-KITDFGLCKEgITDAATMKTFC-GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY 117
Cdd:cd08225  125 RDIKSQNIFLSKNGMVaKLGDFGIARQ-LNDSMELAYTCvGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFE 203
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767912019 118 -NQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd08225  204 gNNLHQLVLKICQGYFAPISPNFSRDLRSLISQLFKVSPRDR 245
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
46-174 1.38e-11

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 62.70  E-value: 1.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCKEgiTDAATMK--TFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGRLPFYN 118
Cdd:cd06608  143 NILLTEEAEVKLVDFGVSAQ--LDSTLGRrnTFIGTPYWMAPEVIAcdqqpDASYDARCDVWSLGITAIELADGKPPLCD 220
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767912019 119 QDHEKLFELILMED---IKFPRTLSSDAKSLLSGLLIKDPNKRlgggPdDAKEIMRHSF 174
Cdd:cd06608  221 MHPMRALFKIPRNPpptLKSPEKWSKEFNDFISECLIKNYEQR----P-FTEELLEHPF 274
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
41-159 1.38e-11

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: 62.60  E-value: 1.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  41 NISLENLMLD--KDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN 118
Cdd:cd14114  125 DIKPENIMCTtkRSNEVKLIDFGLATH-LDPKESVKVTTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAG 203
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767912019 119 QDHEKLFELILMEDIKFP----RTLSSDAKSLLSGLLIKDPNKRL 159
Cdd:cd14114  204 ENDDETLRNVKSCDWNFDdsafSGISEEAKDFIRKLLLADPNKRM 248
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
46-192 1.64e-11

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: 63.05  E-value: 1.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCKEgiTDAAtMKTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH-EK 123
Cdd:cd07880  148 NLAVNEDCELKILDFGLARQ--TDSE-MTGYVVTRWYRAPEViLNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHlDQ 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 124 LFELILM--------------EDIK-----FPRTLSSDAKSLLS-----------GLLIKDPNKRLgggpdDAKEIMRHS 173
Cdd:cd07880  225 LMEIMKVtgtpskefvqklqsEDAKnyvkkLPRFRKKDFRSLLPnanplavnvleKMLVLDAESRI-----TAAEALAHP 299
                        170
                 ....*....|....*....
gi 767912019 174 FFSgvNWQDVYDKKLVPPF 192
Cdd:cd07880  300 YFE--EFHDPEDETEAPPY 316
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
40-175 1.79e-11

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: 62.72  E-value: 1.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCK---EGITDAATmkTFCGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEM------ 109
Cdd:cd07833  124 RDIKPENILVSESGVLKLCDFGFARaltARPASPLT--DYVATRWYRAPELLvGDTNYGKPVDVWAIGCIMAELldgepl 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 110 ---------------MCGRLP------FYNQDH---EKLFELILMEDI--KFPRTLSSDAKSLLSGLLIKDPNKRLgggp 163
Cdd:cd07833  202 fpgdsdidqlyliqkCLGPLPpshqelFSSNPRfagVAFPEPSQPESLerRYPGKVSSPALDFLKACLRMDPKERL---- 277
                        170
                 ....*....|..
gi 767912019 164 dDAKEIMRHSFF 175
Cdd:cd07833  278 -TCDELLQHPYF 288
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
45-158 1.83e-11

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


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 62.30  E-value: 1.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGH---IKITDFGlckegitDAATMKT------FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLP 115
Cdd:cd14113  132 ENILVDQSLSkptIKLADFG-------DAVQLNTtyyihqLLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSP 204
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 767912019 116 FYNQDHEKLFELILMEDIKFP----RTLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd14113  205 FLDESVEETCLNICRLDFSFPddyfKGVSQKAKDFVCFLLQMDPAKR 251
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
40-174 1.90e-11

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: 62.37  E-value: 1.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCK--EGITDAAT-MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd06652  130 RDIKGANILRDSVGNVKLGDFGASKrlQTICLSGTgMKSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPW 209
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 117 YN-QDHEKLFELILM-EDIKFPRTLSSDAKSLLSGLLIKDPNKrlgggpDDAKEIMRHSF 174
Cdd:cd06652  210 AEfEAMAAIFKIATQpTNPQLPAHVSDHCRDFLKRIFVEAKLR------PSADELLRHTF 263
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
40-213 2.74e-11

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: 62.36  E-value: 2.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEgitDAATMKTFCGTPEYLAPEVLED-NDYGRAVDWWGLGVVMYEMMCGRLPFYN 118
Cdd:cd07877  144 RDLKPSNLAVNEDCELKILDFGLARH---TDDEMTGYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLTGRTLFPG 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 119 QDHEKLFELIL----------------------------MEDIKFPRTL---SSDAKSLLSGLLIKDPNKRLgggpdDAK 167
Cdd:cd07877  221 TDHIDQLKLILrlvgtpgaellkkissesarnyiqsltqMPKMNFANVFigaNPLAVDLLEKMLVLDSDKRI-----TAA 295
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767912019 168 EIMRHSFFSgvNWQDVYDKKLVPPFKPQVTSetdtRYFD-EEFTAQT 213
Cdd:cd07877  296 QALAHAYFA--QYHDPDDEPVADPYDQSFES----RDLLiDEWKSLT 336
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
40-158 3.26e-11

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


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 61.52  E-value: 3.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLD-KDGHIKITDFG---LCKEGI-TDaatmktFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGR 113
Cdd:cd14100  130 RDIKDENILIDlNTGELKLIDFGsgaLLKDTVyTD------FDGTRVYSPPEWIRFHRYhGRSAAVWSLGILLYDMVCGD 203
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767912019 114 LPFyNQDHEklfelILMEDIKFPRTLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd14100  204 IPF-EHDEE-----IIRGQVFFRQRVSSECQHLIKWCLALRPSDR 242
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
40-158 3.28e-11

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 61.40  E-value: 3.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLD-KDGHIKITDFGlckEGITDAATMKT-FCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd14101  132 RDIKDENILVDlRTGDIKLIDFG---SGATLKDSMYTdFDGTRVYSPPEWILYHQYhALPATVWSLGILLYDMVCGDIPF 208
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767912019 117 yNQDHEklfelILMEDIKFPRTLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd14101  209 -ERDTD-----ILKAKPSFNKRVSNDCRSLIRSCLAYNPSDR 244
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
40-174 3.59e-11

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: 61.61  E-value: 3.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd06642  125 RDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDL 204
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767912019 120 DHEKLFELILMEDikfPRTL----SSDAKSLLSGLLIKDPNKRlgggpDDAKEIMRHSF 174
Cdd:cd06642  205 HPMRVLFLIPKNS---PPTLegqhSKPFKEFVEACLNKDPRFR-----PTAKELLKHKF 255
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
45-175 3.65e-11

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 61.52  E-value: 3.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKegITDAATMKTFC-GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH-- 121
Cdd:cd07838  136 QNILVTSDGQVKLADFGLAR--IYSFEMALTSVvVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFRGSSEad 213
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912019 122 --EKLFELI------------LMEDIKFPRTLSSDAKS-----------LLSGLLIKDPNKRLGggpddAKEIMRHSFF 175
Cdd:cd07838  214 qlGKIFDVIglpseeewprnsALPRSSFPSYTPRPFKSfvpeideegldLLKKMLTFNPHKRIS-----AFEALQHPYF 287
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
40-158 3.65e-11

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 61.29  E-value: 3.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd08221  125 RDIKTLNIFLTKADLVKLGDFGISKVLDSESSMAESIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDAT 204
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 767912019 120 DHEKLFELIL-----MEDIKFprtlSSDAKSLLSGLLIKDPNKR 158
Cdd:cd08221  205 NPLRLAVKIVqgeyeDIDEQY----SEEIIQLVHDCLHQDPEDR 244
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
52-175 4.45e-11

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 61.09  E-value: 4.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  52 DGHIKITDFGLCKegITDAATMKTFCGTPEYLAPEVLEDNdYGRAVDWWGLGVVMYEMMCGRLPFY-----NQDHEKLFE 126
Cdd:cd13983  141 TGEVKIGDLGLAT--LLRQSFAKSVIGTPEFMAPEMYEEH-YDEKVDIYAFGMCLLEMATGEYPYSectnaAQIYKKVTS 217
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767912019 127 LILMEDIKfpRTLSSDAKSLLSgLLIKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd13983  218 GIKPESLS--KVKDPELKDFIE-KCLKPPDERP-----SARELLEHPFF 258
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
45-175 4.47e-11

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: 61.40  E-value: 4.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRlPFYNQDHE- 122
Cdd:cd07830  128 ENLLVSGPEVVKIADFGLARE-IRSRPPYTDYVSTRWYRAPEIlLRSTSYSSPVDIWALGCIMAELYTLR-PLFPGSSEi 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 123 ----KLFELI-------------LMED--IKFPR-----------TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRH 172
Cdd:cd07830  206 dqlyKICSVLgtptkqdwpegykLASKlgFRFPQfaptslhqlipNASPEAIDLIKDMLRWDPKKRP-----TASQALQH 280

                 ...
gi 767912019 173 SFF 175
Cdd:cd07830  281 PYF 283
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
45-174 4.74e-11

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: 61.24  E-value: 4.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKE-----GITDAATMKtfcGTPEYLAPEVLEDND--YGRAVDWWGLGVVMYEMMCGRLPFY 117
Cdd:cd06629  137 DNILVDLEGICKISDFGISKKsddiyGNNGATSMQ---GSVFWMAPEVIHSQGqgYSAKVDIWSLGCVVLEMLAGRRPWS 213
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912019 118 NQDH-EKLFELI-------LMEDIKfprtLSSDAKSLLSGLLIKDPNKRlgggPdDAKEIMRHSF 174
Cdd:cd06629  214 DDEAiAAMFKLGnkrsappVPEDVN----LSPEALDFLNACFAIDPRDR----P-TAAELLSHPF 269
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
46-174 5.17e-11

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: 61.24  E-value: 5.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCKEGITDAATMKTfCGTPEYLAPEVLEDNDYG----RAvDWWGLGVVMYEMMCGRLPFYNQDH 121
Cdd:cd06618  145 NILLDESGNVKLCDFGISGRLVDSKAKTRS-AGCAAYMAPERIDPPDNPkydiRA-DVWSLGISLVELATGQFPYRNCKT 222
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767912019 122 EklFEL---ILMEDIKFP---RTLSSDAKSLLSGLLIKDPNKRlgggpDDAKEIMRHSF 174
Cdd:cd06618  223 E--FEVltkILNEEPPSLppnEGFSPDFCSFVDLCLTKDHRYR-----PKYRELLQHPF 274
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
45-172 5.72e-11

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 60.90  E-value: 5.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHI-KITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFynqDHEK 123
Cdd:cd08220  130 QNILLNKKRTVvKIGDFGISKI-LSSKSKAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAF---EAAN 205
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767912019 124 LFELIL--MEDIKFPRT--LSSDAKSLLSGLLIKDPNKRlgggpDDAKEIMRH 172
Cdd:cd08220  206 LPALVLkiMRGTFAPISdrYSEELRHLILSMLHLDPNKR-----PTLSEIMAQ 253
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
40-193 6.26e-11

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: 60.86  E-value: 6.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEgITDAATMKT-FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN 118
Cdd:cd06641  125 RDIKAANVLLSEHGEVKLADFGVAGQ-LTDTQIKRN*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSE 203
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912019 119 QDHEKLFELILMEDIKFPR-TLSSDAKSLLSGLLIKDPNKRlgggpDDAKEIMRHSFFSGVNWQDVYDKKLVPPFK 193
Cdd:cd06641  204 LHPMKVLFLIPKNNPPTLEgNYSKPLKEFVEACLNKEPSFR-----PTAKELLKHKFILRNAKKTSYLTELIDRYK 274
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
42-158 6.46e-11

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


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 60.40  E-value: 6.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  42 ISLENLMLDKDGHIKITDFGLC----KEGITDAATmktfcGTPEYLAPEVLeDNDYGRAVDWWGLGVVMYEMMCG-RLPF 116
Cdd:cd14050  126 IKPANIFLSKDGVCKLGDFGLVveldKEDIHDAQE-----GDPRYMAPELL-QGSFTKAADIFSLGITILELACNlELPS 199
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767912019 117 YNQDHEKLFELILMEDikFPRTLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd14050  200 GGDGWHQLRQGYLPEE--FTAGLSPELRSIIKLMMDPDPERR 239
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
13-121 6.89e-11

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 60.54  E-value: 6.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  13 SLLQRtakEDIALPYKIRFRFDLQA-----------PP---KNISLENLMLDKDGHIKITDFGLCK-----EGITDAATM 73
Cdd:cd13978   81 SLLER---EIQDVPWSLRFRIIHEIalgmnflhnmdPPllhHDLKPENILLDNHFHVKISDFGLSKlgmksISANRRRGT 157
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767912019  74 KTFCGTPEYLAPEVLEDNDY--GRAVDWWGLGVVMYEMMCGRLPFYNQDH 121
Cdd:cd13978  158 ENLGGTPIYMAPEAFDDFNKkpTSKSDVYSFAIVIWAVLTRKEPFENAIN 207
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
11-121 7.06e-11

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


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 60.58  E-value: 7.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  11 GISLLQRTakeDIALPY--KIRFRFDLQAPPKNISLENLMLDKDGHIKITDFGLCKegiTDAATMKTFCGTPEYLAPEVL 88
Cdd:cd13975   98 GLSLEERL---QIALDVveGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCK---PEAMMSGSIVGTPIHMAPELF 171
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767912019  89 eDNDYGRAVDWWGLGVVMYEMMCG--RLP-----FYNQDH 121
Cdd:cd13975  172 -SGKYDNSVDVYAFGILFWYLCAGhvKLPeafeqCASKDH 210
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
41-118 7.56e-11

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 60.75  E-value: 7.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  41 NISLENLMLDKDGHIKITDFGLCKEGITDAATMKT--FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN 118
Cdd:cd14066  121 DIKSSNILLDEDFEPKLTDFGLARLIPPSESVSKTsaVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDE 200
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
40-175 8.32e-11

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 60.79  E-value: 8.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRLPFYN 118
Cdd:cd07873  124 RDLKPQNLLINERGELKLADFGLARAKSIPTKTYSNEVVTLWYRPPDILlGSTDYSTQIDMWGVGCIFYEMSTGRPLFPG 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 119 QDHEKLFELILM----------------EDIK---FPR-----------TLSSDAKSLLSGLLIKDPNKRLGggpddAKE 168
Cdd:cd07873  204 STVEEQLHFIFRilgtpteetwpgilsnEEFKsynYPKyradalhnhapRLDSDGADLLSKLLQFEGRKRIS-----AEE 278

                 ....*..
gi 767912019 169 IMRHSFF 175
Cdd:cd07873  279 AMKHPYF 285
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
40-177 1.93e-10

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 59.84  E-value: 1.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLckeGITDAATM---KTFCGTPEYLAPEV----LEDNDY-GRAVDWWGLGVVMYEMMC 111
Cdd:PLN00034 192 RDIKPSNLLINSAKNVKIADFGV---SRILAQTMdpcNSSVGTIAYMSPERintdLNHGAYdGYAGDIWSLGVSILEFYL 268
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 112 GRLPF---YNQDHEKLFELILMEDI-KFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFSG 177
Cdd:PLN00034 269 GRFPFgvgRQGDWASLMCAICMSQPpEAPATASREFRHFISCCLQREPAKRW-----SAMQLLQHPFILR 333
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
40-174 2.28e-10

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 59.67  E-value: 2.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGlckeGITDAATMKTFCGTPEYLAPEV---LEDNDYGRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd06633  145 RDIKAGNILLTEPGQVKLADFG----SASIASPANSFVGTPYWMAPEVilaMDEGQYDGKVDIWSLGITCIELAERKPPL 220
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912019 117 YNQDHEKLFELILMEDikfPRTLSSDA-----KSLLSGLLIKDPNKRLGGGpddakEIMRHSF 174
Cdd:cd06633  221 FNMNAMSALYHIAQND---SPTLQSNEwtdsfRGFVDYCLQKIPQERPSSA-----ELLRHDF 275
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
45-116 2.40e-10

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 59.81  E-value: 2.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCK----EGITDAATMktfCGTPEYLAPEVLEdndyGRAV----DWWGLGVVMYEMMCGRLPF 116
Cdd:NF033483 136 QNILITKDGRVKVTDFGIARalssTTMTQTNSV---LGTVHYLSPEQAR----GGTVdarsDIYSLGIVLYEMLTGRPPF 208
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
42-175 2.60e-10

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


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 59.06  E-value: 2.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  42 ISLENLMLDKDgHIKITDFGLCKEGITDAATMKTFcGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH 121
Cdd:cd14109  125 LRPEDILLQDD-KLKLADFGQSRRLLRGKLTTLIY-GSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDND 202
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767912019 122 EKLFELILMEDIKFPRT----LSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd14109  203 RETLTNVRSGKWSFDSSplgnISDDARDFIKKLLVYIPESRL-----TVDEALNHPWF 255
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
39-158 3.13e-10

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: 58.84  E-value: 3.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  39 PKNISLENlmldKDGHIKITDFGLCK-----EGITDA---------ATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGV 104
Cdd:cd13996  135 PSNIFLDN----DDLQVKIGDFGLATsignqKRELNNlnnnnngntSNNSVGIGTPLYASPEQLDGENYNEKADIYSLGI 210
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767912019 105 VMYEMMCGRlpfyNQDHEKLFELILMEDIKFPRTLSS---DAKSLLSGLLIKDPNKR 158
Cdd:cd13996  211 ILFEMLHPF----KTAMERSTILTDLRNGILPESFKAkhpKEADLIQSLLSKNPEER 263
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
45-175 3.69e-10

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


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 58.54  E-value: 3.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGrLPFY------ 117
Cdd:cd07847  129 ENILITKQGQIKLCDFGFARILTGPGDDYTDYVATRWYRAPELLvGDTQYGPPVDVWAIGCVFAELLTG-QPLWpgksdv 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 118 NQ-------------DHEKLFE-------LIL-----MEDI--KFPRtLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIM 170
Cdd:cd07847  208 DQlylirktlgdlipRHQQIFStnqffkgLSIpepetREPLesKFPN-ISSPALSFLKGCLQMDPTERL-----SCEELL 281

                 ....*
gi 767912019 171 RHSFF 175
Cdd:cd07847  282 EHPYF 286
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
40-174 4.44e-10

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: 58.50  E-value: 4.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCK--EGITDAAT-MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd06653  130 RDIKGANILRDSAGNVKLGDFGASKriQTICMSGTgIKSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPW 209
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 117 YNQDHEKLFELILMEDIK--FPRTLSSDAKSLLSGLLIKDPNKRLgggpddAKEIMRHSF 174
Cdd:cd06653  210 AEYEAMAAIFKIATQPTKpqLPDGVSDACRDFLRQIFVEEKRRPT------AEFLLRHPF 263
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
40-133 4.46e-10

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: 58.35  E-value: 4.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAAtmKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF--Y 117
Cdd:cd06619  119 RDVKPSNMLVNTRGQVKLCDFGVSTQLVNSIA--KTYVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYpqI 196
                         90
                 ....*....|....*.
gi 767912019 118 NQDHEKLFELILMEDI 133
Cdd:cd06619  197 QKNQGSLMPLQLLQCI 212
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
40-175 4.97e-10

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 58.48  E-value: 4.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRLPFYN 118
Cdd:cd07871  127 RDLKPQNLLINEKGELKLADFGLARAKSVPTKTYSNEVVTLWYRPPDVLlGSTEYSTPIDMWGVGCILYEMATGRPMFPG 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 119 QDHEKLFELIL------MEDI-------------KFPR-----------TLSSDAKSLLSGLLIKDPNKRLgggpdDAKE 168
Cdd:cd07871  207 STVKEELHLIFrllgtpTEETwpgvtsneefrsyLFPQyraqplinhapRLDTDGIDLLSSLLLYETKSRI-----SAEA 281

                 ....*..
gi 767912019 169 IMRHSFF 175
Cdd:cd07871  282 ALRHSYF 288
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
40-174 4.98e-10

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: 58.17  E-value: 4.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGIT---DAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd06651  135 RDIKGANILRDSAGNVKLGDFGASKRLQTicmSGTGIRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW 214
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912019 117 ynQDHEKLFELILM----EDIKFPRTLSSDAKSLLSGLLIKDPNKrlgggpDDAKEIMRHSF 174
Cdd:cd06651  215 --AEYEAMAAIFKIatqpTNPQLPSHISEHARDFLGCIFVEARHR------PSAEELLRHPF 268
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
40-191 5.27e-10

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: 58.50  E-value: 5.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAaTMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd07876  147 RDLKPSNIVVKSDCTLKILDFGLARTACTNF-MMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGT 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 120 DH----EKLFELI----------LMEDIK-----------------FP-----------RTLSSDAKSLLSGLLIKDPNK 157
Cdd:cd07876  226 DHidqwNKVIEQLgtpsaefmnrLQPTVRnyvenrpqypgisfeelFPdwifpseserdKLKTSQARDLLSKMLVIDPDK 305
                        170       180       190
                 ....*....|....*....|....*....|....
gi 767912019 158 RLgggpdDAKEIMRHSFFSgvNWQDVYDKKLVPP 191
Cdd:cd07876  306 RI-----SVDEALRHPYIT--VWYDPAEAEAPPP 332
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
40-179 5.34e-10

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


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 58.11  E-value: 5.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVL-----EDNDYGRAVDWWGLGVVMYEMMCGRL 114
Cdd:cd06643  127 RDLKAGNILFTLDGDIKLADFGVSAKNTRTLQRRDSFIGTPYWMAPEVVmcetsKDRPYDYKADVWSLGVTLIEMAQIEP 206
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912019 115 PFYNQDHEKLFELILMED---IKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFSGVN 179
Cdd:cd06643  207 PHHELNPMRVLLKIAKSEpptLAQPSRWSPEFKDFLRKCLEKNVDARW-----TTSQLLQHPFVSVLV 269
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
46-175 5.40e-10

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: 58.48  E-value: 5.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCKeGITDAATMKTFCGTPE------------YLAPE-VLEDNDYGRAVDWWGLGVVMYEMMCG 112
Cdd:cd07866  145 NILIDNQGILKIADFGLAR-PYDGPPPNPKGGGGGGtrkytnlvvtrwYRPPElLLGERRYTTAVDIWGIGCVFAEMFTR 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 113 RlPFY------NQDHeKLFEL------ILM---------EDIKF----PRTLSS-------DAKSLLSGLLIKDPNKRLg 160
Cdd:cd07866  224 R-PILqgksdiDQLH-LIFKLcgtpteETWpgwrslpgcEGVHSftnyPRTLEErfgklgpEGLDLLSKLLSLDPYKRL- 300
                        170
                 ....*....|....*
gi 767912019 161 ggpdDAKEIMRHSFF 175
Cdd:cd07866  301 ----TASDALEHPYF 311
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
46-184 6.50e-10

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: 58.15  E-value: 6.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCKEGITD-AATMKTFCgTPeYLAPEVLEDND----YGRAVDWWGLGVVMYEMMCGRLPF--YN 118
Cdd:cd06616  140 NILLDRNGNIKLCDFGISGQLVDSiAKTRDAGC-RP-YMAPERIDPSAsrdgYDVRSDVWSLGITLYEVATGKFPYpkWN 217
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912019 119 QDHEKLFEL------ILMEDIKFprTLSSDAKSLLSGLLIKDPNKRlgggpDDAKEIMRHSFFSGVNWQDVY 184
Cdd:cd06616  218 SVFDQLTQVvkgdppILSNSEER--EFSPSFVNFVNLCLIKDESKR-----PKYKELLKHPFIKMYEERNVD 282
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
46-170 6.62e-10

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: 58.22  E-value: 6.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCKEGITDAATmkTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDhEKLF 125
Cdd:cd06615  130 NILVNSRGEIKLCDFGVSGQLIDSMAN--SFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPIPPPD-AKEL 206
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767912019 126 ELIlmedikFPRTLSSDAKsllsglliKDPNKRLGGGPDDAKEIM 170
Cdd:cd06615  207 EAM------FGRPVSEGEA--------KESHRPVSGHPPDSPRPM 237
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
46-158 7.46e-10

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 57.45  E-value: 7.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGH-IKITDFGLckegITDAATMKTFC-GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEK 123
Cdd:cd14058  122 NLLLTNGGTvLKICDFGT----ACDISTHMTNNkGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPFDHIGGPA 197
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767912019 124 LFELILMEDIKFP---RTLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd14058  198 FRIMWAVHNGERPpliKNCPKPIESLMTRCWSKDPEKR 235
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
41-172 8.21e-10

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: 57.56  E-value: 8.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  41 NISLENLML--DKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN 118
Cdd:cd14104  122 DIRPENIIYctRRGSYIKIIEFGQSRQ-LKPGDKFRLQYTSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEA 200
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767912019 119 QDHEKLFELILMEDIKFP----RTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRH 172
Cdd:cd14104  201 ETNQQTIENIRNAEYAFDdeafKNISIEALDFVDRLLVKERKSRM-----TAQEALNH 253
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
56-153 8.66e-10

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 57.66  E-value: 8.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  56 KITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN-----QDHEKLFE---- 126
Cdd:cd14038  144 KIIDLGYAKE-LDQGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFLPnwqpvQWHGKVRQksne 222
                         90       100       110
                 ....*....|....*....|....*....|....
gi 767912019 127 -LILMED----IKFPRTL--SSDAKSLLSGLLIK 153
Cdd:cd14038  223 dIVVYEDltgaVKFSSVLptPNNLNGILAGKLER 256
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
40-174 8.81e-10

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 57.35  E-value: 8.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEV--LEDN-DYGRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd06646  130 RDIKGANILLTDNGDVKLADFGVAAKITATIAKRKSFIGTPYWMAPEVaaVEKNgGYNQLCDIWAVGITAIELAELQPPM 209
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912019 117 YnqDHEKLFELILMEDIKF-PRTL------SSDAKSLLSGLLIKDPNKRlgggpDDAKEIMRHSF 174
Cdd:cd06646  210 F--DLHPMRALFLMSKSNFqPPKLkdktkwSSTFHNFVKISLTKNPKKR-----PTAERLLTHLF 267
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
45-175 9.35e-10

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: 57.67  E-value: 9.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDgHIKITDFGLCKeGITDAATMKTFCGTPEYLAPE-VLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD--- 120
Cdd:cd07831  129 ENILIKDD-ILKLADFGSCR-GIYSKPPYTEYISTRWYRAPEcLLTDGYYGPKMDIWAVGCVFFEILSLFPLFPGTNeld 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 121 -----HEKL----FELILME------DIKFPR-----------TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSF 174
Cdd:cd07831  207 qiakiHDVLgtpdAEVLKKFrksrhmNYNFPSkkgtglrkllpNASAEGLDLLKKLLAYDPDERI-----TAKQALRHPY 281

                 .
gi 767912019 175 F 175
Cdd:cd07831  282 F 282
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
40-174 1.14e-09

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


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 56.98  E-value: 1.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGH---IKITDFGLCKE--GITDAATMKTFCGTPeYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGR 113
Cdd:cd14012  128 KSLHAGNVLLDRDAGtgiVKLTDYSLGKTllDMCSRGSLDEFKQTY-WLPPELaQGSKSPTRKTDVWDLGLLFLQMLFGL 206
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912019 114 LPFYNQDHEKLFelilmediKFPRTLSSDAKSLLSGLLIKDPNKRLGggpddAKEIMRHSF 174
Cdd:cd14012  207 DVLEKYTSPNPV--------LVSLDLSASLQDFLSKCLSLDPKKRPT-----ALELLPHEF 254
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
46-176 1.23e-09

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: 57.31  E-value: 1.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCKegITDAA-----TMKTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd07849  136 NLLLNTNCDLKICDFGLAR--IADPEhdhtgFLTEYVATRWYRAPEImLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGK 213
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 120 DHEKLFELIL-------MEDIK-------------------------FPRTlSSDAKSLLSGLLIKDPNKRLgggpdDAK 167
Cdd:cd07849  214 DYLHQLNLILgilgtpsQEDLNciislkarnyikslpfkpkvpwnklFPNA-DPKALDLLDKMLTFNPHKRI-----TVE 287

                 ....*....
gi 767912019 168 EIMRHSFFS 176
Cdd:cd07849  288 EALAHPYLE 296
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
55-116 1.60e-09

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


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 56.63  E-value: 1.60e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912019  55 IKITDFGLCKEgITDAATMKTfCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd14061  142 LKITDFGLARE-WHKTTRMSA-AGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPY 201
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
41-158 1.79e-09

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 56.58  E-value: 1.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  41 NISLENLMLD--KDGHIKITDFGLCKEgiTDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN 118
Cdd:cd14147  135 ILLLQPIENDdmEHKTLKITDFGLARE--WHKTTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRG 212
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767912019 119 QDHEKLFELILMEDIKF--PRTLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd14147  213 IDCLAVAYGVAVNKLTLpiPSTCPEPFAQLMADCWAQDPHRR 254
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
40-124 2.04e-09

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: 56.60  E-value: 2.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATmkTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd06650  128 RDVKPSNILVNSRGEIKLCDFGVSGQLIDSMAN--SFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIPPP 205

                 ....*
gi 767912019 120 DHEKL 124
Cdd:cd06650  206 DAKEL 210
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
46-159 2.44e-09

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: 56.65  E-value: 2.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCKEGITDAaTMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH---- 121
Cdd:cd07850  132 NIVVKSDCTLKILDFGLARTAGTSF-MMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTVLFPGTDHidqw 210
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912019 122 EKLFELI--------------------------------LMEDIKFP-------RTLSSDAKSLLSGLLIKDPNKRL 159
Cdd:cd07850  211 NKIIEQLgtpsdefmsrlqptvrnyvenrpkyagysfeeLFPDVLFPpdseehnKLKASQARDLLSKMLVIDPEKRI 287
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
45-175 2.78e-09

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: 56.12  E-value: 2.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLML--DKDGHIKITDFGLCKEgITDAATmkTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHE 122
Cdd:cd14133  131 ENILLasYSRCQIKIIDFGSSCF-LTQRLY--SYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEV 207
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 123 KLFELILMEDIKFPRTLSSDAKS-------LLSGLLIKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd14133  208 DQLARIIGTIGIPPAHMLDQGKAddelfvdFLKKLLEIDPKERP-----TASQALSHPWL 262
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
40-174 2.84e-09

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 56.27  E-value: 2.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGRL 114
Cdd:cd06637  135 RDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMAEGAP 214
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912019 115 PFYnqDHEKLFELILMEDIKFPR----TLSSDAKSLLSGLLIKDPNKRLGggpddAKEIMRHSF 174
Cdd:cd06637  215 PLC--DMHPMRALFLIPRNPAPRlkskKWSKKFQSFIESCLVKNHSQRPS-----TEQLMKHPF 271
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
46-175 3.40e-09

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: 56.22  E-value: 3.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCK----EGITDAATMKTFCGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEM----------- 109
Cdd:cd07865  149 NILITKDGVLKLADFGLARafslAKNSQPNRYTNRVVTLWYRPPELLlGERDYGPPIDMWGAGCIMAEMwtrspimqgnt 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 110 ----------MCG-----------RLPFYNqdheklfELILMEDIKF-------PRTLSSDAKSLLSGLLIKDPNKRLgg 161
Cdd:cd07865  229 eqhqltlisqLCGsitpevwpgvdKLELFK-------KMELPQGQKRkvkerlkPYVKDPYALDLIDKLLVLDPAKRI-- 299
                        170
                 ....*....|....
gi 767912019 162 gpdDAKEIMRHSFF 175
Cdd:cd07865  300 ---DADTALNHDFF 310
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
45-158 3.44e-09

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: 55.84  E-value: 3.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKEG-------------ITDAA-----TMKTFCGTPEYLAPEVLEDND--YGRAVDWWGLGV 104
Cdd:cd14046  133 VNIFLDSNGNVKIGDFGLATSNklnvelatqdinkSTSAAlgssgDLTGNVGTALYVAPEVQSGTKstYNEKVDMYSLGI 212
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912019 105 VMYEMMcgrLPFyNQDHEKLFEL-------ILMEDiKFPRTLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd14046  213 IFFEMC---YPF-STGMERVQILtalrsvsIEFPP-DFDDNKHSKQAKLIRWLLNHDPAKR 268
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
36-176 3.49e-09

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


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 55.88  E-value: 3.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  36 QAPP---KNISLENLMLD-KDGHIKITDFGLCKEGITDAAtmKTFCGTPEYLAPEVLEDNdYGRAVDWWGLGVVMYEMMC 111
Cdd:cd14031  132 RTPPiihRDLKCDNIFITgPTGSVKIGDLGLATLMRTSFA--KSVIGTPEFMAPEMYEEH-YDESVDVYAFGMCMLEMAT 208
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912019 112 GRLPFYN-QDHEKLFELIL--MEDIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFS 176
Cdd:cd14031  209 SEYPYSEcQNAAQIYRKVTsgIKPASFNKVTDPEVKEIIEGCIRQNKSERL-----SIKDLLNHAFFA 271
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
45-175 3.76e-09

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 55.95  E-value: 3.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKE-GItdaaTMKTFCG---TPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd07836  129 QNLLINKRGELKLADFGLARAfGI----PVNTFSNevvTLWYRAPDVLlGSRTYSTSIDIWSVGCIMAEMITGRPLFPGT 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 120 DHE----KLFELILMED--------------IKFPR-----------TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIM 170
Cdd:cd07836  205 NNEdqllKIFRIMGTPTestwpgisqlpeykPTFPRyppqdlqqlfpHADPLGIDLLHRLLQLNPELRI-----SAHDAL 279

                 ....*
gi 767912019 171 RHSFF 175
Cdd:cd07836  280 QHPWF 284
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
36-175 3.77e-09

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


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 55.78  E-value: 3.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  36 QAPP---KNISLENLMLD-KDGHIKITDFGLCKegITDAATMKTFCGTPEYLAPEVLEDNdYGRAVDWWGLGVVMYEMMC 111
Cdd:cd14033  123 RCPPilhRDLKCDNIFITgPTGSVKIGDLGLAT--LKRASFAKSVIGTPEFMAPEMYEEK-YDEAVDVYAFGMCILEMAT 199
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912019 112 GRLPFYN-QDHEKLFELIL--MEDIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd14033  200 SEYPYSEcQNAAQIYRKVTsgIKPDSFYKVKVPELKEIIEGCIRTDKDERF-----TIQDLLEHRFF 261
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
40-175 3.93e-09

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: 55.84  E-value: 3.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRLPFYN 118
Cdd:cd07845  132 RDLKVSNLLLTDKGCLKIADFGLARTYGLPAKPMTPKVVTLWYRAPELLlGCTTYTTAIDMWAVGCILAELLAHKPLLPG 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 119 QDHEKLFELI-------------------LMEDIKFPRT-----------LSSDAKSLLSGLLIKDPNKRLgggpdDAKE 168
Cdd:cd07845  212 KSEIEQLDLIiqllgtpnesiwpgfsdlpLVGKFTLPKQpynnlkhkfpwLSEAGLRLLNFLLMYDPKKRA-----TAEE 286

                 ....*..
gi 767912019 169 IMRHSFF 175
Cdd:cd07845  287 ALESSYF 293
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
40-176 4.01e-09

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 55.82  E-value: 4.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVL---EDNDYGRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd06645  132 RDIKGANILLTDNGHVKLADFGVSAQITATIAKRKSFIGTPYWMAPEVAaveRKGGYNQLCDIWAVGITAIELAELQPPM 211
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912019 117 YnqDHEKLFELILMEDIKF-PRTLSSDAK------SLLSGLLIKDPNKRlgggpDDAKEIMRHSFFS 176
Cdd:cd06645  212 F--DLHPMRALFLMTKSNFqPPKLKDKMKwsnsfhHFVKMALTKNPKKR-----PTAEKLLQHPFVT 271
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
39-122 4.25e-09

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


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 55.47  E-value: 4.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  39 PKNIslenlMLDKDGHIKITDFG---LCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLP 115
Cdd:cd13979  131 PANI-----LISEQGVCKLCDFGcsvKLGEGNEVGTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELP 205

                 ....*..
gi 767912019 116 fYNQDHE 122
Cdd:cd13979  206 -YAGLRQ 211
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
40-158 4.60e-09

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


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 55.42  E-value: 4.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNq 119
Cdd:cd08229  152 RDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYG- 230
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 767912019 120 DHEKLFELI-LMEDIKFP----RTLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd08229  231 DKMNLYSLCkKIEQCDYPplpsDHYSEELRQLVNMCINPDPEKR 274
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
40-194 4.97e-09

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: 55.82  E-value: 4.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITdAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd07875  150 RDLKPSNIVVKSDCTLKILDFGLARTAGT-SFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFPGT 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 120 DH-----------------------------------------EKLF-ELILMEDIKFPRTLSSDAKSLLSGLLIKDPNK 157
Cdd:cd07875  229 DHidqwnkvieqlgtpcpefmkklqptvrtyvenrpkyagysfEKLFpDVLFPADSEHNKLKASQARDLLSKMLVIDASK 308
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767912019 158 RLggGPDDAkeiMRHSFFSgvNWQDVYDKKLVPPFKP 194
Cdd:cd07875  309 RI--SVDEA---LQHPYIN--VWYDPSEAEAPPPKIP 338
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
46-200 5.60e-09

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: 55.68  E-value: 5.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCKEGitdAATMKTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL 124
Cdd:cd07879  147 NLAVNEDCELKILDFGLARHA---DAEMTGYVVTRWYRAPEViLNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQ 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 125 FELIL-------------MEDI----------KFPR--------TLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHS 173
Cdd:cd07879  224 LTQILkvtgvpgpefvqkLEDKaaksyikslpKYPRkdfstlfpKASPQAVDLLEKMLELDVDKRL-----TATEALEHP 298
                        170       180
                 ....*....|....*....|....*..
gi 767912019 174 FFSgvNWQDVYDKKLVPPFKPQVTSET 200
Cdd:cd07879  299 YFD--SFRDADEETEQQPYDDSLENEK 323
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
59-175 5.61e-09

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: 5.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  59 DFGLCkEGITDAATMKTFC-GTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRLPFYN--QDHEKLFELIlmedik 134
Cdd:cd14019  145 DFGLA-QREEDRPEQRAPRaGTRGFRAPEVLfKCPHQTTAIDIWSAGVILLSILSGRFPFFFssDDIDALAEIA------ 217
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767912019 135 fprTL--SSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd14019  218 ---TIfgSDEAYDLLDKLLELDPSKRI-----TAEEALKHPFF 252
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
46-159 7.42e-09

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: 55.07  E-value: 7.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLED-NDYGRAVDWWGLGVVMYEMMcGRLP-FYNQDHEK 123
Cdd:cd07858  138 NLLLNANCDLKICDFGLARTTSEKGDFMTEYVVTRWYRAPELLLNcSEYTTAIDVWSVGCIFAELL-GRKPlFPGKDYVH 216
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912019 124 LFELILM-------EDIKF-------------PRT-----------LSSDAKSLLSGLLIKDPNKRL 159
Cdd:cd07858  217 QLKLITEllgspseEDLGFirnekarryirslPYTprqsfarlfphANPLAIDLLEKMLVFDPSKRI 283
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
46-177 8.29e-09

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: 55.14  E-value: 8.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLC-KEGITDAATMKTFCGTPEYLAPEVLE-DNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEK 123
Cdd:cd07853  133 NLLVNSNCVLKICDFGLArVEEPDESKHMTQEVVTQYYRAPEILMgSRHYTSAVDIWSVGCIFAELLGRRILFQAQSPIQ 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 124 LFELIL-------MEDIKFPR---------------------TLSSD----AKSLLSGLLIKDPNKRLgggpdDAKEIMR 171
Cdd:cd07853  213 QLDLITdllgtpsLEAMRSACegarahilrgphkppslpvlyTLSSQatheAVHLLCRMLVFDPDKRI-----SAADALA 287

                 ....*.
gi 767912019 172 HSFFSG 177
Cdd:cd07853  288 HPYLDE 293
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
41-158 1.03e-08

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 54.20  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  41 NISLENLMLD---KDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY 117
Cdd:cd14115  114 DIKPENLLIDlriPVPRVKLIDLEDAVQ-ISGHRHVHHLLGNPEFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFL 192
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767912019 118 NQDHEKLFELILMEDIKFPRTLSSD----AKSLLSGLLIKDPNKR 158
Cdd:cd14115  193 DESKEETCINVCRVDFSFPDEYFGDvsqaARDFINVILQEDPRRR 237
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
47-120 1.03e-08

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: 54.27  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  47 LMLDKDGH-------IKITDFGLCKEgiTDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd14146  137 LLLEKIEHddicnktLKITDFGLARE--WHRTTKMSAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGI 214

                 .
gi 767912019 120 D 120
Cdd:cd14146  215 D 215
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
28-124 1.06e-08

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 54.54  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  28 KIRFRfDLQapPKNISLENLMLDKDGHIKITDFGL----CKEGItdaatmKTFCGTPEYLAPEVLEDN-DYGRAVDWWGL 102
Cdd:cd14000  132 MIIYR-DLK--SHNVLVWTLYPNSAIIIKIADYGIsrqcCRMGA------KGSEGTPGFRAPEIARGNvIYNEKVDVFSF 202
                         90       100
                 ....*....|....*....|..
gi 767912019 103 GVVMYEMMCGRLPFynQDHEKL 124
Cdd:cd14000  203 GMLLYEILSGGAPM--VGHLKF 222
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
36-158 1.33e-08

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: 53.88  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  36 QAPP---KNISLENLMLDKDGHIKITDFG---------LCKEGITDAA---TMKTfcgTPEYLAPEVLEDNDY---GRAV 97
Cdd:cd13985  122 QSPPiihRDIKIENILFSNTGRFKLCDFGsattehyplERAEEVNIIEeeiQKNT---TPMYRAPEMIDLYSKkpiGEKA 198
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912019  98 DWWGLGVVMYEMMCGRLPFynQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd13985  199 DIWALGCLLYKLCFFKLPF--DESSKLAIVAGKYSIPEQPRYSPELHDLIRHMLTPDPAER 257
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
40-174 1.67e-08

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


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 53.86  E-value: 1.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGRL 114
Cdd:cd06638  148 RDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLRRNTSVGTPFWMAPEVIAceqqlDSTYDARCDVWSLGITAIELGDGDP 227
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912019 115 PFYN-QDHEKLFELILMEDIKF--PRTLSSDAKSLLSGLLIKDPNKRlgggpDDAKEIMRHSF 174
Cdd:cd06638  228 PLADlHPMRALFKIPRNPPPTLhqPELWSNEFNDFIRKCLTKDYEKR-----PTVSDLLQHVF 285
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
46-118 1.76e-08

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: 53.55  E-value: 1.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLckegitdaATMKTFCGTPEYL----------APEVL---EDNDYGRAVDWWGLGVVMYEMMCG 112
Cdd:cd14062  119 NIFLHEDLTVKIGDFGL--------ATVKTRWSGSQQFeqptgsilwmAPEVIrmqDENPYSFQSDVYAFGIVLYELLTG 190

                 ....*.
gi 767912019 113 RLPFYN 118
Cdd:cd14062  191 QLPYSH 196
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
40-175 1.78e-08

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


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 53.81  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGL-----CKEGITDAATmktfcgTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMcGRL 114
Cdd:cd07863  132 RDLKPENILVTSGGQVKLADFGLariysCQMALTPVVV------TLWYRAPEVLLQSTYATPVDMWSVGCIFAEMF-RRK 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 115 PFYNQDHE-----KLFELILM-------EDIKFPRT----------------LSSDAKSLLSGLLIKDPNKRLgggpdDA 166
Cdd:cd07863  205 PLFCGNSEadqlgKIFDLIGLppeddwpRDVTLPRGafsprgprpvqsvvpeIEESGAQLLLEMLTFNPHKRI-----SA 279

                 ....*....
gi 767912019 167 KEIMRHSFF 175
Cdd:cd07863  280 FRALQHPFF 288
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
55-136 1.98e-08

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 53.51  E-value: 1.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  55 IKITDFGLCKEgiTDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIK 134
Cdd:cd14145  154 LKITDFGLARE--WHRTTKMSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAMNKLS 231

                 ..
gi 767912019 135 FP 136
Cdd:cd14145  232 LP 233
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
45-175 2.28e-08

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


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 53.54  E-value: 2.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRLPF------Y 117
Cdd:cd07844  127 QNLLISERGELKLADFGLARAKSVPSKTYSNEVVTLWYRPPDVLlGSTEYSTSLDMWGVGCIFYEMATGRPLFpgstdvE 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 118 NQDHeKLFELI---------------LMEDIKFPRT-------------LSSDAKSLLSGLLIKDPNKRLGggpddAKEI 169
Cdd:cd07844  207 DQLH-KIFRVLgtpteetwpgvssnpEFKPYSFPFYpprplinhaprldRIPHGEELALKFLQYEPKKRIS-----AAEA 280

                 ....*.
gi 767912019 170 MRHSFF 175
Cdd:cd07844  281 MKHPYF 286
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
14-158 2.39e-08

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 53.38  E-value: 2.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  14 LLQRTAKEDIALPYK--IRFRFDLQA-----PPKNI-----SLENLMLDKDGHIKITDFGLCKEgITDAATMKTFCGTP- 80
Cdd:cd05074  109 LMSRIGEEPFTLPLQtlVRFMIDIASgmeylSSKNFihrdlAARNCMLNENMTVCVADFGLSKK-IYSGDYYRQGCASKl 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  81 --EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFE-LILMEDIKFPRTLSSDAKSLLSGLLIKDPN 156
Cdd:cd05074  188 pvKWLALESLADNVYTTHSDVWAFGVTMWEIMTrGQTPYAGVENSEIYNyLIKGNRLKQPPDCLEDVYELMCQCWSPEPK 267

                 ..
gi 767912019 157 KR 158
Cdd:cd05074  268 CR 269
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
46-174 2.44e-08

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 53.22  E-value: 2.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGlckegitdAATMK----TFCGTPEYLAPEV---LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN 118
Cdd:cd06607  131 NILLTEPGTVKLADFG--------SASLVcpanSFVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPLFN 202
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912019 119 QDHEKLFELILMEDikfPRTLSS-----DAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSF 174
Cdd:cd06607  203 MNAMSALYHIAQND---SPTLSSgewsdDFRNFVDSCLQKIPQDRP-----SAEDLLKHPF 255
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
45-175 2.70e-08

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: 53.32  E-value: 2.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGH--IKITDFGL-CKEGitdaATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH 121
Cdd:cd14210  145 ENILLKQPSKssIKVIDFGSsCFEG----EKVYTYIQSRFYRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGENE 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 122 EKLFELIlMEDIKFP------------------------------------RTLS-----SDAK--SLLSGLLIKDPNKR 158
Cdd:cd14210  221 EEQLACI-MEVLGVPpkslidkasrrkkffdsngkprpttnskgkkrrpgsKSLAqvlkcDDPSflDFLKKCLRWDPSER 299
                        170
                 ....*....|....*..
gi 767912019 159 LgggpdDAKEIMRHSFF 175
Cdd:cd14210  300 M-----TPEEALQHPWI 311
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
45-172 2.78e-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: 53.26  E-value: 2.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMmcgrLPFYNQDHEKL 124
Cdd:cd14047  146 SNIFLVDTGKVKIGDFGLVTS-LKNDGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFEL----LHVCDSAFEKS 220
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767912019 125 FELILMEDIKFPRTLSSDAK---SLLSGLLIKDPNKRlgggpDDAKEIMRH 172
Cdd:cd14047  221 KFWTDLRNGILPDIFDKRYKiekTIIKKMLSKKPEDR-----PNASEILRT 266
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
40-174 2.99e-08

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 53.13  E-value: 2.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGlckeGITDAATMKTFCGTPEYLAPEV---LEDNDYGRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd06635  149 RDIKAGNILLTEPGQVKLADFG----SASIASPANSFVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPL 224
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 117 YNQD-HEKLFELILMEDIKFPRTLSSDA-KSLLSGLLIKDPNKRlgggpDDAKEIMRHSF 174
Cdd:cd06635  225 FNMNaMSALYHIAQNESPTLQSNEWSDYfRNFVDSCLQKIPQDR-----PTSEELLKHMF 279
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
40-124 3.00e-08

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


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 53.51  E-value: 3.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATmkTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd06649  128 RDVKPSNILVNSRGEIKLCDFGVSGQLIDSMAN--SFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIPPP 205

                 ....*
gi 767912019 120 DHEKL 124
Cdd:cd06649  206 DAKEL 210
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
36-176 3.29e-08

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


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 52.77  E-value: 3.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  36 QAPP---KNISLENLMLD-KDGHIKITDFGLCKegITDAATMKTFCGTPEYLAPEVLEDNdYGRAVDWWGLGVVMYEMMC 111
Cdd:cd14032  123 RTPPiihRDLKCDNIFITgPTGSVKIGDLGLAT--LKRASFAKSVIGTPEFMAPEMYEEH-YDESVDVYAFGMCMLEMAT 199
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912019 112 GRLPFYN-QDHEKLFELIL--MEDIKFPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFS 176
Cdd:cd14032  200 SEYPYSEcQNAAQIYRKVTcgIKPASFEKVTDPEIKEIIGECICKNKEERY-----EIKDLLSHAFFA 262
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
40-175 3.72e-08

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 53.07  E-value: 3.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRLPFYN 118
Cdd:cd07872  128 RDLKPQNLLINERGELKLADFGLARAKSVPTKTYSNEVVTLWYRPPDVLlGSSEYSTQIDMWGVGCIFFEMASGRPLFPG 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 119 QDHEKLFELIL-------------------MEDIKFPR-----------TLSSDAKSLLSGLLIKDPNKRLgggpdDAKE 168
Cdd:cd07872  208 STVEDELHLIFrllgtpteetwpgissndeFKNYNFPKykpqplinhapRLDTEGIELLTKFLQYESKKRI-----SAEE 282

                 ....*..
gi 767912019 169 IMRHSFF 175
Cdd:cd07872  283 AMKHAYF 289
Pkinase_C pfam00433
Protein kinase C terminal domain;
196-243 3.74e-08

Protein kinase C terminal domain;


Pssm-ID: 425678 [Multi-domain]  Cd Length: 42  Bit Score: 48.35  E-value: 3.74e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 767912019  196 VTSETDTRYFDEEFTAQTITITPPEKydedgmDCMDNERRPHFPQFSY 243
Cdd:pfam00433   1 VKSETDTSNFDPEFTEEPPVLTPPDS------SILSSIDQEEFRGFSY 42
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
56-154 3.94e-08

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 53.59  E-value: 3.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019   56 KITDFGLCKE-GITDAAtmKTFCGTPEYLAPEVL--EDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHeklFELILMED 132
Cdd:PTZ00266  182 KIGDFGLSKNiGIESMA--HSCVGTPYYWSPELLlhETKSYDDKSDMWALGCIIYELCSGKTPFHKANN---FSQLISEL 256
                          90       100
                  ....*....|....*....|..
gi 767912019  133 IKFPRtLSSDAKSLLSGLLIKD 154
Cdd:PTZ00266  257 KRGPD-LPIKGKSKELNILIKN 277
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
39-175 4.14e-08

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: 52.66  E-value: 4.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  39 PKNISLENLMLDKDGHIKITDFGLCKEGITDAATMK---TFCGTPEYLAPEVLEDNDYGR---AVDWWGLGVVMYEMMC- 111
Cdd:cd13982  127 PQNILISTPNAHGNVRAMISDFGLCKKLDVGRSSFSrrsGVAGTSGWIAPEMLSGSTKRRqtrAVDIFSLGCVFYYVLSg 206
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912019 112 GRLPF-------YNQDHEKLFELILMEDIKFPrtlsSDAKSLLSGLLIKDPNKRlgggPdDAKEIMRHSFF 175
Cdd:cd13982  207 GSHPFgdklereANILKGKYSLDKLLSLGEHG----PEAQDLIERMIDFDPEKR----P-SAEEVLNHPFF 268
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
40-174 4.24e-08

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 52.70  E-value: 4.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGRL 114
Cdd:cd06636  145 RDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAP 224
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912019 115 PFYnqDHEKLFELILMEDIKFPRTLSSDAK----SLLSGLLIKDPNKRlgggpDDAKEIMRHSF 174
Cdd:cd06636  225 PLC--DMHPMRALFLIPRNPPPKLKSKKWSkkfiDFIEGCLVKNYLSR-----PSTEQLLKHPF 281
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
40-116 4.86e-08

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: 52.49  E-value: 4.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLM--LDKDGH--IKITDFGLCKEgITDAATMKTFCGTPEYLAPEVLE--------DNDYGRAVDWWGLGVVMY 107
Cdd:cd13988  120 RDIKPGNIMrvIGEDGQsvYKLTDFGAARE-LEDDEQFVSLYGTEEYLHPDMYEravlrkdhQKKYGATVDLWSIGVTFY 198

                 ....*....
gi 767912019 108 EMMCGRLPF 116
Cdd:cd13988  199 HAATGSLPF 207
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
55-120 5.40e-08

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 52.30  E-value: 5.40e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912019  55 IKITDFGLCKEgiTDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD 120
Cdd:cd14148  142 LKITDFGLARE--WHKTTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREID 205
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
46-177 5.46e-08

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: 52.75  E-value: 5.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCKEGITDAATMKTF----CGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQD 120
Cdd:cd07855  139 NLLVNENCELKIGDFGMARGLCTSPEEHKYFmteyVATRWYRAPELmLSLPEYTQAIDMWSVGCIFAEMLGRRQLFPGKN 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 121 HEKLFELILM----------EDIKFPRT---------------------LSSDAKSLLSGLLIKDPNKRLgggpdDAKEI 169
Cdd:cd07855  219 YVHQLQLILTvlgtpsqaviNAIGADRVrryiqnlpnkqpvpwetlypkADQQALDLLSQMLRFDPSERI-----TVAEA 293

                 ....*...
gi 767912019 170 MRHSFFSG 177
Cdd:cd07855  294 LQHPFLAK 301
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
35-175 6.29e-08

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: 51.83  E-value: 6.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  35 LQAPPKNIslenLMLD-KDGHIKITDFGLCKEGITDAatmKTFC--GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC 111
Cdd:cd14108  121 LDLKPENL----LMADqKTDQVRICDFGNAQELTPNE---PQYCkyGTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLT 193
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912019 112 GRLPFYNQDHEKLFELILMEDIKFPRT----LSSDAKSLLSGLLIKDpnkRLgggPDDAKEIMRHSFF 175
Cdd:cd14108  194 GISPFVGENDRTTLMNIRNYNVAFEESmfkdLCREAKGFIIKVLVSD---RL---RPDAEETLEHPWF 255
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
41-175 7.89e-08

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


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 51.94  E-value: 7.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  41 NISLENLMLDKDGHIKITDFGLC--KEGITDAATMKTFCG---------TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEM 109
Cdd:cd14011  140 NICPESVVINSNGEWKLAGFDFCisSEQATDQFPYFREYDpnlpplaqpNLNYLAPEYILSKTCDPASDMFSLGVLIYAI 219
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912019 110 MC-GRLPF--------YNQDHEKLFELILMEDIKFPRTLSSDAKSLLSglliKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd14011  220 YNkGKPLFdcvnnllsYKKNSNQLRQLSLSLLEKVPEELRDHVKTLLN----VTPEVRP-----DAEQLSKIPFF 285
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
25-116 9.77e-08

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 51.34  E-value: 9.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  25 LPYKIRFRFDLQ-----------APP---KNISLENLMLDKDGHIKITDFGL--CKEGITDA-ATMKTFCGTPEYLAPE- 86
Cdd:cd14025   89 LPWELRFRIIHEtavgmnflhcmKPPllhLDLKPANILLDAHYHVKISDFGLakWNGLSHSHdLSRDGLRGTIAYLPPEr 168
                         90       100       110
                 ....*....|....*....|....*....|.
gi 767912019  87 VLEDND-YGRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd14025  169 FKEKNRcPDTKHDVYSFAIVIWGILTQKKPF 199
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
40-175 1.03e-07

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 51.65  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRlPFYN 118
Cdd:cd07846  124 RDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDYVATRWYRAPELLvGDTKYGKAVDVWAVGCLVTEMLTGE-PLFP 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 119 QD-------------------HEKLF---------------ELILMEDiKFPRtLSSDAKSLLSGLLIKDPNKRLGGGpd 164
Cdd:cd07846  203 GDsdidqlyhiikclgnliprHQELFqknplfagvrlpevkEVEPLER-RYPK-LSGVVIDLAKKCLHIDPDKRPSCS-- 278
                        170
                 ....*....|.
gi 767912019 165 dakEIMRHSFF 175
Cdd:cd07846  279 ---ELLHHEFF 286
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
40-128 1.35e-07

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 51.22  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLC--KEGITDAATMKTFCGTPEYLAPEVL---EDNDYGRAVDWWGLGVVMYEMMCGRL 114
Cdd:cd14151  128 RDLKSNNIFLHEDLTVKIGDFGLAtvKSRWSGSHQFEQLSGSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQL 207
                         90
                 ....*....|....*
gi 767912019 115 PFYN-QDHEKLFELI 128
Cdd:cd14151  208 PYSNiNNRDQIIFMV 222
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
40-158 2.98e-07

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 50.38  E-value: 2.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMMCGRL 114
Cdd:cd06639  152 RDVKGNNILLTTEGGVKLVDFGVSAQLTSARLRRNTSVGTPFWMAPEVIAceqqyDYSYDARCDVWSLGITAIELADGDP 231
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767912019 115 PFYNQDHEK-LFEL------ILMEDIKFPRTLSsdakSLLSGLLIKDPNKR 158
Cdd:cd06639  232 PLFDMHPVKaLFKIprnpppTLLNPEKWCRGFS----HFISQCLIKDFEKR 278
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
40-191 3.95e-07

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: 50.09  E-value: 3.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITdAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQ 119
Cdd:cd07874  143 RDLKPSNIVVKSDCTLKILDFGLARTAGT-SFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGR 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 120 DH----EKLFELI--------------------------------LMEDIKFP------RTLSSDAKSLLSGLLIKDPNK 157
Cdd:cd07874  222 DYidqwNKVIEQLgtpcpefmkklqptvrnyvenrpkyagltfpkLFPDSLFPadsehnKLKASQARDLLSKMLVIDPAK 301
                        170       180       190
                 ....*....|....*....|....*....|....
gi 767912019 158 RLggGPDDAkeiMRHSFFSgvNWQDVYDKKLVPP 191
Cdd:cd07874  302 RI--SVDEA---LQHPYIN--VWYDPAEVEAPPP 328
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
40-118 4.61e-07

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 49.63  E-value: 4.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLC--KEGITDAATMKTFCGTPEYLAPEVL---EDNDYGRAVDWWGLGVVMYEMMCGRL 114
Cdd:cd14150  120 RDLKSNNIFLHEGLTVKIGDFGLAtvKTRWSGSQQVEQPSGSILWMAPEVIrmqDTNPYSFQSDVYAYGVVLYELMSGTL 199

                 ....
gi 767912019 115 PFYN 118
Cdd:cd14150  200 PYSN 203
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
36-175 4.82e-07

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


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 49.66  E-value: 4.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  36 QAPP---KNISLENLMLD-KDGHIKITDFGLCKegITDAATMKTFCGTPEYLAPEVLEDNdYGRAVDWWGLGVVMYEMMC 111
Cdd:cd14030  147 RTPPiihRDLKCDNIFITgPTGSVKIGDLGLAT--LKRASFAKSVIGTPEFMAPEMYEEK-YDESVDVYAFGMCMLEMAT 223
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912019 112 GRLPFYN-QDHEKLFELIL--MEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGggpddAKEIMRHSFF 175
Cdd:cd14030  224 SEYPYSEcQNAAQIYRRVTsgVKPASFDKVAIPEVKEIIEGCIRQNKDERYA-----IKDLLNHAFF 285
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
46-175 5.40e-07

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: 49.53  E-value: 5.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLED-NDYGRAVDWWGLGVVMYEMMCGRlPFYNQDHE-- 122
Cdd:cd07843  136 NLLLNNRGILKICDFGLAREYGSPLKPYTQLVVTLWYRAPELLLGaKEYSTAIDMWSVGCIFAELLTKK-PLFPGKSEid 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 123 ---KLFELILM--EDI-------------------------KFPRTLSSDAK-SLLSGLLIKDPNKRLgggpdDAKEIMR 171
Cdd:cd07843  215 qlnKIFKLLGTptEKIwpgfselpgakkktftkypynqlrkKFPALSLSDNGfDLLNRLLTYDPAKRI-----SAEDALK 289

                 ....
gi 767912019 172 HSFF 175
Cdd:cd07843  290 HPYF 293
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
40-147 5.43e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 49.61  E-value: 5.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGL-CKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFY- 117
Cdd:PHA03212 206 RDIKAENIFINHPGDVCLGDFGAaCFPVDINANKYYGWAGTIATNAPELLARDPYGPAVDIWSAGIVLFEMATCHDSLFe 285
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767912019 118 ------NQDHEKLFELILMEDIKFPRTLSSDAKSLL 147
Cdd:PHA03212 286 kdgldgDCDSDRQIKLIIRRSGTHPNEFPIDAQANL 321
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
46-158 5.88e-07

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 49.22  E-value: 5.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCK------EGITDAATMKTFC---GTPEYLAPE---VLEDNDYGRAVDWWGLGVVMYEMMCGR 113
Cdd:cd13986  139 NVLLSEDDEPILMDLGSMNparieiEGRREALALQDWAaehCTMPYRAPElfdVKSHCTIDEKTDIWSLGCTLYALMYGE 218
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767912019 114 LPFyNQDHEK---LFELILMEDIKFPRT--LSSDAKSLLSGLLIKDPNKR 158
Cdd:cd13986  219 SPF-ERIFQKgdsLALAVLSGNYSFPDNsrYSEELHQLVKSMLVVNPAER 267
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
39-176 6.88e-07

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: 49.39  E-value: 6.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  39 PKN--ISLENLMLdkdghiKITDFGLCKegITDAA-------TMKTFcgTPEYLAPE-VLEDNDYGRAVDWWGLGVVMYE 108
Cdd:cd07854  142 PANvfINTEDLVL------KIGDFGLAR--IVDPHyshkgylSEGLV--TKWYRSPRlLLSPNNYTKAIDMWAAGCIFAE 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 109 MMCGRlPFYNQDHE-KLFELIL----------------------MEDIKFPR--------TLSSDAKSLLSGLLIKDPNK 157
Cdd:cd07854  212 MLTGK-PLFAGAHElEQMQLILesvpvvreedrnellnvipsfvRNDGGEPRrplrdllpGVNPEALDFLEQILTFNPMD 290
                        170
                 ....*....|....*....
gi 767912019 158 RLgggpdDAKEIMRHSFFS 176
Cdd:cd07854  291 RL-----TAEEALMHPYMS 304
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
40-109 7.33e-07

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 49.12  E-value: 7.33e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCK--EGITDAATMKTFCGTPEY-LAPEVLEDNDYGRAVDWWGLGVVMYEM 109
Cdd:cd05081  132 RDLAARNILVESEAHVKIADFGLAKllPLDKDYYVVREPGQSPIFwYAPESLSDNIFSRQSDVWSFGVVLYEL 204
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
40-128 8.15e-07

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: 48.79  E-value: 8.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFY 117
Cdd:cd05112  124 RDLAARNCLVGENQVVKVSDFGMTRFVLDDQYTSSTGTKFPvKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYE 203
                         90
                 ....*....|.
gi 767912019 118 NQDHEKLFELI 128
Cdd:cd05112  204 NRSNSEVVEDI 214
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
40-175 1.05e-06

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 48.60  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCG---------TPE-----YLAPEVL-EDNDYGRAVDWWGLGV 104
Cdd:PTZ00024 143 RDLSPANIFINSKGICKIADFGLARRYGYPPYSDTLSKDetmqrreemTSKvvtlwYRAPELLmGAEKYHFAVDMWSVGC 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 105 VMYEMMCGRlPFYNQDHE-----KLFELI-LMEDIKFPRTL-----------------------SSDAKSLLSGLLIKDP 155
Cdd:PTZ00024 223 IFAELLTGK-PLFPGENEidqlgRIFELLgTPNEDNWPQAKklplyteftprkpkdlktifpnaSDDAIDLLQSLLKLNP 301
                        170       180
                 ....*....|....*....|
gi 767912019 156 NKRLgggpdDAKEIMRHSFF 175
Cdd:PTZ00024 302 LERI-----SAKEALKHEYF 316
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
33-147 1.06e-06

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 48.51  E-value: 1.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  33 FDLQapPKNIslenLMLDKD--GHIKITDFGLCK------EGITDAATMKTFCGTPEYLAPEVL----EDNDYGRAVDWW 100
Cdd:cd14040  137 YDLK--PGNI----LLVDGTacGEIKITDFGLSKimdddsYGVDGMDLTSQGAGTYWYLPPECFvvgkEPPKISNKVDVW 210
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767912019 101 GLGVVMYEMMCGRLPF-YNQDHEKLFE---LILMEDIKFP--RTLSSDAKSLL 147
Cdd:cd14040  211 SVGVIFFQCLYGRKPFgHNQSQQDILQentILKATEVQFPvkPVVSNEAKAFI 263
pknD PRK13184
serine/threonine-protein kinase PknD;
40-158 1.29e-06

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 49.00  E-value: 1.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCK-------EGITDAATMKTFC-----------GTPEYLAPEVLEDNDYGRAVDWWG 101
Cdd:PRK13184 137 RDLKPDNILLGLFGEVVILDWGAAIfkkleeeDLLDIDVDERNICyssmtipgkivGTPDYMAPERLLGVPASESTDIYA 216
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912019 102 LGVVMYEMMCGRLPFYNQDHEKlfeLILMEDIKFPRTLS--SDAKSLLSGLLIK----DPNKR 158
Cdd:PRK13184 217 LGVILYQMLTLSFPYRRKKGRK---ISYRDVILSPIEVApyREIPPFLSQIAMKalavDPAER 276
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
40-159 1.64e-06

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 48.49  E-value: 1.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGH-IKITDFGLCKEGITDAATMKTFCgTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFY 117
Cdd:PTZ00036 194 RDLKPQNLLIDPNTHtLKLCDFGSAKNLLAGQRSVSYIC-SRFYRAPELmLGATNYTTHIDLWSLGCIIAEMILGYPIFS 272
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912019 118 NQDH-EKLFELILM----------------EDIKFPRTLSSDAK------------SLLSGLLIKDPNKRL 159
Cdd:PTZ00036 273 GQSSvDQLVRIIQVlgtptedqlkemnpnyADIKFPDVKPKDLKkvfpkgtpddaiNFISQFLKYEPLKRL 343
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
15-163 1.85e-06

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: 47.64  E-value: 1.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  15 LQRTAKEDIALPYKIRFRF---------DLQapPKNISLENLMLDKDGHIKITDFGL----CKEGItdaatmKTFCGTPE 81
Cdd:cd14068   83 LTRTLQHRIALHVADGLRYlhsamiiyrDLK--PHNVLLFTLYPNCAIIAKIADYGIaqycCRMGI------KTSEGTPG 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  82 YLAPEVLEDN-DYGRAVDWWGLGVVMYEMM-CGRLpfynqdheklfeliLMEDIKFPRTLSSDAkslLSGLLiKDPNKRL 159
Cdd:cd14068  155 FRAPEVARGNvIYNQQADVYSFGLLLYDILtCGER--------------IVEGLKFPNEFDELA---IQGKL-PDPVKEY 216

                 ....
gi 767912019 160 GGGP 163
Cdd:cd14068  217 GCAP 220
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
40-109 1.97e-06

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


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 47.76  E-value: 1.97e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCK--EGITDAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEM 109
Cdd:cd05038  133 RDLAARNILVESEDLVKISDFGLAKvlPEDKEYYYVKEPGESPiFWYAPECLRESRFSSASDVWSFGVTLYEL 205
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
40-120 1.98e-06

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 47.71  E-value: 1.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGlckeGITDAATMKTFCGTPEYLAPEV---LEDNDYGRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd06634  139 RDVKAGNILLTEPGLVKLGDFG----SASIMAPANSFVGTPYWMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPL 214

                 ....
gi 767912019 117 YNQD 120
Cdd:cd06634  215 FNMN 218
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
35-151 2.31e-06

kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to the C-terminal protein kinase catalytic fold (C lobe). Its presence at the N terminus of signalling proteins and the absence of the active-site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurrence of KIND only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features


Pssm-ID: 214801  Cd Length: 176  Bit Score: 46.62  E-value: 2.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019    35 LQAPPKNISLENLMLDKDGHIKItdFGLCkeGITDAATMKtfcGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRL 114
Cdd:smart00750  30 LRELHRQAKSGNILLTWDGLLKL--DGSV--AFKTPEQSR---PDPYFMAPEVIQGQSYTEKADIYSLGITLYEALDYEL 102
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 767912019   115 PfYNQDHEklFELILMEDIKFPRTLSSDAKSLLSGLL 151
Cdd:smart00750 103 P-YNEERE--LSAILEILLNGMPADDPRDRSNLEGVS 136
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
40-122 2.57e-06

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 47.34  E-value: 2.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENlmldkdGHIKITDFGLCK-EGITDAATMKTFCGTPE----YLAPEVL----------EDNDYGRAVDWWGLGV 104
Cdd:cd14063  126 KNIFLEN------GRVVITDFGLFSlSGLLQPGRREDTLVIPNgwlcYLAPEIIralspdldfeESLPFTKASDVYAFGT 199
                         90
                 ....*....|....*...
gi 767912019 105 VMYEMMCGRLPFYNQDHE 122
Cdd:cd14063  200 VWYELLAGRWPFKEQPAE 217
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
14-116 2.64e-06

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 47.22  E-value: 2.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  14 LLQRTAKEDIALPYKIRFRFDL---------QAPP---KNISLENLMLDKDGHIKITDFGLCK---EGITDAATMKTF-- 76
Cdd:cd14026   88 LHEKDIYPDVAWPLRLRILYEIalgvnylhnMSPPllhHDLKTQNILLDGEFHVKIADFGLSKwrqLSISQSRSSKSApe 167
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767912019  77 CGTPEYLAPEVLEDNDYGRAV---DWWGLGVVMYEMMCGRLPF 116
Cdd:cd14026  168 GGTIIYMPPEEYEPSQKRRASvkhDIYSYAIIMWEVLSRKIPF 210
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
40-127 2.91e-06

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 47.30  E-value: 2.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCK---EGitDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRlPF 116
Cdd:cd07848  124 RDIKPENLLISHNDVLKLCDFGFARnlsEG--SNANYTEYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQ-PL 200
                         90
                 ....*....|...
gi 767912019 117 YNQDHE--KLFEL 127
Cdd:cd07848  201 FPGESEidQLFTI 213
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
36-116 3.05e-06

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 46.87  E-value: 3.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  36 QAPPKNISLE----NLMLDKDGHIKITDFGLCKegITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC 111
Cdd:cd14060  103 EAPVKVIHRDlksrNVVIAADGVLKICDFGASR--FHSHTTHMSLVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLT 180

                 ....*
gi 767912019 112 GRLPF 116
Cdd:cd14060  181 REVPF 185
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
33-159 3.29e-06

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


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 46.98  E-value: 3.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  33 FDLQapPKNISLENLMldKDGHIKITDFGLCK------EGITDAATMKT-FCGTPEYLAPEVL----EDNDYGRAVDWWG 101
Cdd:cd14041  137 YDLK--PGNILLVNGT--ACGEIKITDFGLSKimdddsYNSVDGMELTSqGAGTYWYLPPECFvvgkEPPKISNKVDVWS 212
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912019 102 LGVVMYEMMCGRLPF-YNQDHEKLFE---LILMEDIKFPRT--LSSDAKSLLSGLLIKDPNKRL 159
Cdd:cd14041  213 VGVIFYQCLYGRKPFgHNQSQQDILQentILKATEVQFPPKpvVTPEAKAFIRRCLAYRKEDRI 276
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
40-117 3.60e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 47.15  E-value: 3.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGL-CKegiTDAATMKTFC----GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRL 114
Cdd:PHA03207 209 RDVKTENIFLDEPENAVLGDFGAaCK---LDAHPDTPQCygwsGTLETNSPELLALDPYCAKTDIWSAGLVLFEMSVKNV 285

                 ...
gi 767912019 115 PFY 117
Cdd:PHA03207 286 TLF 288
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
40-110 3.73e-06

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


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 46.85  E-value: 3.73e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAA--TMKTFCGTPEY-LAPEVLEDNDYGRAVDWWGLGVVMYEMM 110
Cdd:cd05079  133 RDLAARNVLVESEHQVKIGDFGLTKAIETDKEyyTVKDDLDSPVFwYAPECLIQSKFYIASDVWSFGVTLYELL 206
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
46-130 5.32e-06

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: 46.29  E-value: 5.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMM-CGRLPFYNQDHEK 123
Cdd:cd05059  130 NCLVGEQNVVKVSDFGLARYVLDDEYTSSVGTKFPvKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFsEGKMPYERFSNSE 209

                 ....*..
gi 767912019 124 LFELILM 130
Cdd:cd05059  210 VVEHISQ 216
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
38-158 5.84e-06

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 46.12  E-value: 5.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  38 PP---KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFC---------GTPEYLAPEVLedNDYGRAV-----DWW 100
Cdd:cd14037  129 PPlihRDLKVENVLISDSGNYKLCDFGSATTKILPPQTKQGVTyveedikkyTTLQYRAPEMI--DLYRGKPiteksDIW 206
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912019 101 GLGVVMYemmcgRLPFYNQDHEKLFEL-ILMEDIKFP--RTLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd14037  207 ALGCLLY-----KLCFYTTPFEESGQLaILNGNFTFPdnSRYSKRLHKLIRYMLEEDPEKR 262
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
40-158 5.89e-06

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 46.49  E-value: 5.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCG-TP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 116
Cdd:cd05045  151 RDLAARNVLVAEGRKMKISDFGLSRDVYEEDSYVKRSKGrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPY 230
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767912019 117 YNQDHEKLFELI----LMEDikfPRTLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd05045  231 PGIAPERLFNLLktgyRMER---PENCSEEMYNLMLTCWKQEPDKR 273
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
51-175 6.10e-06

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: 46.40  E-value: 6.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  51 KDGHIKITDFGlckegitdAATMK-----TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFynQDHEKLF 125
Cdd:cd14134  169 KSTDIKLIDFG--------SATFDdeyhsSIVSTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTGELLF--QTHDNLE 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 126 ELILMEDI--KFPRTLSSDAKS-----------------------------------------------LLSGLLIKDPN 156
Cdd:cd14134  239 HLAMMERIlgPLPKRMIRRAKKgakyfyfyhgrldwpegsssgrsikrvckplkrlmllvdpehrllfdLIRKMLEYDPS 318
                        170
                 ....*....|....*....
gi 767912019 157 KRLgggpdDAKEIMRHSFF 175
Cdd:cd14134  319 KRI-----TAKEALKHPFF 332
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
46-158 6.97e-06

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


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 45.84  E-value: 6.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLckEGITDAATMKTFCGTPE-----YLAPEVLEDNDYGR----AVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd13992  128 NCLVDSRWVVKLTDFGL--RNLLEEQTNHQLDEDAQhkkllWTAPELLRGSLLEVrgtqKGDVYSFAIILYEILFRSDPF 205
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767912019 117 YNQDHEKLFELILMEDIKFPR---TLSSDAKSLLSGLLIK-----DPNKR 158
Cdd:cd13992  206 ALEREVAIVEKVISGGNKPFRpelAVLLDEFPPRLVLLVKqcwaeNPEKR 255
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
40-163 8.33e-06

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 45.79  E-value: 8.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCgTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMcGRLPFY-- 117
Cdd:cd07862  134 RDLKPQNILVTSSGQIKLADFGLARIYSFQMALTSVVV-TLWYRAPEVLLQSSYATPVDLWSVGCIFAEMF-RRKPLFrg 211
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912019 118 NQDHE---KLFELILM-------EDIKFPRTLSSD----------------AKSLLSGLLIKDPNKRLGGGP 163
Cdd:cd07862  212 SSDVDqlgKILDVIGLpgeedwpRDVALPRQAFHSksaqpiekfvtdidelGKDLLLKCLTFNPAKRISAYS 283
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
46-108 8.68e-06

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 45.88  E-value: 8.68e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912019  46 NLMLDKDGHIKITDFGlckegitdaatMKTFCGTP---------EYLAPEVLEDNDYGRAVDWWGLGVVMYE 108
Cdd:cd14052  136 NVLITFEGTLKIGDFG-----------MATVWPLIrgieregdrEYIAPEILSEHMYDKPADIFSLGLILLE 196
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
40-174 8.99e-06

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: 45.95  E-value: 8.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAA---TMKTFcgTPEYLAPE-VLEDNDYGRAVDWWGLGVVMYEM------ 109
Cdd:cd07864  140 RDIKCSNILLNNKGQIKLADFGLARLYNSEESrpyTNKVI--TLWYRPPElLLGEERYGPAIDVWSCGCILGELftkkpi 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 110 ---------------MCG-----------RLPFYNQ-DHEKLFELILMEDIKFprtLSSDAKSLLSGLLIKDPNKRLggg 162
Cdd:cd07864  218 fqanqelaqlelisrLCGspcpavwpdviKLPYFNTmKPKKQYRRRLREEFSF---IPTPALDLLDHMLTLDPSKRC--- 291
                        170
                 ....*....|..
gi 767912019 163 pdDAKEIMRHSF 174
Cdd:cd07864  292 --TAEQALNSPW 301
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
36-159 9.09e-06

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 45.58  E-value: 9.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  36 QAPP---KNISLENLMLDKDGHIKITDFG---------------LCKEGITDAATMKTfcgTPEYLAPEVLE---DNDYG 94
Cdd:cd14036  127 QSPPiihRDLKIENLLIGNQGQIKLCDFGsatteahypdyswsaQKRSLVEDEITRNT---TPMYRTPEMIDlysNYPIG 203
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  95 RAVDWWGLGVVMYEMMCGRLPFynQDHEKLfeLILMEDIKFPrtlSSDAK-----SLLSGLLIKDPNKRL 159
Cdd:cd14036  204 EKQDIWALGCILYLLCFRKHPF--EDGAKL--RIINAKYTIP---PNDTQytvfhDLIRSTLKVNPEERL 266
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
40-116 9.65e-06

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: 45.36  E-value: 9.65e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGitdAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 116
Cdd:cd05082  126 RDLAARNVLVSEDNVAKVSDFGLTKEA---SSTQDTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPY 200
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
46-159 1.10e-05

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: 45.64  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCKegITDAaTMKTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKL 124
Cdd:cd07856  138 NILVNENCDLKICDFGLAR--IQDP-QMTGYVSTRYYRAPEImLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQ 214
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912019 125 FELI----------LMEDI----------------------KFPrTLSSDAKSLLSGLLIKDPNKRL 159
Cdd:cd07856  215 FSIItellgtppddVINTIcsentlrfvqslpkrervpfseKFK-NADPDAIDLLEKMLVFDPKKRI 280
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
40-110 1.13e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 45.64  E-value: 1.13e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKtFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMM 110
Cdd:PHA03209 181 RDVKTENIFINDVDQVCIGDLGAAQFPVVAPAFLG-LAGTVETNAPEVLARDKYNSKADIWSAGIVLFEML 250
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
46-111 1.16e-05

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


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 45.34  E-value: 1.16e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912019  46 NLMLDKDGHIKITDFGLCKEGITDAATMK----TFCGTPEYLAPEVLEDN------DYGRAVDWWGLGVVMYEMMC 111
Cdd:cd14056  130 NILVKRDGTCCIADLGLAVRYDSDTNTIDippnPRVGTKRYMAPEVLDDSinpksfESFKMADIYSFGLVLWEIAR 205
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
41-115 1.26e-05

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. 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 LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 45.34  E-value: 1.26e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912019  41 NISLENLMLDKDGHIKITDFGLCKEGITDAATMKTfcGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLP 115
Cdd:cd14067  144 NILVWSLDVQEHINIKLSDYGISRQSFHEGALGVE--GTPGYQAPEIRPRIVYDEKVDMFSYGMVLYELLSGQRP 216
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
50-175 1.46e-05

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: 45.35  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  50 DKDGHIKITDFGLCKegITDAATMKTFCGTPE-----YLAPEV-LEDNDYGRAVDWWGLGVVMYEM-------------M 110
Cdd:cd07842  146 PERGVVKIGDLGLAR--LFNAPLKPLADLDPVvvtiwYRAPELlLGARHYTKAIDIWAIGCIFAELltlepifkgreakI 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 111 CGRLPFYNQDHEKLFELI-------------------LMEDIKF--------------PRTLSSDAKSLLSGLLIKDPNK 157
Cdd:cd07842  224 KKSNPFQRDQLERIFEVLgtptekdwpdikkmpeydtLKSDTKAstypnsllakwmhkHKKPDSQGFDLLRKLLEYDPTK 303
                        170
                 ....*....|....*...
gi 767912019 158 RLgggpdDAKEIMRHSFF 175
Cdd:cd07842  304 RI-----TAEEALEHPYF 316
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
40-128 1.46e-05

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


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 45.34  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKeGITDAATMK-TFCG-TP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLP 115
Cdd:cd05099  158 RDLAARNVLVTEDNVMKIADFGLAR-GVHDIDYYKkTSNGrLPvKWMAPEALFDRVYTHQSDVWSFGILMWEIFTlGGSP 236
                         90
                 ....*....|...
gi 767912019 116 FYNQDHEKLFELI 128
Cdd:cd05099  237 YPGIPVEELFKLL 249
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
40-124 1.54e-05

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 45.13  E-value: 1.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKegitDAATMKTFC-GTPEY-----LAPEVLEDNDYGRAVDWWGLGVVMYEMMC-G 112
Cdd:cd05043  140 KDIAARNCVIDDELQVKITDNALSR----DLFPMDYHClGDNENrpikwMSLESLVNKEYSSASDVWSFGVLLWELMTlG 215
                         90
                 ....*....|..
gi 767912019 113 RLPFYNQDHEKL 124
Cdd:cd05043  216 QTPYVEIDPFEM 227
PHA02988 PHA02988
hypothetical protein; Provisional
38-136 1.78e-05

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 44.73  E-value: 1.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  38 PPKNISLENLMLDKDGHIKITDFGLckEGITDAATMKTFcGTPEYLAPEVLED--NDYGRAVDWWGLGVVMYEMMCGRLP 115
Cdd:PHA02988 145 PYKNLTSVSFLVTENYKLKIICHGL--EKILSSPPFKNV-NFMVYFSYKMLNDifSEYTIKDDIYSLGVVLWEIFTGKIP 221
                         90       100
                 ....*....|....*....|.
gi 767912019 116 FYNQDHEKLFELILMEDIKFP 136
Cdd:PHA02988 222 FENLTTKEIYDLIINKNNSLK 242
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
16-128 2.13e-05

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 44.62  E-value: 2.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  16 QRTAKEDIALPYKIRFRFDLQAPPK----NISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCG--TPEYLAPEVLE 89
Cdd:cd05101  142 QMTFKDLVSCTYQLARGMEYLASQKcihrDLAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGrlPVKWMAPEALF 221
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767912019  90 DNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELI 128
Cdd:cd05101  222 DRVYTHQSDVWSFGVLMWEIFTlGGSPYPGIPVEELFKLL 261
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
16-128 2.15e-05

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


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 44.62  E-value: 2.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  16 QRTAKEDIALPYKIRFRFDLQAPPK----NISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCG--TPEYLAPEVLE 89
Cdd:cd05098  131 QLSSKDLVSCAYQVARGMEYLASKKcihrDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGrlPVKWMAPEALF 210
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767912019  90 DNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELI 128
Cdd:cd05098  211 DRIYTHQSDVWSFGVLLWEIFTlGGSPYPGVPVEELFKLL 250
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
40-116 2.25e-05

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: 44.49  E-value: 2.25e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 116
Cdd:cd05113  124 RDLAARNCLVNDQGVVKVSDFGLSRYVLDDEYTSSVGSKFPvRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlGKMPY 202
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
40-116 2.31e-05

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 44.41  E-value: 2.31e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCK-EGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd14664  121 RDVKSNNILLDEEFEAHVADFGLAKlMDDKDSHVMSSVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPF 198
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
29-120 2.61e-05

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: 44.09  E-value: 2.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  29 IRFRFDLQAPPKNISLENLMLDKDGHIKITDFGLCK--EGITDAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVV 105
Cdd:cd05066  119 MKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRvlEDDPEAAYTTRGGKIPiRWTAPEAIAYRKFTSASDVWSYGIV 198
                         90
                 ....*....|....*....
gi 767912019 106 MYEMMC-GRLPFY---NQD 120
Cdd:cd05066  199 MWEVMSyGERPYWemsNQD 217
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
40-128 3.08e-05

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 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: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 44.23  E-value: 3.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEgitdAATMKTFCGTPE------YLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-G 112
Cdd:cd05090  148 KDLAARNILVGEQLHVKISDLGLSRE----IYSSDYYRVQNKsllpirWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfG 223
                         90
                 ....*....|....*.
gi 767912019 113 RLPFYNQDHEKLFELI 128
Cdd:cd05090  224 LQPYYGFSNQEVIEMV 239
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
16-128 3.11e-05

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


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 44.24  E-value: 3.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  16 QRTAKEDIALPYKIRFRFDLQAPPK----NISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCG--TPEYLAPEVLE 89
Cdd:cd05100  130 QLTFKDLVSCAYQVARGMEYLASQKcihrDLAARNVLVTEDNVMKIADFGLARDVHNIDYYKKTTNGrlPVKWMAPEALF 209
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767912019  90 DNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELI 128
Cdd:cd05100  210 DRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFKLL 249
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
40-116 3.49e-05

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 43.80  E-value: 3.49e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd07870  122 RDLKPQNLLISYLGELKLADFGLARAKSIPSQTYSSEVVTLWYRPPDVLlGATDYSSALDIWGAGCIFIEMLQGQPAF 199
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
40-128 3.55e-05

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: 43.70  E-value: 3.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFY 117
Cdd:cd05114  124 RDLAARNCLVNDTGVVKVSDFGMTRYVLDDQYTSSSGAKFPvKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTeGKMPFE 203
                         90
                 ....*....|.
gi 767912019 118 NQDHEKLFELI 128
Cdd:cd05114  204 SKSNYEVVEMV 214
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
45-175 3.57e-05

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 44.04  E-value: 3.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGH-IKITDFGLCKE-GITdaatMKTFCG---TPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRlPFYN 118
Cdd:PLN00009 131 QNLLIDRRTNaLKLADFGLARAfGIP----VRTFTHevvTLWYRAPEILlGSRHYSTPVDIWSVGCIFAEMVNQK-PLFP 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 119 QDHE-----KLFELI------------LMEDIK--FPR-----------TLSSDAKSLLSGLLIKDPNKRLgggpdDAKE 168
Cdd:PLN00009 206 GDSEidelfKIFRILgtpneetwpgvtSLPDYKsaFPKwppkdlatvvpTLEPAGVDLLSKMLRLDPSKRI-----TARA 280

                 ....*..
gi 767912019 169 IMRHSFF 175
Cdd:PLN00009 281 ALEHEYF 287
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
40-173 4.07e-05

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: 43.47  E-value: 4.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLEN-LMLDKD-GHIKITDFGLC-KEGitdaATMKTFCGTPEYLAPEVLEDNDYGR-----AVDWWGLGVVMYEMMC 111
Cdd:cd13987  115 RDIKPENvLLFDKDcRRVKLCDFGLTrRVG----STVKRVSGTIPYTAPEVCEAKKNEGfvvdpSIDVWAFGVLLFCCLT 190
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912019 112 GRLPFYNQD-HEKLFELIL--------MEDIKFpRTLSSDAKSLLSGLLIKDPNKRlgGGPDDAKEIMRHS 173
Cdd:cd13987  191 GNFPWEKADsDDQFYEEFVrwqkrkntAVPSQW-RRFTPKALRMFKKLLAPEPERR--CSIKEVFKYLGDR 258
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
40-116 4.36e-05

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 43.71  E-value: 4.36e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTfcgTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 116
Cdd:cd05083  124 RDLAARNILVSEDGVAKISDFGLAKVGSMGVDNSRL---PVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSyGRAPY 198
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
40-110 4.46e-05

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 43.73  E-value: 4.46e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCK---EG-----ITDAATMKTFcgtpeYLAPEVLEDNDYGRAVDWWGLGVVMYEMM 110
Cdd:cd05080  131 RDLAARNVLLDNDRLVKIGDFGLAKavpEGheyyrVREDGDSPVF-----WYAPECLKEYKFYYASDVWSFGVTLYELL 204
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
57-172 4.47e-05

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: 43.46  E-value: 4.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  57 ITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL------- 129
Cdd:cd13995  136 LVDFGLSVQMTEDVYVPKDLRGTEIYMSPEVILCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAYPSYLyiihkqa 215
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767912019 130 --MEDIkfPRTLSSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRH 172
Cdd:cd13995  216 ppLEDI--AQDCSPAMRELLEAALERNPNHRS-----SAAELLKH 253
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
82-175 4.54e-05

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: 43.68  E-value: 4.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  82 YLAPEVLEDN-DYGRAVDWWGLGVVMYEMMCGRLPFY----NQDH----------EKLFELILMEDIKFPRTL------- 139
Cdd:cd14132  178 YKGPELLVDYqYYDYSLDMWSLGCMLASMIFRKEPFFhghdNYDQlvkiakvlgtDDLYAYLDKYGIELPPRLndilgrh 257
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767912019 140 -----------------SSDAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 175
Cdd:cd14132  258 skkpwerfvnsenqhlvTPEALDLLDKLLRYDHQERI-----TAKEAMQHPYF 305
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
51-160 4.87e-05

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


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 43.84  E-value: 4.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  51 KDGHIKITDFGlckEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFynQDHEKLFELILM 130
Cdd:cd14214  171 KNTSIRVADFG---SATFDHEHHTTIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLF--QTHENREHLVMM 245
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767912019 131 EDI--KFPRTL---SSDAKSLLSGLLIKDPNKRLG 160
Cdd:cd14214  246 EKIlgPIPSHMihrTRKQKYFYKGSLVWDENSSDG 280
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
40-109 4.96e-05

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 43.47  E-value: 4.96e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAA--TMKTFCGTPEY-LAPEVLEDNDYGRAVDWWGLGVVMYEM 109
Cdd:cd14205  132 RDLATRNILVENENRVKIGDFGLTKVLPQDKEyyKVKEPGESPIFwYAPESLTESKFSVASDVWSFGVVLYEL 204
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
40-116 5.48e-05

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


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 43.53  E-value: 5.48e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPF 116
Cdd:cd07869  127 RDLKPQNLLISDTGELKLADFGLARAKSVPSHTYSNEVVTLWYRPPDVlLGSTEYSTCLDMWGVGCIFVEMIQGVAAF 204
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
40-116 6.81e-05

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: 43.10  E-value: 6.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLC--KEGITDAATMKTFCGTPEYLAPEVL---EDNDYGRAVDWWGLGVVMYEMMCGRL 114
Cdd:cd14149  132 RDMKSNNIFLHEGLTVKIGDFGLAtvKSRWSGSQQVEQPTGSILWMAPEVIrmqDNNPFSFQSDVYSYGIVLYELMTGEL 211

                 ..
gi 767912019 115 PF 116
Cdd:cd14149  212 PY 213
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
46-116 7.05e-05

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 42.72  E-value: 7.05e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912019  46 NLMLDKDGHIKITDFGLCKEGITDAATMKTfcgtP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 116
Cdd:cd05039  132 NVLVSEDNVAKVSDFGLAKEASSNQDGGKL----PiKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPY 200
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
40-116 7.60e-05

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 42.79  E-value: 7.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCG-TP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 116
Cdd:cd05057  133 RDLAARNVLVKTPNHVKITDFGLAKLLDVDEKEYHAEGGkVPiKWMALESIQYRIYTHKSDVWSYGVTVWELMTfGAKPY 212
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
40-116 8.15e-05

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


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 42.52  E-value: 8.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFG----LCKegiTDAATMKTFCGTPEYLAPEVLEDN-DYGRAVDWWGLGVVMYEMMCGRL 114
Cdd:cd14064  119 RDLNSHNILLYEDGHAVVADFGesrfLQS---LDEDNMTKQPGNLRWMAPEVFTQCtRYSIKADVFSYALCLWELLTGEI 195

                 ..
gi 767912019 115 PF 116
Cdd:cd14064  196 PF 197
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
39-110 8.53e-05

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: 42.88  E-value: 8.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  39 PKNISLENlmldKDGHIKITDFGL-CKEGITDAA-----------TMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVM 106
Cdd:cd14049  148 PRNIFLHG----SDIHVRIGDFGLaCPDILQDGNdsttmsrlnglTHTSGVGTCLYAAPEQLEGSHYDFKSDMYSIGVIL 223

                 ....
gi 767912019 107 YEMM 110
Cdd:cd14049  224 LELF 227
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
45-112 9.44e-05

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


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 42.81  E-value: 9.44e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGH--IKITDFGlckEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCG 112
Cdd:cd14224  197 ENILLKQQGRsgIKVIDFG---SSCYEHQRIYTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTG 263
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
40-110 1.18e-04

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 42.76  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGlckegitdaaTMKTF-----------CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYE 108
Cdd:PHA03210 291 RDIKLENIFLNCDGKIVLGDFG----------TAMPFekereafdygwVGTVATNSPEILAGDGYCEITDIWSCGLILLD 360

                 ..
gi 767912019 109 MM 110
Cdd:PHA03210 361 ML 362
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
46-129 1.18e-04

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


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 42.33  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCKEGITDAATMKTFCGT-P-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHE 122
Cdd:cd05032  149 NCMVAEDLTVKIGDFGMTRDIYETDYYRKGGKGLlPvRWMAPESLKDGVFTTKSDVWSFGVVLWEMATlAEQPYQGLSNE 228

                 ....*..
gi 767912019 123 KLFELIL 129
Cdd:cd05032  229 EVLKFVI 235
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
40-159 1.36e-04

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


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 42.33  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGI-TDAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 116
Cdd:cd05093  144 RDLATRNCLVGENLLVKIGDFGMSRDVYsTDYYRVGGHTMLPiRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPW 223
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 767912019 117 YNQDHEKLFELILMEDI-KFPRTLSSDAKSLLSGLLIKDPNKRL 159
Cdd:cd05093  224 YQLSNNEVIECITQGRVlQRPRTCPKEVYDLMLGCWQREPHMRL 267
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
40-128 1.39e-04

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 42.27  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTP---EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLP 115
Cdd:cd05063  131 RDLAARNILVNSNLECKVSDFGLSRVLEDDPEGTYTTSGGKipiRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSfGERP 210
                         90
                 ....*....|...
gi 767912019 116 FYNQDHEKLFELI 128
Cdd:cd05063  211 YWDMSNHEVMKAI 223
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
40-159 1.58e-04

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


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 41.88  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGI-TDAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 116
Cdd:cd05092  146 RDLATRNCLVGQGLVVKIGDFGMSRDIYsTDYYRVGGRTMLPiRWMPPESILYRKFTTESDIWSFGVVLWEIFTyGKQPW 225
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 767912019 117 YNQDHEKLFELILM-EDIKFPRTLSSDAKSLLSGLLIKDPNKRL 159
Cdd:cd05092  226 YQLSNTEAIECITQgRELERPRTCPPEVYAIMQGCWQREPQQRH 269
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
46-109 1.59e-04

Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 42.04  E-value: 1.59e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912019  46 NLMLDKDGHIKITDFGLC-----KEGITDAATMKTfCGTPEYLAPEVLED-------NDYGRaVDWWGLGVVMYEM 109
Cdd:cd13998  131 NILVKNDGTCCIADFGLAvrlspSTGEEDNANNGQ-VGTKRYMAPEVLEGainlrdfESFKR-VDIYAMGLVLWEM 204
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
40-128 1.94e-04

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


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 41.63  E-value: 1.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGT-P-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 116
Cdd:cd05053  157 RDLAARNVLVTEDNVMKIADFGLARDIHHIDYYRKTTNGRlPvKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPY 236
                         90
                 ....*....|..
gi 767912019 117 YNQDHEKLFELI 128
Cdd:cd05053  237 PGIPVEELFKLL 248
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
46-158 2.63e-04

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 41.20  E-value: 2.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCKEGITDAATMKTFCG-TP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHE 122
Cdd:cd05033  136 NILVNSDLVCKVSDFGLSRRLEDSEATYTTKGGkIPiRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSyGERPYWDMSNQ 215
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767912019 123 KLFELIlMEDIKFPRTLssDAKSLLSGLLI----KDPNKR 158
Cdd:cd05033  216 DVIKAV-EDGYRLPPPM--DCPSALYQLMLdcwqKDRNER 252
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
34-130 3.00e-04

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


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 41.15  E-value: 3.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  34 DLQapPKNISLENlmlDKDGHIKITDFG-LCKEGitdaATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCG 112
Cdd:cd14226  143 DLK--PENILLCN---PKRSAIKIIDFGsSCQLG----QRIYQYIQSRFYRSPEVLLGLPYDLAIDMWSLGCILVEMHTG 213
                         90       100
                 ....*....|....*....|...
gi 767912019 113 rLPFYNQDHE-----KLFELILM 130
Cdd:cd14226  214 -EPLFSGANEvdqmnKIVEVLGM 235
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
41-175 3.51e-04

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


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 40.94  E-value: 3.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  41 NISLEnlmLDKDG--HIKITDFGLC------------------KEGitDAATMktfcgtpeylAPEVLEDN-------DY 93
Cdd:cd14018  168 NILLE---LDFDGcpWLVIADFGCCladdsiglqlpfsswyvdRGG--NACLM----------APEVSTAVpgpgvviNY 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  94 GRAvDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMED--IKFPRTLSSDAKSLLSGLLIKDPNKRLggGPDDAKEIMR 171
Cdd:cd14018  233 SKA-DAWAVGAIAYEIFGLSNPFYGLGDTMLESRSYQESqlPALPSAVPPDVRQVVKDLLQRDPNKRV--SARVAANVLH 309

                 ....
gi 767912019 172 HSFF 175
Cdd:cd14018  310 LSLW 313
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
40-116 3.62e-04

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


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 41.16  E-value: 3.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDA---ATMKTFCGTpEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLP 115
Cdd:cd05105  261 RDLAARNVLLAQGKIVKICDFGLARDIMHDSnyvSKGSTFLPV-KWMAPESIFDNLYTTLSDVWSYGILLWEIFSlGGTP 339

                 .
gi 767912019 116 F 116
Cdd:cd05105  340 Y 340
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
45-158 4.23e-04

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


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 40.67  E-value: 4.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGT-PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEK 123
Cdd:cd14110  128 ENMIITEKNLLKIVDLGNAQPFNQGKVLMTDKKGDyVETMAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWE 207
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767912019 124 LFELILMEDIKFPRT---LSSDAKSLLSGLLIKDPNKR 158
Cdd:cd14110  208 RDRNIRKGKVQLSRCyagLSGGAVNFLKSTLCAKPWGR 245
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
55-159 5.15e-04

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 40.62  E-value: 5.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  55 IKITDFGLCK-------EGITDAATMKTF----CGTPEYLAPEVLEDNdYGRAVDWWGLGVVMYEMMcGRLPFYNQDHEK 123
Cdd:cd13977  176 LKVADFGLSKvcsgsglNPEEPANVNKHFlssaCGSDFYMAPEVWEGH-YTAKADIFALGIIIWAMV-ERITFRDGETKK 253
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767912019 124 LF---------ELI-----LMED--------IKFPRTLSSDAKSLLSGLLIKDPNKRL 159
Cdd:cd13977  254 ELlgtyiqqgkEIVplgeaLLENpklelqipLKKKKSMNDDMKQLLRDMLAANPQERP 311
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
29-158 5.17e-04

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: 5.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  29 IRFRFDLQAPPKNISLENLMLDKDGHIKITDFGLCK---EGITDAATMKTFCGT-P-EYLAPEVLEDNDYGRAVDWWGLG 103
Cdd:cd05065  119 MKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRfleDDTSDPTYTSSLGGKiPiRWTAPEAIAYRKFTSASDVWSYG 198
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 104 VVMYEMMC-GRLPFYNQDHEKLFELIlMEDIKFPRTLssDAKSLLSGLLI----KDPNKR 158
Cdd:cd05065  199 IVMWEVMSyGERPYWDMSNQDVINAI-EQDYRLPPPM--DCPTALHQLMLdcwqKDRNLR 255
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
40-109 5.21e-04

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


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 40.50  E-value: 5.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLC-----KEGITDAATmKTFCGTPEYLAPEVLEDN------DYGRAVDWWGLGVVMYE 108
Cdd:cd14142  134 RDLKSKNILVKSNGQCCIADLGLAvthsqETNQLDVGN-NPRVGTKRYMAPEVLDETintdcfESYKRVDIYAFGLVLWE 212

                 .
gi 767912019 109 M 109
Cdd:cd14142  213 V 213
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
40-158 6.05e-04

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


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 40.37  E-value: 6.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATM-KTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 116
Cdd:cd14207  204 RDLAARNILLSENNVVKICDFGLARDIYKNPDYVrKGDARLPlKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSlGASPY 283
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 767912019 117 YNQDHEKLFELILMEDIKF--PRTLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd14207  284 PGVQIDEDFCSKLKEGIRMraPEFATSEIYQIMLDCWQGDPNER 327
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
82-136 6.40e-04

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


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 40.14  E-value: 6.40e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767912019  82 YLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELILMEDIKFP 136
Cdd:cd05046  184 WLAPEAVQEDDFSTKSDVWSFGVLMWEVFTqGELPFYGLSDEEVLNRLQAGKLELP 239
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
40-122 6.62e-04

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 40.18  E-value: 6.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFG---------LCKEGITDAATMKTFC----GTPEYLAPEVLEDNDY--GRAVDWWGLGV 104
Cdd:cd14027  114 KDLKPENILVDNDFHIKIADLGlasfkmwskLTKEEHNEQREVDGTAkknaGTLYYMAPEHLNDVNAkpTEKSDVYSFAI 193
                         90
                 ....*....|....*...
gi 767912019 105 VMYEMMCGRLPFYNQDHE 122
Cdd:cd14027  194 VLWAIFANKEPYENAINE 211
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
51-136 7.20e-04

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


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 40.00  E-value: 7.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  51 KDGHIKITDFGlckEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFynQDHEKLFELILM 130
Cdd:cd14215  170 KSTAIRVVDFG---SATFDHEHHSTIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLF--QTHDNREHLAMM 244

                 ....*.
gi 767912019 131 EDIKFP 136
Cdd:cd14215  245 ERILGP 250
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
40-109 8.11e-04

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


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 39.96  E-value: 8.11e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATM-KTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEM 109
Cdd:cd05103  203 RDLAARNILLSENNVVKICDFGLARDIYKDPDYVrKGDARLPlKWMAPETIFDRVYTIQSDVWSFGVLLWEI 274
Kinase-like pfam14531
Kinase-like; This family includes the pseudokinases ROP2 and ROP8 from Toxoplasma gondii. ...
40-158 1.08e-03

Kinase-like; This family includes the pseudokinases ROP2 and ROP8 from Toxoplasma gondii. These proteins have a typical bilobed protein kinase fold, but lack catalytic actvity.


Pssm-ID: 405254 [Multi-domain]  Cd Length: 288  Bit Score: 39.40  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019   40 KNISLENLMLDKDGHIKITDFG-LCKEG--ITDAATMKTFcGTPEYLApevlEDNDYGR--------AVDWWGLGVVMYE 108
Cdd:pfam14531 168 GQFTVDNFFLDQRGGVFLGGFEhLVRDGtkVVASEVPRGF-APPELLG----SRGGYTMknttlmthAFDAWQLGLVIYW 242
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767912019  109 MMCGRLPFynqdhEKLFELILMEDIKFP-RTLSSDAKSLLSGLLIKDPNKR 158
Cdd:pfam14531 243 IWCLDLPN-----TLDAEEGGIEWKFRLcKNIPEPVRALLKGFLNYSQEDR 288
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
39-122 1.13e-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: 39.54  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  39 PKNISLENLmldKDGHIKITDFG-LCKEGitdaATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGrLPFY 117
Cdd:cd14212  131 PENILLVNL---DSPEIKLIDFGsACFEN----YTLYTYIQSRFYRSPEVLLGLPYSTAIDMWSLGCIAAELFLG-LPLF 202

                 ....*
gi 767912019 118 NQDHE 122
Cdd:cd14212  203 PGNSE 207
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
57-115 1.14e-03

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


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 39.42  E-value: 1.14e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912019  57 ITDFGLCKE----GITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMcGRLP 115
Cdd:cd14156  133 VTDFGLAREvgemPANDPERKLSLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEIL-ARIP 194
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
40-116 1.67e-03

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


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 38.85  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCG-TP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 116
Cdd:cd05108  133 RDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGkVPiKWMALESILHRIYTHQSDVWSYGVTVWELMTfGSKPY 212
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
41-158 1.79e-03

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: 38.67  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  41 NISLENLMLD--KDGHIKITDFGLCKEgiTDAATMKTFCGTPEYLAPEVLEDNDYGRA-VDWWGLGVVMYEMMCGRLPFY 117
Cdd:cd14112  124 DVQPDNIMFQsvRSWQVKLVDFGRAQK--VSKLGKVPVDGDTDWASPEFHNPETPITVqSDIWGLGVLTFCLLSGFHPFT 201
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767912019 118 NQ--DHEKLFELILMEDIKF---PRTLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd14112  202 SEydDEEETKENVIFVKCRPnliFVEATQEALRFATWALKKSPTRR 247
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
40-158 1.87e-03

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. Ephrin/EphR interaction 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. EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). In general, class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The EphA10 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: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 38.75  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAaTMKTFCGTPEYL--APEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 116
Cdd:cd05064  131 KGLAAHKVLVNSDLVCKISGFRRLQEDKSEA-IYTTMSGKSPVLwaAPEAIQYHHFSSASDVWSFGIVMWEVMSyGERPY 209
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767912019 117 YNQDHEKLFELIlmED---IKFPRTLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd05064  210 WDMSGQDVIKAV--EDgfrLPAPRNCPNLLHQLMLDCWQKERGER 252
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
40-109 2.24e-03

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


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 38.61  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATM----KTFCGTPEYLAPEVLED-------NDYGRAvDWWGLGVVMYE 108
Cdd:cd14144  124 RDIKSKNILVKKNGTCCIADLGLAVKFISETNEVdlppNTRVGTKRYMAPEVLDEslnrnhfDAYKMA-DMYSFGLVLWE 202

                 .
gi 767912019 109 M 109
Cdd:cd14144  203 I 203
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
40-124 2.42e-03

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


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 38.27  E-value: 2.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGL---------CKEGITDAATMKtfcgtpeYLAPEVLEDNDYGRAVDWWGLGVVMYEMM 110
Cdd:cd05050  154 RDLATRNCLVGENMVVKIADFGLsrniysadyYKASENDAIPIR-------WMPPESIFYNRYTTESDVWAYGVVLWEIF 226
                         90
                 ....*....|....*
gi 767912019 111 C-GRLPFYNQDHEKL 124
Cdd:cd05050  227 SyGMQPYYGMAHEEV 241
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
51-136 2.57e-03

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


Pssm-ID: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 38.29  E-value: 2.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  51 KDGHIKITDFGlckEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFynQDHEKLFELILM 130
Cdd:cd14213  170 KNPDIKVVDFG---SATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVF--QTHDSKEHLAMM 244

                 ....*.
gi 767912019 131 EDIKFP 136
Cdd:cd14213  245 ERILGP 250
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
45-117 2.58e-03

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


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 38.47  E-value: 2.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLML----DKDGHIKITDFGlckegiTDAATMKTFCGT----PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGrLPF 116
Cdd:cd14229  131 ENIMLvdpvRQPYRVKVIDFG------SASHVSKTVCSTylqsRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG-WPL 203

                 .
gi 767912019 117 Y 117
Cdd:cd14229  204 Y 204
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
57-115 2.74e-03

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: 38.24  E-value: 2.74e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912019  57 ITDFGLCKEgITDAATMK-------TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMcGRLP 115
Cdd:cd14065  133 VADFGLARE-MPDEKTKKpdrkkrlTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEII-GRVP 196
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
40-158 3.04e-03

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Mer subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 37.99  E-value: 3.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGIT-DAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 116
Cdd:cd14204  144 RDLAARNCMLRDDMTVCVADFGLSKKIYSgDYYRQGRIAKMPvKWIAVESLADRVYTVKSDVWAFGVTMWEIATrGMTPY 223
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767912019 117 YN-QDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKR 158
Cdd:cd14204  224 PGvQNHEIYDYLLHGHRLKQPEDCLDELYDIMYSCWRSDPTDR 266
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
40-109 3.06e-03

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 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: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 38.04  E-value: 3.06e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATM-KTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEM 109
Cdd:cd05102  196 RDLAARNILLSENNVVKICDFGLARDIYKDPDYVrKGSARLPlKWMAPESIFDKVYTTQSDVWSFGVLLWEI 267
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
46-116 3.14e-03

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


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 38.08  E-value: 3.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLCKEGITDAATMKTF--CGTPEYLAPEVLE-----DNDYGRAVDWWGLGVVMYEMM--CG---- 112
Cdd:cd14053  132 NVLLKSDLTACIADFGLALKFEPGKSCGDTHgqVGTRRYMAPEVLEgainfTRDAFLRIDMYAMGLVLWELLsrCSvhdg 211

                 ....*....
gi 767912019 113 -----RLPF 116
Cdd:cd14053  212 pvdeyQLPF 220
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
33-142 3.16e-03

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


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 38.11  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  33 FDLQAPP----KNISLENLMLDKDGHIKITDFGLCKEGITDAATM----KTFCGTPEYLAPEVLED----NDYGRAV--D 98
Cdd:cd14219  123 FSTQGKPaiahRDLKSKNILVKKNGTCCIADLGLAVKFISDTNEVdippNTRVGTKRYMPPEVLDEslnrNHFQSYImaD 202
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912019  99 WWGLGVVMYEM----MCG------RLPFYNQ-----DHEKLFELILMEDIK--FPRTLSSD 142
Cdd:cd14219  203 MYSFGLILWEVarrcVSGgiveeyQLPYHDLvpsdpSYEDMREIVCIKRLRpsFPNRWSSD 263
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
40-129 3.17e-03

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


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 38.03  E-value: 3.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGT-P-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 116
Cdd:cd05061  143 RDLAARNCMVAHDFTVKIGDFGMTRDIYETDYYRKGGKGLlPvRWMAPESLKDGVFTTSSDMWSFGVVLWEITSlAEQPY 222
                         90
                 ....*....|...
gi 767912019 117 YNQDHEKLFELIL 129
Cdd:cd05061  223 QGLSNEQVLKFVM 235
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
46-118 3.31e-03

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


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 37.81  E-value: 3.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGL--CKEGITDAATMKT--FCGTPEYLAPEVLED-------NDYGRAvDWWGLGVVMYEMM---- 110
Cdd:cd14143  130 NILVKKNGTCCIADLGLavRHDSATDTIDIAPnhRVGTKRYMAPEVLDDtinmkhfESFKRA-DIYALGLVFWEIArrcs 208
                         90
                 ....*....|....
gi 767912019 111 CG------RLPFYN 118
Cdd:cd14143  209 IGgihedyQLPYYD 222
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
40-129 4.07e-03

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 37.51  E-value: 4.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEgITDAATMKTFCGTP---EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLP 115
Cdd:cd05035  137 RDLAARNCMLDENMTVCVADFGLSRK-IYSGDYYRQGRISKmpvKWIALESLADNVYTSKSDVWSFGVTMWEIATrGQTP 215
                         90
                 ....*....|....
gi 767912019 116 FYNQDHEKLFELIL 129
Cdd:cd05035  216 YPGVENHEIYDYLR 229
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
40-111 4.27e-03

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 37.73  E-value: 4.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGL------CK--EGITDAATMKTF--CGTPEYLAPEVLED----NDYGRA---VDWWGL 102
Cdd:cd14054  126 RDLNSRNVLVKADGSCVICDFGLamvlrgSSlvRGRPGAAENASIseVGTLRYMAPEVLEGavnlRDCESAlkqVDVYAL 205
                         90
                 ....*....|.
gi 767912019 103 GVVMYE--MMC 111
Cdd:cd14054  206 GLVLWEiaMRC 216
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
39-112 5.03e-03

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


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 37.22  E-value: 5.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  39 PKNIslenLMLDKDGHIKITDFGLC-KEGITDAATMKTfcgtPEYLAPE-----------VLEDNDYGRAVDWWGLGVVM 106
Cdd:cd14020  138 PRNI----LWSAEDECFKLIDFGLSfKEGNQDVKYIQT----DGYRAPEaelqnclaqagLQSETECTSAVDLWSLGIVL 209

                 ....*.
gi 767912019 107 YEMMCG 112
Cdd:cd14020  210 LEMFSG 215
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
40-198 5.37e-03

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


Pssm-ID: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 37.32  E-value: 5.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCG--TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPF 116
Cdd:cd05062  143 RDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGKGllPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATlAEQPY 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019 117 YNQDHEKLFELIlMEdikfprtlssdaksllSGLLIKDPNkrlggGPDDAKEIMRhsffsgVNWQdvYDKKLVPPFKPQV 196
Cdd:cd05062  223 QGMSNEQVLRFV-ME----------------GGLLDKPDN-----CPDMLFELMR------MCWQ--YNPKMRPSFLEII 272

                 ..
gi 767912019 197 TS 198
Cdd:cd05062  273 SS 274
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
40-116 5.59e-03

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 37.23  E-value: 5.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDAA--TMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLP 115
Cdd:cd05115  128 RDLAARNVLLVNQHYAKISDFGLSKALGADDSyyKARSAGKWPlKWYAPECINFRKFSSRSDVWSYGVTMWEAFSyGQKP 207

                 .
gi 767912019 116 F 116
Cdd:cd05115  208 Y 208
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
46-110 7.00e-03

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


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 36.97  E-value: 7.00e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912019  46 NLMLDKDGHIKITDFGLC-----KEGITDAATMKTfCGTPEYLAPEVLE------DNDYGRAVDWWGLGVVMYEMM 110
Cdd:cd14055  137 NILVKNDGTCVLADFGLAlrldpSLSVDELANSGQ-VGTARYMAPEALEsrvnleDLESFKQIDVYSMALVLWEMA 211
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
40-134 7.86e-03

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


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 36.94  E-value: 7.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLCKEGITDA----ATMKTFCGTPEYLAPEVLED----NDYGRAV--DWWGLGVVMYEM 109
Cdd:cd14220  124 RDLKSKNILIKKNGTCCIADLGLAVKFNSDTnevdVPLNTRVGTKRYMAPEVLDEslnkNHFQAYImaDIYSFGLIIWEM 203
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767912019 110 ----MCG------RLPFYNQ-----DHEKLFELILMEDIK 134
Cdd:cd14220  204 arrcVTGgiveeyQLPYYDMvpsdpSYEDMREVVCVKRLR 243
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
40-110 8.42e-03

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 36.85  E-value: 8.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  40 KNISLENLMLDKDGHIKITDFGLC-------KEGITDAATMK-------------TFCGTPEYLAPEVLEDNDYGRAVDW 99
Cdd:cd14222  114 RDLNSHNCLIKLDKTVVVADFGLSrliveekKKPPPDKPTTKkrtlrkndrkkryTVVGNPYWMAPEMLNGKSYDEKVDI 193
                         90
                 ....*....|.
gi 767912019 100 WGLGVVMYEMM 110
Cdd:cd14222  194 FSFGIVLCEII 204
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
46-140 8.66e-03

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 36.64  E-value: 8.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  46 NLMLDKDGHIKITDFGLC---KEGITDAATMKTfcgtP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQD 120
Cdd:cd05148  134 NILVGEDLVCKVADFGLArliKEDVYLSSDKKI----PyKWTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVPYPGMN 209
                         90       100
                 ....*....|....*....|
gi 767912019 121 HEKLFELIlMEDIKFPRTLS 140
Cdd:cd05148  210 NHEVYDQI-TAGYRMPCPAK 228
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
45-122 9.38e-03

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


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 36.60  E-value: 9.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912019  45 ENLMLDKDGH--IKITDFGL-CKEgitdAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGrLPFYNQDH 121
Cdd:cd14225  175 ENILLRQRGQssIKVIDFGSsCYE----HQRVYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTG-YPLFPGEN 249

                 .
gi 767912019 122 E 122
Cdd:cd14225  250 E 250
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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