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Conserved domains on  [gi|568977678|ref|XP_006515118|]
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tribbles homolog 2 isoform X2 [Mus musculus]

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 ...
 45-273 5.29e-178

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 cd14022:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 242  Bit Score: 491.09  E-value: 5.29e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  45 HSRARSEIPGHVFEISCYQESLAPCFCLSAHSNINQITEILLGETKAYVFFERSYGDMHSFVRTCKKLREEEAARLFYQI 124
Cdd:cd14022   14 HLHSGEELVCKVFDIGCYQESLAPCFCLPAHSNINQITEIILGETKAYVFFERSYGDMHSFVRTCKKLREEEAARLFYQI 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 125 ASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSGSYSGKAADVWS 204
Cdd:cd14022   94 ASAVAHCHDGGLVLRDLKLRKFVFKDEERTRVKLESLEDAYILRGHDDSLSDKHGCPAYVSPEILNTSGSYSGKAADVWS 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568977678 205 LGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd14022  174 LGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPWF 242
 
Name Accession Description Interval E-value
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
 45-273 5.29e-178

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: 491.09  E-value: 5.29e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  45 HSRARSEIPGHVFEISCYQESLAPCFCLSAHSNINQITEILLGETKAYVFFERSYGDMHSFVRTCKKLREEEAARLFYQI 124
Cdd:cd14022   14 HLHSGEELVCKVFDIGCYQESLAPCFCLPAHSNINQITEIILGETKAYVFFERSYGDMHSFVRTCKKLREEEAARLFYQI 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 125 ASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSGSYSGKAADVWS 204
Cdd:cd14022   94 ASAVAHCHDGGLVLRDLKLRKFVFKDEERTRVKLESLEDAYILRGHDDSLSDKHGCPAYVSPEILNTSGSYSGKAADVWS 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568977678 205 LGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd14022  174 LGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPWF 242
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
 75-273 5.82e-45

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 153.07  E-value: 5.82e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678    75 HSNINQITEILLGETKAYVFFER-SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKdeER 153
Cdd:smart00220  56 HPNIVRLYDVFEDEDKLYLVMEYcEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLD--ED 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678   154 TRVKLESLEDAYILRgDDDSLSDKHGCPAYVSPEILNTSGsYsGKAADVWSLGVMLYTMLVGRYPF-HDIEPSSLFSKIR 232
Cdd:smart00220 134 GHVKLADFGLARQLD-PGEKLTTFVGTPEYMAPEVLLGKG-Y-GKAVDIWSLGVILYELLTGKPPFpGDDQLLELFKKIG 210

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 568977678   233 RGQFNIPE---TLSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:smart00220 211 KPKPPFPPpewDISPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
75-273 4.66e-30

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 113.11  E-value: 4.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678   75 HSNINQITEILLGETKAYVFFER-SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHChdgglvlrdlklrkfifkdeer 153
Cdd:pfam00069  57 HPNIVRLYDAFEDKDNLYLVLEYvEGGSLFDLLSEKGAFSEREAKFIMKQILEGLESG---------------------- 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  154 trVKLESLEdayilrgdddslsdkhGCPAYVSPEILntSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRR 233
Cdd:pfam00069 115 --SSLTTFV----------------GTPWYMAPEVL--GGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIID 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 568977678  234 G---QFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:pfam00069 175 QpyaFPELPSNLSEEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
100-269 3.68e-21

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 93.15  E-value: 3.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLK-----LRkfifkdeERTRVKL-----------ESLED 163
Cdd:COG0515   92 ESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKpanilLT-------PDGRVKLidfgiaralggATLTQ 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 164 AYILRGDddslsdkhgcPAYVSPEILntSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQF------- 236
Cdd:COG0515  165 TGTVVGT----------PGYMAPEQA--RGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPpppselr 232

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568977678 237 -NIPETLSPkakcLIRSILRREPSERLTS-QEILD 269
Cdd:COG0515  233 pDLPPALDA----IVLRALAKDPEERYQSaAELAA 263
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
 100-274 8.16e-21

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 90.65  E-value: 8.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCKKLREEEAArlFY--QIASAVAHCHDGGLVLRDLKLRKFIFkdEERTRVKLESLEDAYILRGDDDSLSdk 177
Cdd:PTZ00263 103 GELFTHLRKAGRFPNDVAK--FYhaELVLAFEYLHSKDIIYRDLKPENLLL--DNKGHVKVTDFGFAKKVPDRTFTLC-- 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 178 hGCPAYVSPEILNTSGSysGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRRE 257
Cdd:PTZ00263 177 -GTPEYLAPEVIQSKGH--GKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGLLQTD 253

                        170       180
                 ....*....|....*....|..
gi 568977678 258 PSERLTS-----QEILDHPWFS 274
Cdd:PTZ00263 254 HTKRLGTlkggvADVKNHPYFH 275
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
115-219 5.93e-05

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 44.40  E-value: 5.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 115 EEAARLFYQIASAVAHCHDGGLVLRDLK----LrkfIFKDEertRVKL----------ESledayilrgdddSLSDKH-- 178
Cdd:NF033483 107 EEAVEIMIQILSALEHAHRNGIVHRDIKpqniL---ITKDG---RVKVtdfgiaralsST------------TMTQTNsv 168

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 568977678 179 -GCPAYVSPEIlnTSGSYSGKAADVWSLGVMLYTMLVGRYPF 219
Cdd:NF033483 169 lGTVHYLSPEQ--ARGGTVDARSDIYSLGIVLYEMLTGRPPF 208
 
Name Accession Description Interval E-value
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
 45-273 5.29e-178

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: 491.09  E-value: 5.29e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  45 HSRARSEIPGHVFEISCYQESLAPCFCLSAHSNINQITEILLGETKAYVFFERSYGDMHSFVRTCKKLREEEAARLFYQI 124
Cdd:cd14022   14 HLHSGEELVCKVFDIGCYQESLAPCFCLPAHSNINQITEIILGETKAYVFFERSYGDMHSFVRTCKKLREEEAARLFYQI 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 125 ASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSGSYSGKAADVWS 204
Cdd:cd14022   94 ASAVAHCHDGGLVLRDLKLRKFVFKDEERTRVKLESLEDAYILRGHDDSLSDKHGCPAYVSPEILNTSGSYSGKAADVWS 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568977678 205 LGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd14022  174 LGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPWF 242
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
 33-273 2.99e-152

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: 426.07  E-value: 2.99e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  33 EQARRARTHTRTHSRARSEIPGHVFEISCYQESLAPCFCLSAHSNINQITEILLGETKAYVFFERSYGDMHSFVRTCKKL 112
Cdd:cd13976    2 EPAEGSSLYRCVDIHTGEELVCKVVPVPECHAVLRAYFRLPSHPNISGVHEVIAGETKAYVFFERDHGDLHSYVRSRKRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 113 REEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTS 192
Cdd:cd13976   82 REPEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVFADEERTKLRLESLEDAVILEGEDDSLSDKHGCPAYVSPEILNSG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 193 GSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd13976  162 ATYSGKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRRGQFAIPETLSPRARCLIRSLLRREPSERLTAEDILLHPW 241


                 .
gi 568977678 273 F 273
Cdd:cd13976  242 L 242
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
 31-273 2.95e-138

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: 390.56  E-value: 2.95e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  31 EREQARRARthtRTHSRARSEIPghVFEISCYQESLAPCFCLSAHSNINQITEILLGETKAYVFFERSYGDMHSFVRTCK 110
Cdd:cd14023    5 GREHVYRAL---QLHSGAELQCK--VFPLKHYQDKIRPYIQLPSHRNITGIVEVILGDTKAYVFFEKDFGDMHSYVRSCK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 111 KLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILN 190
Cdd:cd14023   80 RLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSDEERTQLRLESLEDTHIMKGEDDALSDKHGCPAYVSPEILN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 191 TSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDH 270
Cdd:cd14023  160 TTGTYSGKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPDHVSPKARCLIRSLLRREPSERLTAPEILLH 239


                 ...
gi 568977678 271 PWF 273
Cdd:cd14023  240 PWF 242
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
 38-272 6.22e-118

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: 339.16  E-value: 6.22e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  38 ARTHTRTHSRARSEIPGHVFEISCYQESLAPCFCLSAHSNINQITEILLGETKAYVFFERSYGDMHSFVRTCKKLREEEA 117
Cdd:cd14024    7 QELYRAEHYQTEKEYTCKVLSLRSYQECLAPYDRLGPHEGVCSVLEVVIGQDRAYAFFSRHYGDMHSHVRRRRRLSEDEA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 118 ARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSGSYSG 197
Cdd:cd14024   87 RGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRTKLVLVNLEDSCPLNGDDDSLTDKHGCPAYVGPEILSSRRSYSG 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568977678 198 KAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14024  167 KAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIRRGAFSLPAWLSPGARCLVSCMLRRSPAERLKASEILLHPW 241
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
 75-272 1.77e-55

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: 180.41  E-value: 1.77e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFErsY---GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKfIFKDE 151
Cdd:cd14003   58 HPNIIKLYEVIETENKIYLVME--YasgGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLEN-ILLDK 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 152 ErTRVKLesledayilrGD---------DDSLSDKHGCPAYVSPEILNTSGsYSGKAADVWSLGVMLYTMLVGRYPFHDI 222
Cdd:cd14003  135 N-GNLKI----------IDfglsnefrgGSLLKTFCGTPAYAAPEVLLGRK-YDGPKADVWSLGVILYAMLTGYLPFDDD 202

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 568977678 223 EPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14003  203 NDSKLFRKILKGKYPIPSHLSPDARDLIRRMLVVDPSKRITIEEILNHPW 252
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
 75-272 2.15e-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: 154.56  E-value: 2.15e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILlgETKAYVFFERSY---GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDE 151
Cdd:cd05117   58 HPNIVKLYEVF--EDDKNLYLVMELctgGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASK 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 152 ERT-RVKLEsleD---AYILRgDDDSLSDKHGCPAYVSPEILNTSGsYsGKAADVWSLGVMLYTMLVGRYPFHDIEPSSL 227
Cdd:cd05117  136 DPDsPIKII---DfglAKIFE-EGEKLKTVCGTPYYVAPEVLKGKG-Y-GKKCDIWSLGVILYILLCGYPPFYGETEQEL 209

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568977678 228 FSKIRRGQFNIPE----TLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd05117  210 FEKILKGKYSFDSpewkNVSEEAKDLIKRLLVVDPKKRLTAAEALNHPW 258
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
 110-270 2.37e-45

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: 155.26  E-value: 2.37e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 110 KKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFkdEERTR-VKLESLEDAYILRGDDDSLSDKHGCPAYVSPEI 188
Cdd:cd13974  127 KRLSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVL--NKRTRkITITNFCLGKHLVSEDDLLKDQRGSPAYISPDV 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 189 LntSGS-YSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPET--LSPKAKCLIRSILRREPSERLTSQ 265
Cdd:cd13974  205 L--SGKpYLGKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAAEYTIPEDgrVSENTVCLIRKLLVLNPQKRLTAS 282


                 ....*
gi 568977678 266 EILDH 270
Cdd:cd13974  283 EVLDS 287
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
 75-273 5.82e-45

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 153.07  E-value: 5.82e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678    75 HSNINQITEILLGETKAYVFFER-SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKdeER 153
Cdd:smart00220  56 HPNIVRLYDVFEDEDKLYLVMEYcEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLD--ED 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678   154 TRVKLESLEDAYILRgDDDSLSDKHGCPAYVSPEILNTSGsYsGKAADVWSLGVMLYTMLVGRYPF-HDIEPSSLFSKIR 232
Cdd:smart00220 134 GHVKLADFGLARQLD-PGEKLTTFVGTPEYMAPEVLLGKG-Y-GKAVDIWSLGVILYELLTGKPPFpGDDQLLELFKKIG 210

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 568977678   233 RGQFNIPE---TLSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:smart00220 211 KPKPPFPPpewDISPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
 75-273 9.61e-44

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: 150.10  E-value: 9.61e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILlgETKAYVFFERSY---GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDE 151
Cdd:cd14081   60 HPNVLKLYDVY--ENKKYLYLVLEYvsgGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEK 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 152 ERTRVK---LESLEdayilrGDDDSLSDKHGCPAYVSPEILntSG-SYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSL 227
Cdd:cd14081  138 NNIKIAdfgMASLQ------PEGSLLETSCGSPHYACPEVI--KGeKYDGRKADIWSCGVILYALLVGALPFDDDNLRQL 209

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568977678 228 FSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd14081  210 LEKVKRGVFHIPHFISPDAQDLLRRMLEVNPEKRITIEEIKKHPWF 255
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
 75-273 2.52e-42

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: 146.56  E-value: 2.52e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFErsY---GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKfIFKDE 151
Cdd:cd14080   61 HPNIIQVYSIFERGSKVFIFME--YaehGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCEN-ILLDS 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 152 ERTrVKLESLEDA-YILRGDDDSLSDKH-GCPAYVSPEILNTSgSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFS 229
Cdd:cd14080  138 NNN-VKLSDFGFArLCPDDDGDVLSKTFcGSAAYAAPEILQGI-PYDPKKYDIWSLGVILYIMLCGSMPFDDSNIKKMLK 215

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 568977678 230 KIRRGQFNIPET---LSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd14080  216 DQQNRKVRFPSSvkkLSPECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
 75-272 2.94e-41

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: 143.70  E-value: 2.94e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFER-SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEER 153
Cdd:cd14663   59 HPNIVELHEVMATKTKIFFVMELvTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGN 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 154 TRVK---LESLEDAyilRGDDDSLSDKHGCPAYVSPEILNTSGsYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSK 230
Cdd:cd14663  139 LKISdfgLSALSEQ---FRQDGLLHTTCGTPNYVAPEVLARRG-YDGAKADIWSCGVILFVLLAGYLPFDDENLMALYRK 214

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568977678 231 IRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14663  215 IMKGEFEYPRWFSPGAKSLIKRILDPNPSTRITVEQIMASPW 256
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
 72-273 8.06e-41

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: 142.41  E-value: 8.06e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  72 LSAHSNINQITEILlgETKAYVFFERSY---GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIF 148
Cdd:cd14079   58 LFRHPHIIRLYEVI--ETPTDIFMVMEYvsgGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLL 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 149 kdEERTRVKLESLEDAYILRgDDDSLSDKHGCPAYVSPEILntSG-SYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSL 227
Cdd:cd14079  136 --DSNMNVKIADFGLSNIMR-DGEFLKTSCGSPNYAAPEVI--SGkLYAGPEVDVWSCGVILYALLCGSLPFDDEHIPNL 210

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568977678 228 FSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd14079  211 FKKIKSGIYTIPSHLSPGARDLIKRMLVVDPLKRITIPEIRQHPWF 256
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
 75-272 1.01e-39

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: 139.83  E-value: 1.01e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFER-SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEER 153
Cdd:cd14078   60 HQHICRLYHVIETDNKIFMVLEYcPGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQN 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 154 TRvklesLED----AYILRGDDDSLSDKHGCPAYVSPEILnTSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFS 229
Cdd:cd14078  140 LK-----LIDfglcAKPKGGMDHHLETCCGSPAYAAPELI-QGKPYIGSEADVWSMGVLLYALLCGFLPFDDDNVMALYR 213

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 568977678 230 KIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14078  214 KIQSGKYEEPEWLSPSSKLLLDQMLQVDPKKRITVKELLNHPW 256
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
 92-273 6.51e-38

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: 134.99  E-value: 6.51e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  92 YVFFE----RSYGDMHsfvRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKfIFKDEErTRVKLESLEDAYIL 167
Cdd:cd14099   77 YILLElcsnGSLMELL---KRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGN-LFLDEN-MNVKIGDFGLAARL 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 168 rgddDSLSDKH----GCPAYVSPEILNTSGSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETL- 242
Cdd:cd14099  152 ----EYDGERKktlcGTPNYIAPEVLEKKKGHSFEV-DIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPSHLs 226

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568977678 243 -SPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd14099  227 iSDEAKDLIRSMLQPDPTKRPSLDEILSHPFF 258
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
 75-272 1.41e-37

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: 134.05  E-value: 1.41e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFE-RSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEER 153
Cdd:cd14073   60 HPHIIRIYEVFENKDKIVIVMEyASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGN 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 154 TRVKLESLEDAYilrGDDDSLSDKHGCPAYVSPEILNTSgSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRR 233
Cdd:cd14073  140 AKIADFGLSNLY---SKDKLLQTFCGSPLYASPEIVNGT-PYQGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISS 215

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568977678 234 GQFNIPETLSpKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14073  216 GDYREPTQPS-DASGLIRWMLTVNPKRRATIEDIANHWW 253
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
 109-273 3.99e-37

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: 133.06  E-value: 3.99e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 109 CKKLREEEAARLFYQIASAVAHCHDGGLVLRDLK----LRKfifkdeERTRVKLESLEDAYILRGDDDSLSDKHGCPAYV 184
Cdd:cd14008  102 VPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKpenlLLT------ADGTVKISDFGVSEMFEDGNDTLQKTAGTPAFL 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 185 SPEILN-TSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQ--FNIPETLSPKAKCLIRSILRREPSER 261
Cdd:cd14008  176 APELCDgDSKTYSGKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNdeFPIPPELSPELKDLLRRMLEKDPEKR 255

                        170
                 ....*....|..
gi 568977678 262 LTSQEILDHPWF 273
Cdd:cd14008  256 ITLKEIKEHPWV 267
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 75-280 4.77e-36

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: 131.65  E-value: 4.77e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFER-SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDE-E 152
Cdd:cd14092   58 HPNIVKLHEVFQDELHTYLVMELlRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEdD 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 153 RTRVKLESLEDAYiLRGDDDSLSDKHGCPAYVSPEILNTSGSYSG--KAADVWSLGVMLYTMLVGRYPFH----DIEPSS 226
Cdd:cd14092  138 DAEIKIVDFGFAR-LKPENQPLKTPCFTLPYAAPEVLKQALSTQGydESCDLWSLGVILYTMLSGQVPFQspsrNESAAE 216

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568977678 227 LFSKIRRGQFNIP----ETLSPKAKCLIRSILRREPSERLTSQEILDHPWFSTDFSVS 280
Cdd:cd14092  217 IMKRIKSGDFSFDgeewKNVSSEAKSLIQGLLTVDPSKRLTMSELRNHPWLQGSSSPS 274
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
 62-272 4.88e-36

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: 130.23  E-value: 4.88e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  62 YQEslAPCFCLSAHSNINQITEILLGETKAYVFFER-SYGDMHSFV-RTCKKLREEEAARLFYQIASAVAHCHDGGLVLR 139
Cdd:cd14074   50 FQE--VRCMKLVQHPNVVRLYEVIDTQTKLYLILELgDGGDMYDYImKHENGLNEDLARKYFRQIVSAISYCHKLHVVHR 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 140 DLKLRKFIFKdEERTRVKLES--LEDAYIlrgDDDSLSDKHGCPAYVSPEILnTSGSYSGKAADVWSLGVMLYTMLVGRY 217
Cdd:cd14074  128 DLKPENVVFF-EKQGLVKLTDfgFSNKFQ---PGEKLETSCGSLAYSAPEIL-LGDEYDAPAVDIWSLGVILYMLVCGQP 202

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568977678 218 PFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14074  203 PFQEANDSETLTMIMDCKYTVPAHVSPECKDLIRRMLIRDPKKRASLEEIENHPW 257
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
 75-272 2.28e-35

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: 128.22  E-value: 2.28e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFE-RSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEer 153
Cdd:cd14075   60 HPNIIRLYEVVETLSKLHLVMEyASGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASN-- 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 154 TRVKLESLEDAYILRgDDDSLSDKHGCPAYVSPEiLNTSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRR 233
Cdd:cd14075  138 NCVKVGDFGFSTHAK-RGETLNTFCGSPPYAAPE-LFKDEHYIGIYVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILE 215

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568977678 234 GQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14075  216 GTYTIPSYVSEPCQELIRGILQPVPSDRYSIDEIKNSEW 254
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
 100-273 2.90e-35

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: 127.63  E-value: 2.90e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCKKLREEEAArlFY--QIASAVAHCHDGGLVLRDLKLRKFIFKDEerTRVKLESLEDAYILRGDDDSLSDK 177
Cdd:cd05123   78 GELFSHLSKEGRFPEERAR--FYaaEIVLALEYLHSLGIIYRDLKPENILLDSD--GHIKLTDFGLAKELSSDGDRTYTF 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 178 HGCPAYVSPEILNtSGSYsGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRRE 257
Cdd:cd05123  154 CGTPEYLAPEVLL-GKGY-GKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPEYVSPEAKSLISGLLQKD 231

                        170
                 ....*....|....*....
gi 568977678 258 PSERLTS---QEILDHPWF 273
Cdd:cd05123  232 PTKRLGSggaEEIKAHPFF 250
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
 75-272 3.36e-35

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: 127.59  E-value: 3.36e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQiteiLLG--ETKAYVFFERSY---GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLK----Lrk 145
Cdd:cd14007   59 HPNILR----LYGyfEDKKRIYLILEYapnGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKpeniL-- 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 146 fIFKDEErtrVKLE----SLEDAYILRgdddslsdKHGC--PAYVSPEILNtSGSYsGKAADVWSLGVMLYTMLVGRYPF 219
Cdd:cd14007  133 -LGSNGE---LKLAdfgwSVHAPSNRR--------KTFCgtLDYLPPEMVE-GKEY-DYKVDIWSLGVLCYELLVGKPPF 198

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568977678 220 HDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14007  199 ESKSHQETYKRIQNVDIKFPSSVSPEAKDLISKLLQKDPSKRLSLEQVLNHPW 251
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
 75-273 3.14e-33

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: 122.75  E-value: 3.14e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKA--YVFFERSYGDMHSFVRTC--KKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKD 150
Cdd:cd14119   53 HRNVIKLVDVLYNEEKQklYMVMEYCVGGLQEMLDSApdKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTT 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 151 EERtrVKLESLEDAYILR--GDDDSLSDKHGCPAYVSPEILNTSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLF 228
Cdd:cd14119  133 DGT--LKISDFGVAEALDlfAEDDTCTTSQGSPAFQPPEIANGQDSFSGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLF 210

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 568977678 229 SKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd14119  211 ENIGKGEYTIPDDVDPDLQDLLRGMLEKDPEKRFTIEQIRQHPWF 255
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 75-272 3.90e-33

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: 123.30  E-value: 3.90e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFER-SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEER 153
Cdd:cd14086   59 HPNIVRLHDSISEEGFHYLVFDLvTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSK 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 154 -TRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSgSYsGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIR 232
Cdd:cd14086  139 gAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLRKD-PY-GKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIK 216

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 568977678 233 RGQFNIP----ETLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14086  217 AGAYDYPspewDTVTPEAKDLINQMLTVNPAKRITAAEALKHPW 260
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
 75-272 4.10e-33

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: 122.89  E-value: 4.10e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFE-RSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKD-EE 152
Cdd:cd14084   70 HPCIIKIEDFFDAEDDYYIVLElMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSqEE 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 153 RTRVKLESLEDAYILrGDDDSLSDKHGCPAYVSPEILNTSGS--YSgKAADVWSLGVMLYTMLVGRYPF-HDIEPSSLFS 229
Cdd:cd14084  150 ECLIKITDFGLSKIL-GETSLMKTLCGTPTYLAPEVLRSFGTegYT-RAVDCWSLGVILFICLSGYPPFsEEYTQMSLKE 227

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 568977678 230 KIRRGQFN-IPE---TLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14084  228 QILSGKYTfIPKawkNVSEEAKDLVKKMLVVDPSRRPSIEEALEHPW 274
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
 75-272 4.11e-33

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: 122.85  E-value: 4.11e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEIL--LGETKAYVFFE-RSYGDMHSfVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDE 151
Cdd:cd14118   73 HPNVVKLVEVLddPNEDNLYMVFElVDKGAVME-VPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDD 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 152 erTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSG-SYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSK 230
Cdd:cd14118  152 --GHVKIADFGVSNEFEGDDALLSSTAGTPAFMAPEALSESRkKFSGKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEK 229

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 568977678 231 IRRGQFNIPE--TLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14118  230 IKTDPVVFPDdpVVSEQLKDLILRMLDKNPSERITLPEIKEHPW 273
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
 75-272 4.87e-33

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: 122.40  E-value: 4.87e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFERSYGDmHSFVRTCK--KLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEE 152
Cdd:cd14665   55 HPNIVRFKEVILTPTHLAIVMEYAAGG-ELFERICNagRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSP 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 153 RTRVKLESL--EDAYILRGDDDSLSdkhGCPAYVSPEILnTSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSK 230
Cdd:cd14665  134 APRLKICDFgySKSSVLHSQPKSTV---GTPAYIAPEVL-LKKEYDGKIADVWSCGVTLYVMLVGAYPFEDPEEPRNFRK 209

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 568977678 231 ----IRRGQFNIPET--LSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14665  210 tiqrILSVQYSIPDYvhISPECRHLISRIFVADPATRITIPEIRNHEW 257
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
 75-272 1.54e-32

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: 121.02  E-value: 1.54e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFER-SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEER 153
Cdd:cd14077   72 HPHICRLRDFLRTPNHYYMLFEYvDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGN 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 154 TRVKLESLEDAYilrGDDDSLSDKHGCPAYVSPEILNTSgSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRR 233
Cdd:cd14077  152 IKIIDFGLSNLY---DPRRLLRTFCGSLYFAAPELLQAQ-PYTGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKK 227

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568977678 234 GQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14077  228 GKVEYPSYLSSECKSLISRMLVVDPKKRATLEQVLNHPW 266
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
 95-273 2.80e-32

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: 120.03  E-value: 2.80e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  95 FERSYG--DMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFkDEERTRVKLESLEDAYILRgdDD 172
Cdd:cd14005   85 MERPEPcqDLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLI-NLRTGEVKLIDFGCGALLK--DS 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 173 SLSDKHGCPAYVSPEiLNTSGSYSGKAADVWSLGVMLYTMLVGRYPFH-DIEpsslfskIRRGQFNIPETLSPKAKCLIR 251
Cdd:cd14005  162 VYTDFDGTRVYSPPE-WIRHGRYHGRPATVWSLGILLYDMLCGDIPFEnDEQ-------ILRGNVLFRPRLSKECCDLIS 233

                        170       180
                 ....*....|....*....|..
gi 568977678 252 SILRREPSERLTSQEILDHPWF 273
Cdd:cd14005  234 RCLQFDPSKRPSLEQILSHPWF 255
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
 75-273 5.37e-32

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: 119.32  E-value: 5.37e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFERS-YGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFkdEER 153
Cdd:cd14162   59 HPNLICFYEAIETTSRVYIIMELAeNGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLL--DKN 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 154 TRVKLESLEDAYILRGDDDS---LSDKH-GCPAYVSPEILNtSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFS 229
Cdd:cd14162  137 NNLKITDFGFARGVMKTKDGkpkLSETYcGSYAYASPEILR-GIPYDPFLSDIWSMGVVLYTMVYGRLPFDDSNLKVLLK 215

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 568977678 230 KIRRG-QFNIPETLSPKAKCLIRSILRREPsERLTSQEILDHPWF 273
Cdd:cd14162  216 QVQRRvVFPKNPTVSEECKDLILRMLSPVK-KRITIEEIKRDPWF 259
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
 75-272 5.48e-32

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: 119.35  E-value: 5.48e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFER-SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEE- 152
Cdd:cd14095   57 HPNIVQLIEEYDTDTELYLVMELvKGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEd 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 153 -RTRVKLESLEDAYILRgddDSLSDKHGCPAYVSPEILNTSGsYsGKAADVWSLGVMLYTMLVGRYPFH--DIEPSSLFS 229
Cdd:cd14095  137 gSKSLKLADFGLATEVK---EPLFTVCGTPTYVAPEILAETG-Y-GLKVDIWAAGVITYILLCGFPPFRspDRDQEELFD 211

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 568977678 230 KIRRGQFNIP----ETLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14095  212 LILAGEFEFLspywDNISDSAKDLISRMLVVDPEKRYSAGQVLDHPW 258
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
 75-272 9.06e-31

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: 116.41  E-value: 9.06e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFERSYGDmHSFVRTCKKLR--EEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEE 152
Cdd:cd14662   55 HPNIIRFKEVVLTPTHLAIVMEYAAGG-ELFERICNAGRfsEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSP 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 153 RTRVKLESL--EDAYILRGDDDSLSdkhGCPAYVSPEILNTSgSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSK 230
Cdd:cd14662  134 APRLKICDFgySKSSVLHSQPKSTV---GTPAYIAPEVLSRK-EYDGKVADVWSCGVTLYVMLVGAYPFEDPDDPKNFRK 209

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 568977678 231 ----IRRGQFNIPE--TLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14662  210 tiqrIMSVQYKIPDyvRVSQDCRHLLSRIFVANPAKRITIPEIKNHPW 257
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 75-276 1.17e-30

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: 116.53  E-value: 1.17e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFERSYGDmHSFVRTCKK--LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKdee 152
Cdd:cd14169   60 HENIVSLEDIYESPTHLYLAMELVTGG-ELFDRIIERgsYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYA--- 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 153 rtrvklESLEDAYILRGD--------DDSLSDKHGCPAYVSPEILNTSgSYsGKAADVWSLGVMLYTMLVGRYPFHDIEP 224
Cdd:cd14169  136 ------TPFEDSKIMISDfglskieaQGMLSTACGTPGYVAPELLEQK-PY-GKAVDVWAIGVISYILLCGYPPFYDEND 207

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568977678 225 SSLFSKIRRG--QFNIP--ETLSPKAKCLIRSILRREPSERLTSQEILDHPWFSTD 276
Cdd:cd14169  208 SELFNQILKAeyEFDSPywDDISESAKDFIRHLLERDPEKRFTCEQALQHPWISGD 263
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
 75-272 1.22e-30

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: 115.82  E-value: 1.22e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFE-RSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEER 153
Cdd:cd14161   61 HPHIISVYEVFENSSKIVIVMEyASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGN 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 154 TRVKLESLEDAYilrGDDDSLSDKHGCPAYVSPEILNTSgSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRR 233
Cdd:cd14161  141 IKIADFGLSNLY---NQDKFLQTYCGSPLYASPEIVNGR-PYIGPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISS 216

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568977678 234 GQFNIPETLSpKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14161  217 GAYREPTKPS-DACGLIRWLLMVNPERRATLEDVASHWW 254
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 75-276 1.54e-30

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: 116.25  E-value: 1.54e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFER-SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIF-KDEE 152
Cdd:cd14166   59 HENIVTLEDIYESTTHYYLVMQLvSGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYlTPDE 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 153 RTRVK-----LESLEDAYILrgdddslSDKHGCPAYVSPEILnTSGSYSgKAADVWSLGVMLYTMLVGRYPFHDIEPSSL 227
Cdd:cd14166  139 NSKIMitdfgLSKMEQNGIM-------STACGTPGYVAPEVL-AQKPYS-KAVDCWSIGVITYILLCGYPPFYEETESRL 209

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568977678 228 FSKIRRG--QFNIP--ETLSPKAKCLIRSILRREPSERLTSQEILDHPWFSTD 276
Cdd:cd14166  210 FEKIKEGyyEFESPfwDDISESAKDFIRHLLEKNPSKRYTCEKALSHPWIIGN 262
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
 98-273 2.02e-30

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: 115.78  E-value: 2.02e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  98 SYGDMHSFVRTCKKLrEEEAARlFY--QIASAVAHCHDGGLVLRDLKLRKFIFkdEERTRVKLESLEDAYILRGDDDSLS 175
Cdd:cd05581   84 PNGDLLEYIRKYGSL-DEKCTR-FYtaEIVLALEYLHSKGIIHRDLKPENILL--DEDMHIKITDFGTAKVLGPDSSPES 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 176 DKH-----------------GCPAYVSPEILNtsGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNI 238
Cdd:cd05581  160 TKGdadsqiaynqaraasfvGTAEYVSPELLN--EKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYEF 237

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 568977678 239 PETLSPKAKCLIRSILRREPSERLTS------QEILDHPWF 273
Cdd:cd05581  238 PENFPPDAKDLIQKLLVLDPSKRLGVnenggyDELKAHPFF 278
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 75-272 3.22e-30

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: 114.78  E-value: 3.22e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFER-SYGDMhsFVRTCKK--LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDE 151
Cdd:cd14083   60 HPNIVQLLDIYESKSHLYLVMELvTGGEL--FDRIVEKgsYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSP 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 152 ErtrvkleslEDAYILRGD------DDS--LSDKHGCPAYVSPEILNTSGsYsGKAADVWSLGVMLYTMLVGRYPFHDIE 223
Cdd:cd14083  138 D---------EDSKIMISDfglskmEDSgvMSTACGTPGYVAPEVLAQKP-Y-GKAVDCWSIGVISYILLCGYPPFYDEN 206

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568977678 224 PSSLFSKIRRG--QFNIP--ETLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14083  207 DSKLFAQILKAeyEFDSPywDDISDSAKDFIRHLMEKDPNKRYTCEQALEHPW 259
Pkinase pfam00069
Protein kinase domain;
75-273 4.66e-30

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 113.11  E-value: 4.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678   75 HSNINQITEILLGETKAYVFFER-SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHChdgglvlrdlklrkfifkdeer 153
Cdd:pfam00069  57 HPNIVRLYDAFEDKDNLYLVLEYvEGGSLFDLLSEKGAFSEREAKFIMKQILEGLESG---------------------- 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  154 trVKLESLEdayilrgdddslsdkhGCPAYVSPEILntSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRR 233
Cdd:pfam00069 115 --SSLTTFV----------------GTPWYMAPEVL--GGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIID 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 568977678  234 G---QFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:pfam00069 175 QpyaFPELPSNLSEEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
 89-274 7.63e-30

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: 114.24  E-value: 7.63e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  89 TKAYVFFERSY---GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLK------------------LRKFI 147
Cdd:cd05579   64 GKKNLYLVMEYlpgGDLYSLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKpdnilidanghlkltdfgLSKVG 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 148 FKDEERTRVKLEsledayiLRGDDDSLSDKH--GCPAYVSPEILNTSGSysGKAADVWSLGVMLYTMLVGRYPFHDIEPS 225
Cdd:cd05579  144 LVRRQIKLSIQK-------KSNGAPEKEDRRivGTPDYLAPEILLGQGH--GKTVDWWSLGVILYEFLVGIPPFHAETPE 214

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568977678 226 SLFSKIRRGQFNIPE--TLSPKAKCLIRSILRREPSERL---TSQEILDHPWFS 274
Cdd:cd05579  215 EIFQNILNGKIEWPEdpEVSDEAKDLISKLLTPDPEKRLgakGIEEIKNHPFFK 268
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
 75-273 1.80e-29

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: 112.49  E-value: 1.80e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILlgETKAYVFFERSY---GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFkdE 151
Cdd:cd14071   58 HPHIIKLYQVM--ETKDMLYLVTEYasnGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLL--D 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 152 ERTRVKLESLEDAYILRgDDDSLSDKHGCPAYVSPEILNTSgSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKI 231
Cdd:cd14071  134 ANMNIKIADFGFSNFFK-PGELLKTWCGSPPYAAPEVFEGK-EYEGPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRV 211

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568977678 232 RRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd14071  212 LSGRFRIPFFMSTDCEHLIRRMLVLDPSKRLTIEQIKKHKWM 253
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 75-274 2.49e-29

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: 112.43  E-value: 2.49e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFER-SYGDMhsFVRTCKK--LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKD- 150
Cdd:cd14167   60 HPNIVALDDIYESGGHLYLIMQLvSGGEL--FDRIVEKgfYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSl 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 151 EERTRVKLESLEDAYIlRGDDDSLSDKHGCPAYVSPEILnTSGSYSgKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSK 230
Cdd:cd14167  138 DEDSKIMISDFGLSKI-EGSGSVMSTACGTPGYVAPEVL-AQKPYS-KAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQ 214

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 568977678 231 IRRG--QFNIP--ETLSPKAKCLIRSILRREPSERLTSQEILDHPWFS 274
Cdd:cd14167  215 ILKAeyEFDSPywDDISDSAKDFIQHLMEKDPEKRFTCEQALQHPWIA 262
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
 75-272 2.94e-29

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: 112.22  E-value: 2.94e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFERSYGD--MHsfvRTCKK--LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKD 150
Cdd:cd14070   62 HPNITQLLDILETENSYYLVMELCPGGnlMH---RIYDKkrLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDE 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 151 EERTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILntSGSYSGKAADVWSLGVMLYTMLVGRYPFhDIEPSS---L 227
Cdd:cd14070  139 NDNIKLIDFGLSNCAGILGYSDPFSTQCGSPAYAAPELL--ARKKYGPKVDVWSIGVNMYAMLTGTLPF-TVEPFSlraL 215

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568977678 228 FSKIRRGQFN-IPETLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14070  216 HQKMVDKEMNpLPTDLSPGAISFLRSLLEPDPLKRPNIKQALANRW 261
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
 114-272 4.10e-29

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: 112.00  E-value: 4.10e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 114 EEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRV-KLESLEDAYILRGDDdSLSDKHGCPAYVSPEILNTS 192
Cdd:cd14089   99 EREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPNAIlKLTDFGFAKETTTKK-SLQTPCYTPYYVAPEVLGPE 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 193 gSYSgKAADVWSLGVMLYTMLVGRYPFHD-----IEPSsLFSKIRRGQFNIPET----LSPKAKCLIRSILRREPSERLT 263
Cdd:cd14089  178 -KYD-KSCDMWSLGVIMYILLCGYPPFYSnhglaISPG-MKKRIRNGQYEFPNPewsnVSEEAKDLIRGLLKTDPSERLT 254


                 ....*....
gi 568977678 264 SQEILDHPW 272
Cdd:cd14089  255 IEEVMNHPW 263
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
 100-271 9.58e-29

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: 110.63  E-value: 9.58e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCKK----LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRK-FIFKDEertRVKLESLEDAYILRGDDDSL 174
Cdd:cd08215   84 GDLAQKIKKQKKkgqpFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNiFLTKDG---VVKLGDFGISKVLESTTDLA 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 175 SDKHGCPAYVSPEILNtSGSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFN-IPETLSPKAKCLIRSI 253
Cdd:cd08215  161 KTVVGTPYYLSPELCE-NKPYNYKS-DIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPpIPSQYSSELRDLVNSM 238

                        170
                 ....*....|....*...
gi 568977678 254 LRREPSERLTSQEILDHP 271
Cdd:cd08215  239 LQKDPEKRPSANEILSSP 256
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
 72-273 1.04e-28

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: 111.29  E-value: 1.04e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  72 LSAHSNINQITEILlgETKAYVF--FE--RSyGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFI 147
Cdd:cd14093   65 VSGHPNIIELHDVF--ESPTFIFlvFElcRK-GELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENIL 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 148 FKDEERtrVKLESLEDAYILrGDDDSLSDKHGCPAYVSPEILNTS-----GSYsGKAADVWSLGVMLYTMLVGRYPFHDI 222
Cdd:cd14093  142 LDDNLN--VKISDFGFATRL-DEGEKLRELCGTPGYLAPEVLKCSmydnaPGY-GKEVDMWACGVIMYTLLAGCPPFWHR 217

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568977678 223 EPSSLFSKIRRGQFNIP----ETLSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd14093  218 KQMVMLRNIMEGKYEFGspewDDISDTAKDLISKLLVVDPKKRLTAEEALEHPFF 272
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
 114-272 1.14e-28

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: 111.40  E-value: 1.14e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 114 EEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDE-ERTRVKLESLEDAYIlrgDDDSLSDKHGCPAYVSPEILNT- 191
Cdd:cd14171  108 EKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNsEDAPIKLCDFGFAKV---DQGDLMTPQFTPYYVAPQVLEAq 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 192 -------SGSYS-------GKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFS-----KIRRGQFNIPET----LSPKAKC 248
Cdd:cd14171  185 rrhrkerSGIPTsptpytyDKSCDMWSLGVIIYIMLCGYPPFYSEHPSRTITkdmkrKIMTGSYEFPEEewsqISEMAKD 264

                        170       180
                 ....*....|....*....|....
gi 568977678 249 LIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14171  265 IVRKLLCVDPEERMTIEEVLHHPW 288
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
 101-273 1.37e-28

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: 110.55  E-value: 1.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 101 DMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFkdEERTRVKLESL-EDAYILRGDDDSLSdkhG 179
Cdd:cd14004   95 DLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVIL--DGNGTIKLIDFgSAAYIKSGPFDTFV---G 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 180 CPAYVSPEILNTSgSYSGKAADVWSLGVMLYTMLVGRYPFHDIEpsslfsKIRRGQFNIPETLSPKAKCLIRSILRREPS 259
Cdd:cd14004  170 TIDYAAPEVLRGN-PYGGKEQDIWALGVLLYTLVFKENPFYNIE------EILEADLRIPYAVSEDLIDLISRMLNRDVG 242

                        170
                 ....*....|....
gi 568977678 260 ERLTSQEILDHPWF 273
Cdd:cd14004  243 DRPTIEELLTDPWL 256
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
 75-271 1.37e-28

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 109.28  E-value: 1.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFER-SYGDMHSFVRTC-KKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEE 152
Cdd:cd00180   50 HPNIVKLYDVFETENFLYLVMEYcEGGSLKDLLKENkGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDG 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 153 rtRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSGSYSGKAADVWSLGVMLYTMlvgrypfhdiepsslfskir 232
Cdd:cd00180  130 --TVKLADFGLAKDLDSDDSLLKTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL-------------------- 187

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568977678 233 rgqfnipetlsPKAKCLIRSILRREPSERLTSQEILDHP 271
Cdd:cd00180  188 -----------EELKDLIRRMLQYDPKKRPSAKELLEHL 215
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
 110-273 1.92e-28

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: 110.80  E-value: 1.92e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 110 KKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRvklESLE--D---AYILRGDDDSLSDKHGCPAYV 184
Cdd:cd14091   89 KFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGDP---ESLRicDfgfAKQLRAENGLLMTPCYTANFV 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 185 SPEILNTSGsYSgKAADVWSLGVMLYTMLVGRYPF----HDiEPSSLFSKIRRGQFNIP----ETLSPKAKCLIRSILRR 256
Cdd:cd14091  166 APEVLKKQG-YD-AACDIWSLGVLLYTMLAGYTPFasgpND-TPEVILARIGSGKIDLSggnwDHVSDSAKDLVRKMLHV 242

                        170
                 ....*....|....*..
gi 568977678 257 EPSERLTSQEILDHPWF 273
Cdd:cd14091  243 DPSQRPTAAQVLQHPWI 259
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
 75-272 2.26e-28

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: 110.27  E-value: 2.26e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILlgETKAYVFFERSY---GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFkDE 151
Cdd:cd14076   65 HPNIVRLLDVL--KTKKYIGIVLEFvsgGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLL-DK 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 152 ERTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSGSYSGKAADVWSLGVMLYTMLVGRYPFHDiEPSS----- 226
Cdd:cd14076  142 NRNLVITDFGFANTFDHFNGDLMSTSCGSPCYAAPELVVSDSMYAGRKADIWSCGVILYAMLAGYLPFDD-DPHNpngdn 220

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568977678 227 ---LFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14076  221 vprLYRYICNTPLIFPEYVTPKARDLLRRILVPNPRKRIRLSAIMRHAW 269
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 37-282 4.49e-28

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: 110.51  E-value: 4.49e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  37 RARTHTRTHSRARSEIPGHVFEISCYQESLAPCFClSAHSNINQITEILLGETKAYVFFER-SYGDMHSFVRTCKKLREE 115
Cdd:cd14179   24 RKCLHKKTNQEYAVKIVSKRMEANTQREIAALKLC-EGHPNIVKLHEVYHDQLHTFLVMELlKGGELLERIKKKQHFSET 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 116 EAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDE-ERTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSGs 194
Cdd:cd14179  103 EASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDEsDNSEIKIIDFGFARLKPPDNQPLKTPCFTLHYAAPELLNYNG- 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 195 YSgKAADVWSLGVMLYTMLVGRYPFHDIEPS-------SLFSKIRRGQFNIP----ETLSPKAKCLIRSILRREPSERLT 263
Cdd:cd14179  182 YD-ESCDLWSLGVILYTMLSGQVPFQCHDKSltctsaeEIMKKIKQGDFSFEgeawKNVSQEAKDLIQGLLTVDPNKRIK 260

                        250
                 ....*....|....*....
gi 568977678 264 SQEILDHPWFSTDFSVSNS 282
Cdd:cd14179  261 MSGLRYNEWLQDGSQLSSN 279
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
 75-273 8.76e-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: 108.33  E-value: 8.76e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEIL-LGETKAYVFFERSY-GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEe 152
Cdd:cd14165   60 HKSIIKTYEIFeTSDGKVYIVMELGVqGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKD- 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 153 rTRVKLESLEDAYILRGDDDS---LSDKH-GCPAYVSPEILNtSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLF 228
Cdd:cd14165  139 -FNIKLTDFGFSKRCLRDENGrivLSKTFcGSAAYAAPEVLQ-GIPYDPRIYDIWSLGVILYIMVCGSMPYDDSNVKKML 216

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 568977678 229 SKIRRGQFNIPET--LSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd14165  217 KIQKEHRVRFPRSknLTSECKDLIYRLLQPDVSQRLCIDEVLSHPWL 263
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
 75-272 1.50e-27

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: 107.31  E-value: 1.50e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFErsY---GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIF-KD 150
Cdd:cd14009   51 HPNIVRLYDVQKTEDFIYLVLE--YcagGDLSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLsTS 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 151 EERTRVKLESLEDAYILrgDDDSLSDK-HGCPAYVSPEILNtSGSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPSSLFS 229
Cdd:cd14009  129 GDDPVLKIADFGFARSL--QPASMAETlCGSPLYMAPEILQ-FQKYDAKA-DLWSVGAILFEMLVGKPPFRGSNHVQLLR 204

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 568977678 230 KIRRG----QFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14009  205 NIERSdaviPFPIAAQLSPDCKDLLRRLLRRDPAERISFEEFFAHPF 251
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
 62-273 1.65e-27

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: 107.78  E-value: 1.65e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  62 YQESLAPCFCLSA---HSNINQITEILLGETKAYVFFER--SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGL 136
Cdd:cd13994   40 YVKRLTSEYIISSklhHPNIVKVLDLCQDLHGKWCLVMEycPGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGI 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 137 VLRDLKLRKFIFkdEERTRVKLESLEDAYILRGDDDSLSDKH----GCPAYVSPEILnTSGSYSGKAADVWSLGVMLYTM 212
Cdd:cd13994  120 AHRDLKPENILL--DEDGVLKLTDFGTAEVFGMPAEKESPMSaglcGSEPYMAPEVF-TSGSYDGRAVDVWSCGIVLFAL 196

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568977678 213 LVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPK--------AKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd13994  197 FTGRFPWRSAKKSDSAYKAYEKSGDFTNGPYEPienllpseCRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
 71-272 1.87e-27

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: 107.25  E-value: 1.87e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  71 CLSAHSNINQITEILLGETKAYVFFERSY-GDMHSFVRTCKK-LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIF 148
Cdd:cd14186   56 CQLKHPSILELYNYFEDSNYVYLVLEMCHnGEMSRYLKNRKKpFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLL 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 149 KDEerTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEIlnTSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLF 228
Cdd:cd14186  136 TRN--MNIKIADFGLATQLKMPHEKHFTMCGTPNYISPEI--ATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTL 211

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 568977678 229 SKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14186  212 NKVVLADYEMPAFLSREAQDLIHQLLRKNPADRLSLSSVLDHPF 255
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
 100-275 2.55e-27

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: 107.66  E-value: 2.55e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCKKLREEEAarLFY--QIASAVAHCHDGGLVLRDLK-------------LRKFIF--KDEERTrvklesle 162
Cdd:cd05580   86 GELFSLLRRSGRFPNDVA--KFYaaEVVLALEYLHSLDIVYRDLKpenllldsdghikITDFGFakRVKDRT-------- 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 163 daYILrgdddslsdkHGCPAYVSPEILNTSGSysGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETL 242
Cdd:cd05580  156 --YTL----------CGTPEYLAPEIILSKGH--GKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFPSFF 221

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568977678 243 SPKAKCLIRSILRREPSERL-----TSQEILDHPWFST 275
Cdd:cd05580  222 DPDAKDLIKRLLVVDLTKRLgnlknGVEDIKNHPWFAG 259
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
 20-272 2.96e-27

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: 107.50  E-value: 2.96e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  20 GNVSVTLNGETEREQARRARTHTRTHSRARseipghVF-EIscyqESLAPCfclSAHSNINQITEILLGETKAYVFFERS 98
Cdd:cd14090   16 ASVQTCINLYTGKEYAVKIIEKHPGHSRSR------VFrEV----ETLHQC---QGHPNILQLIEYFEDDERFYLVFEKM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  99 YG-DMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEER-TRVKLESLEDAYILRGDDDS--- 173
Cdd:cd14090   83 RGgPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKvSPVKICDFDLGSGIKLSSTSmtp 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 174 -----LSDKHGCPAYVSPEILNT---SGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSS---------------LFSK 230
Cdd:cd14090  163 vttpeLLTPVGSAEYMAPEVVDAfvgEALSYDKRCDLWSLGVILYIMLCGYPPFYGRCGEDcgwdrgeacqdcqelLFHS 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 568977678 231 IRRGQFNIPET----LSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14090  243 IQEGEYEFPEKewshISAEAKDLISHLLVRDASQRYTAEQVLQHPW 288
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
 75-271 4.35e-27

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: 106.33  E-value: 4.35e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFER-SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFkdEER 153
Cdd:cd06632   61 HPNIVQYYGTEREEDNLYIFLEYvPGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILV--DTN 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 154 TRVKLESLEDAYILRGDDDSLSDKhGCPAYVSPEILNTSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRR 233
Cdd:cd06632  139 GVVKLADFGMAKHVEAFSFAKSFK-GSPYWMAPEVIMQKNSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGN 217

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568977678 234 GQF--NIPETLSPKAKCLIRSILRREPSERLTSQEILDHP 271
Cdd:cd06632  218 SGElpPIPDHLSPDAKDFIRLCLQRDPEDRPTASQLLEHP 257
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
 112-273 1.06e-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: 105.39  E-value: 1.06e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 112 LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKdeERTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNT 191
Cdd:cd14189   98 LLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFIN--ENMELKVGDFGLAARLEPPEQRKKTICGTPNYLAPEVLLR 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 192 SGSysGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHP 271
Cdd:cd14189  176 QGH--GPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPASLSLPARHLLAGILKRNPGDRLTLDQILEHE 253


                 ..
gi 568977678 272 WF 273
Cdd:cd14189  254 FF 255
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
 75-272 9.19e-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: 102.60  E-value: 9.19e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFE-RSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEER 153
Cdd:cd14072   58 HPNIVKLFEVIETEKTLYLVMEyASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMN 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 154 TRVKLESLEDAYILRGDDDSLSdkhGCPAYVSPEILNTSgSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRR 233
Cdd:cd14072  138 IKIADFGFSNEFTPGNKLDTFC---GSPPYAAPELFQGK-KYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLR 213

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568977678 234 GQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14072  214 GKYRIPFYMSTDCENLLKKFLVLNPSKRGTLEQIMKDRW 252
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
 101-272 1.41e-25

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: 102.36  E-value: 1.41e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 101 DMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKlRKFIFKDEERTRVKLESLEDAYILRgdDDSLSDKHGC 180
Cdd:cd14100   92 DLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIK-DENILIDLNTGELKLIDFGSGALLK--DTVYTDFDGT 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 181 PAYVSPEILNTSgSYSGKAADVWSLGVMLYTMLVGRYPF-HDIEpsslfskIRRGQFNIPETLSPKAKCLIRSILRREPS 259
Cdd:cd14100  169 RVYSPPEWIRFH-RYHGRSAAVWSLGILLYDMVCGDIPFeHDEE-------IIRGQVFFRQRVSSECQHLIKWCLALRPS 240

                        170
                 ....*....|...
gi 568977678 260 ERLTSQEILDHPW 272
Cdd:cd14100  241 DRPSFEDIQNHPW 253
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
 22-272 1.97e-25

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: 102.80  E-value: 1.97e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  22 VSVTLNGETEREQARRARTHTRTHSRARseipghVF-EIscyqESLAPCfclSAHSNINQITEILLGETKAYVFFERSYG 100
Cdd:cd14173   18 VQTCINLITNKEYAVKIIEKRPGHSRSR------VFrEV----EMLYQC---QGHRNVLELIEFFEEEDKFYLVFEKMRG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 101 -DMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEER-TRVKL--ESLEDAYILRGDDDSLSD 176
Cdd:cd14173   85 gSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQvSPVKIcdFDLGSGIKLNSDCSPIST 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 177 KH-----GCPAYVSPEIL---NTSGSYSGKAADVWSLGVMLYTMLVGRYPF-----HDI-----EP-----SSLFSKIRR 233
Cdd:cd14173  165 PElltpcGSAEYMAPEVVeafNEEASIYDKRCDLWSLGVILYIMLSGYPPFvgrcgSDCgwdrgEAcpacqNMLFESIQE 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 568977678 234 GQFNIPET----LSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14173  245 GKYEFPEKdwahISCAAKDLISKLLVRDAKQRLSAAQVLQHPW 287
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
 101-272 3.05e-25

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


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 101.57  E-value: 3.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 101 DMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFkDEERTRVKLESLEDAYILRgdDDSLSDKHGC 180
Cdd:cd14102   91 DLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLV-DLRTGELKLIDFGSGALLK--DTVYTDFDGT 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 181 PAYVSPEILNTSgSYSGKAADVWSLGVMLYTMLVGRYPFHDIEpsslfsKIRRGQFNIPETLSPKAKCLIRSILRREPSE 260
Cdd:cd14102  168 RVYSPPEWIRYH-RYHGRSATVWSLGVLLYDMVCGDIPFEQDE------EILRGRLYFRRRVSPECQQLIKWCLSLRPSD 240

                        170
                 ....*....|..
gi 568977678 261 RLTSQEILDHPW 272
Cdd:cd14102  241 RPTLEQIFDHPW 252
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 100-271 5.14e-25

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: 101.08  E-value: 5.14e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCKKLRE--EEAA--RLFYQIASAVAHCH----DGGLVL-RDLKLRKfIFKDEERTrVKLESLEDAYILRGD 170
Cdd:cd08217   86 GDLAQLIKKCKKENQyiPEEFiwKIFTQLLLALYECHnrsvGGGKILhRDLKPAN-IFLDSDNN-VKLGDFGLARVLSHD 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 171 DDSLSDKHGCPAYVSPEILNtSGSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFN-IPETLSPKAKCL 249
Cdd:cd08217  164 SSFAKTYVGTPYYMSPELLN-EQSYDEKS-DIWSLGCLIYELCALHPPFQAANQLELAKKIKEGKFPrIPSRYSSELNEV 241

                        170       180
                 ....*....|....*....|..
gi 568977678 250 IRSILRREPSERLTSQEILDHP 271
Cdd:cd08217  242 IKSMLNVDPDKRPSVEELLQLP 263
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
 88-275 5.20e-25

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: 102.08  E-value: 5.20e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  88 ETKAYVFFERSY---GDMHSFVRTCKKLrEEEAARlFY--QIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRV------ 156
Cdd:cd05592   66 QTESHLFFVMEYlngGDLMFHIQQSGRF-DEDRAR-FYgaEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIadfgmc 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 157 KLESLedayilrgDDDSLSDKHGCPAYVSPEILNtsGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQF 236
Cdd:cd05592  144 KENIY--------GENKASTFCGTPDYIAPEILK--GQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTP 213

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 568977678 237 NIPETLSPKAKCLIRSILRREPSERLTSQE-----ILDHPWFST 275
Cdd:cd05592  214 HYPRWLTKEAASCLSLLLERNPEKRLGVPEcpagdIRDHPFFKT 257
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
 75-272 5.22e-25

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: 101.01  E-value: 5.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFER-SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEER 153
Cdd:cd14098   60 HPGIVRLIDWYEDDQHIYLVMEYvEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDP 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 154 TRVKLESLEDAYILRGDDdSLSDKHGCPAYVSPEIL-----NTSGSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPSSLF 228
Cdd:cd14098  140 VIVKISDFGLAKVIHTGT-FLVTFCGTMAYLAPEILmskeqNLQGGYSNLV-DMWSVGCLVYVMLTGALPFDGSSQLPVE 217

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 568977678 229 SKIRRGQFNIPETL----SPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14098  218 KRIRKGRYTQPPLVdfniSEEAIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
 75-294 6.66e-25

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: 101.26  E-value: 6.66e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFE-RSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDE-- 151
Cdd:cd14175   54 HPNIITLKDVYDDGKHVYLVTElMRGGELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDEsg 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 152 ERTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSGSYSGkaADVWSLGVMLYTMLVGRYPFHD---IEPSSLF 228
Cdd:cd14175  134 NPESLRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDEG--CDIWSLGILLYTMLAGYTPFANgpsDTPEEIL 211

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 229 SKIRRGQFNIP----ETLSPKAKCLIRSILRREPSERLTSQEILDHPWFSTDFSVSNSGFGAKEAcdQLV 294
Cdd:cd14175  212 TRIGSGKFTLSggnwNTVSDAAKDLVSKMLHVDPHQRLTAKQVLQHPWITQKDKLPQSQLNHQDV--QLV 279
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
 115-275 7.06e-25

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: 102.01  E-value: 7.06e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 115 EEAARlFY--QIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDAYIlrGDDDSLSDKHGCPAYVSPEILNTS 192
Cdd:cd05595   94 EDRAR-FYgaEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGI--TDGATMKTFCGTPEYLAPEVLEDN 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 193 gSYsGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERL-----TSQEI 267
Cdd:cd05595  171 -DY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLgggpsDAKEV 248


                 ....*...
gi 568977678 268 LDHPWFST 275
Cdd:cd05595  249 MEHRFFLS 256
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
 75-272 1.39e-24

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: 99.55  E-value: 1.39e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEIL-LGETKAYVFFERSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEER 153
Cdd:cd14164   59 HPNIVQMFECIeVANGRLYIVMEAAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDR 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 154 tRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILnTSGSYSGKAADVWSLGVMLYTMLVGRYPFHDiepsSLFSKIRR 233
Cdd:cd14164  139 -KIKIADFGFARFVEDYPELSTTFCGSRAYTPPEVI-LGTPYDPKKYDVWSLGVVLYVMVTGTMPFDE----TNVRRLRL 212

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 568977678 234 GQ--FNIPETLSPKAKC--LIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14164  213 QQrgVLYPSGVALEEPCraLIRTLLQFNPSTRPSIQQVAGNSW 255
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
 75-272 1.52e-24

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: 100.59  E-value: 1.52e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILlgETKAYVFFERSYGD----MHSFVR-TCkkLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFK 149
Cdd:cd14096   65 HPNIVKLLDFQ--ESDEYYYIVLELADggeiFHQIVRlTY--FSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFE 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 150 --DEERTRVKLESLEDAY------------------ILRGDDDSLS----DKH-----GCPAYVSPEILnTSGSYSgKAA 200
Cdd:cd14096  141 piPFIPSIVKLRKADDDEtkvdegefipgvggggigIVKLADFGLSkqvwDSNtktpcGTVGYTAPEVV-KDERYS-KKV 218

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568977678 201 DVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFnipETLSP-------KAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14096  219 DMWALGCVLYTLLCGFPPFYDESIETLTEKISRGDY---TFLSPwwdeiskSAKDLISHLLTVDPAKRYDIDEFLAHPW 294
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
 75-274 2.01e-24

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


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 100.02  E-value: 2.01e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEIL--LGETKAYVFFERSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEe 152
Cdd:cd14200   82 HVNIVKLIEVLddPAEDNLYMVFDLLRKGPVMEVPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDD- 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 153 rTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSG-SYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKI 231
Cdd:cd14200  161 -GHVKIADFGVSNQFEGNDALLSSTAGTPAFMAPETLSDSGqSFSGKALDVWAMGVTLYCFVYGKCPFIDEFILALHNKI 239

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 568977678 232 RRGQFNIPE--TLSPKAKCLIRSILRREPSERLTSQEILDHPWFS 274
Cdd:cd14200  240 KNKPVEFPEepEISEELKDLILKMLDKNPETRITVPEIKVHPWVT 284
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
 88-274 2.39e-24

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: 100.37  E-value: 2.39e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  88 ETKAYVFFERSY---GDMHSFVRTCKKLREEEAArlFY--QIASAVAHCHDGGLVLRDLKLRKfIFKDEErTRVKL---- 158
Cdd:cd05570   66 QTEDRLYFVMEYvngGDLMFHIQRARRFTEERAR--FYaaEICLALQFLHERGIIYRDLKLDN-VLLDAE-GHIKIadfg 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 159 ---ESLedayilrGDDDSLSDKHGCPAYVSPEILNTSgSYsGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQ 235
Cdd:cd05570  142 mckEGI-------WGGNTTSTFCGTPDYIAPEILREQ-DY-GFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDE 212

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 568977678 236 FNIPETLSPKAKCLIRSILRREPSERLTS-----QEILDHPWFS 274
Cdd:cd05570  213 VLYPRWLSREAVSILKGLLTKDPARRLGCgpkgeADIKAHPFFR 256
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
 75-273 2.57e-24

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: 98.93  E-value: 2.57e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFER-SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKdeER 153
Cdd:cd14188   60 HKHVVQFYHYFEDKENIYILLEYcSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFIN--EN 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 154 TRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSGSysGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRR 233
Cdd:cd14188  138 MELKVGDFGLAARLEPLEHRRRTICGTPNYLSPEVLNKQGH--GCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIRE 215

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568977678 234 GQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd14188  216 ARYSLPSSLLAPAKHLIASMLSKNPEDRPSLDEIIRHDFF 255
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
 75-272 2.59e-24

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: 98.88  E-value: 2.59e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFER-SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEER 153
Cdd:cd14006   48 HPRIIQLHEAYESPTELVLILELcSGGELLDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPS 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 154 TRVKLESLEDAYILrGDDDSLSDKHGCPAYVSPEILNtsGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRR 233
Cdd:cd14006  128 PQIKIIDFGLARKL-NPGEELKEIFGTPEFVAPEIVN--GEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISA 204

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 568977678 234 GQFNIPET----LSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14006  205 CRVDFSEEyfssVSQEAKDFIRKLLVKEPRKRPTAQEALQHPW 247
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
 75-272 3.17e-24

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: 98.51  E-value: 3.17e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFER-SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEER 153
Cdd:cd14121   54 HPHIVELKDFQWDEEHIYLIMEYcSGGDLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYN 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 154 TRVKLESLEDAYILRGDDDSLSDKhGCPAYVSPEILnTSGSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRR 233
Cdd:cd14121  134 PVLKLADFGFAQHLKPNDEAHSLR-GSPLYMAPEMI-LKKKYDARV-DLWSVGVILYECLFGRAPFASRSFEELEEKIRS 210

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568977678 234 GQ-FNIPET--LSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14121  211 SKpIEIPTRpeLSADCRDLLLRLLQRDPDRRISFEEFFAHPF 252
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 75-276 4.73e-24

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: 99.35  E-value: 4.73e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFERSYGDmHSFVRTCKK--LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFI-FKDE 151
Cdd:cd14168   67 HENIVALEDIYESPNHLYLVMQLVSGG-ELFDRIVEKgfYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLyFSQD 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 152 ERTRVKLESLEDAYiLRGDDDSLSDKHGCPAYVSPEILnTSGSYSgKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKI 231
Cdd:cd14168  146 EESKIMISDFGLSK-MEGKGDVMSTACGTPGYVAPEVL-AQKPYS-KAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQI 222

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568977678 232 RRG--QFNIP--ETLSPKAKCLIRSILRREPSERLTSQEILDHPWFSTD 276
Cdd:cd14168  223 LKAdyEFDSPywDDISDSAKDFIRNLMEKDPNKRYTCEQALRHPWIAGD 271
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
 88-275 9.29e-24

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: 97.55  E-value: 9.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  88 ETKAYVFFERSY---GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFkdEERTRVKLESL--- 161
Cdd:cd05611   67 QSKDYLYLVMEYlngGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLI--DQTGHLKLTDFgls 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 162 EDAYILRGDDDSLsdkhGCPAYVSPEILNtsGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIP-- 239
Cdd:cd05611  145 RNGLEKRHNKKFV----GTPDYLAPETIL--GVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPee 218

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 568977678 240 --ETLSPKAKCLIRSILRREPSERLTS---QEILDHPWFST 275
Cdd:cd05611  219 vkEFCSPEAVDLINRLLCMDPAKRLGAngyQEIKSHPFFKS 259
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
 45-272 1.83e-23

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: 97.41  E-value: 1.83e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  45 HSRARseipghVF-EIscyqESLAPCfclSAHSNINQITEILLGETKAYVFFERSYG-DMHSFVRTCKKLREEEAARLFY 122
Cdd:cd14174   41 HSRSR------VFrEV----ETLYQC---QGNKNILELIEFFEDDTRFYLVFEKLRGgSILAHIQKRKHFNEREASRVVR 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 123 QIASAVAHCHDGGLVLRDLKLRKFIFKDEER-TRVKLESLEDAYILRGDDD-------SLSDKHGCPAYVSPEILNT--- 191
Cdd:cd14174  108 DIASALDFLHTKGIAHRDLKPENILCESPDKvSPVKICDFDLGSGVKLNSActpittpELTTPCGSAEYMAPEVVEVftd 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 192 SGSYSGKAADVWSLGVMLYTMLVGRYPFHD---------------IEPSSLFSKIRRGQFNIPET----LSPKAKCLIRS 252
Cdd:cd14174  188 EATFYDKRCDLWSLGVILYIMLSGYPPFVGhcgtdcgwdrgevcrVCQNKLFESIQEGKYEFPDKdwshISSEAKDLISK 267

                        250       260
                 ....*....|....*....|
gi 568977678 253 ILRREPSERLTSQEILDHPW 272
Cdd:cd14174  268 LLVRDAKERLSAAQVLQHPW 287
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
 92-273 1.92e-23

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: 96.44  E-value: 1.92e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  92 YVFFER-SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKfIFKDEERtRVKL------ESLEDA 164
Cdd:cd06606   75 NIFLEYvPGGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGAN-ILVDSDG-VVKLadfgcaKRLAEI 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 165 YILrgddDSLSDKHGCPAYVSPEILNTSGSysGKAADVWSLGVMLYTMLVGRYPFHDIE-PSSLFSKIRRGQF--NIPET 241
Cdd:cd06606  153 ATG----EGTKSLRGTPYWMAPEVIRGEGY--GRAADIWSLGCTVIEMATGKPPWSELGnPVAALFKIGSSGEppPIPEH 226

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568977678 242 LSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd06606  227 LSEEAKDFLRKCLQRDPKKRPTADELLQHPFL 258
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
 75-272 2.06e-23

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: 96.45  E-value: 2.06e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFE-RSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDE-E 152
Cdd:cd14087   56 HTNIIQLIEVFETKERVYMVMElATGGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPgP 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 153 RTRVKLESLEDAYILR-GDDDSLSDKHGCPAYVSPEILnTSGSYSgKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKI 231
Cdd:cd14087  136 DSKIMITDFGLASTRKkGPNCLMKTTCGTPEYIAPEIL-LRKPYT-QSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQI 213

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 568977678 232 RRGQFNI-PE---TLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14087  214 LRAKYSYsGEpwpSVSNLAKDFIDRLLTVNPGERLSATQALKHPW 258
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
 74-269 3.60e-23

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: 95.73  E-value: 3.60e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  74 AHSNINQITEILLGETKAYVFFERSYG-DMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLK----LrkfIF 148
Cdd:cd14014   58 SHPNIVRVYDVGEDDGRPYIVMEYVEGgSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKpaniL---LT 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 149 KDEertRVKLEsleD---AYILRGDDDSLSDKHGC-PAYVSPEILntSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEP 224
Cdd:cd14014  135 EDG---RVKLT---DfgiARALGDSGLTQTGSVLGtPAYMAPEQA--RGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSP 206

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 568977678 225 SSLFSKIRRGQFNIPET----LSPKAKCLIRSILRREPSERLTS-QEILD 269
Cdd:cd14014  207 AAVLAKHLQEAPPPPSPlnpdVPPALDAIILRALAKDPEERPQSaAELLA 256
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 75-272 6.01e-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: 96.05  E-value: 6.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFERSYGDmHSFVRTCKK--LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDE- 151
Cdd:cd14085   57 HPNIIKLKEIFETPTEISLVLELVTGG-ELFDRIVEKgyYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPa 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 152 ERTRVKLESLEDAYILRgDDDSLSDKHGCPAYVSPEILntSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSS-LFSK 230
Cdd:cd14085  136 PDAPLKIADFGLSKIVD-QQVTMKTVCGTPGYCAPEIL--RGCAYGPEVDMWSVGVITYILLCGFEPFYDERGDQyMFKR 212

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568977678 231 IRRGQFNI--P--ETLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14085  213 ILNCDYDFvsPwwDDVSLNAKDLVKKLIVLDPKKRLTTQQALQHPW 258
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
 75-272 6.94e-23

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: 95.31  E-value: 6.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFERSY-GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFK---- 149
Cdd:cd14097   59 HAHIIHLEEVFETPKRMYLVMELCEdGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKssii 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 150 -DEERTRVKLESLEDAYILRG-DDDSLSDKHGCPAYVSPEILNTSGsYSgKAADVWSLGVMLYTMLVGRYPFHDIEPSSL 227
Cdd:cd14097  139 dNNDKLNIKVTDFGLSVQKYGlGEDMLQETCGTPIYMAPEVISAHG-YS-QQCDIWSIGVIMYMLLCGEPPFVAKSEEKL 216

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568977678 228 FSKIRRGQFNIP----ETLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14097  217 FEEIRKGDLTFTqsvwQSVSDAAKNVLQQLLKVDPAHRMTASELLDNPW 265
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
 114-275 1.15e-22

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: 95.93  E-value: 1.15e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 114 EEEAArlFY--QIASAVAHCHDGGLVLRDLKLRKfIFKDEErTRVKL-------ESLEDayilrgddDSLSDKH-GCPAY 183
Cdd:cd05584   99 EDTAC--FYlaEITLALGHLHSLGIIYRDLKPEN-ILLDAQ-GHVKLtdfglckESIHD--------GTVTHTFcGTIEY 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 184 VSPEILNTSGSysGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLT 263
Cdd:cd05584  167 MAPEILTRSGH--GKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLPPYLTNEARDLLKKLLKRNVSSRLG 244

                        170
                 ....*....|....*..
gi 568977678 264 S-----QEILDHPWFST 275
Cdd:cd05584  245 SgpgdaEEIKAHPFFRH 261
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
 75-272 1.20e-22

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: 95.03  E-value: 1.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEIL--LGETKAYVFFERSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKdeE 152
Cdd:cd14199   84 HPNVVKLVEVLddPSEDHLYMVFELVKQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVG--E 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 153 RTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILN-TSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKI 231
Cdd:cd14199  162 DGHIKIADFGVSNEFEGSDALLTNTVGTPAFMAPETLSeTRKIFSGKALDVWAMGVTLYCFVFGQCPFMDERILSLHSKI 241

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 568977678 232 RRGQFNIPET--LSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14199  242 KTQPLEFPDQpdISDDLKDLLFRMLDKNPESRISVPEIKLHPW 284
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
 75-272 2.18e-22

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: 94.09  E-value: 2.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFER-SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIF--KDE 151
Cdd:cd14105   67 HPNIITLHDVFENKTDVVLILELvAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLldKNV 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 152 ERTRVKLESLEDAYILRgDDDSLSDKHGCPAYVSPEILNtsgsYS--GKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFS 229
Cdd:cd14105  147 PIPRIKLIDFGLAHKIE-DGNEFKNIFGTPEFVAPEIVN----YEplGLEADMWSIGVITYILLSGASPFLGDTKQETLA 221

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 568977678 230 KIRRGQFNIPETL----SPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14105  222 NITAVNYDFDDEYfsntSELAKDFIRQLLVKDPRKRMTIQESLRHPW 268
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
 110-272 2.42e-22

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: 95.09  E-value: 2.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 110 KKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERT--RVKLESLEDAYILRGDDDSLSDKHGCPAYVSPE 187
Cdd:cd14176  108 KFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNpeSIRICDFGFAKQLRAENGLLMTPCYTANFVAPE 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 188 ILNTSGsYSGkAADVWSLGVMLYTMLVGRYPFH---DIEPSSLFSKIRRGQFNIP----ETLSPKAKCLIRSILRREPSE 260
Cdd:cd14176  188 VLERQG-YDA-ACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSggywNSVSDTAKDLVSKMLHVDPHQ 265

                        170
                 ....*....|..
gi 568977678 261 RLTSQEILDHPW 272
Cdd:cd14176  266 RLTAALVLRHPW 277
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
 92-277 2.91e-22

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: 93.46  E-value: 2.91e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  92 YVFFE----RSYGDMHsfvRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEerTRVKLESLEDAYIL 167
Cdd:cd14187   83 YVVLElcrrRSLLELH---KRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDD--MEVKIGDFGLATKV 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 168 RGDDDSLSDKHGCPAYVSPEILNTSG-SYSgkaADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKA 246
Cdd:cd14187  158 EYDGERKKTLCGTPNYIAPEVLSKKGhSFE---VDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVA 234

                        170       180       190
                 ....*....|....*....|....*....|.
gi 568977678 247 KCLIRSILRREPSERLTSQEILDHPWFSTDF 277
Cdd:cd14187  235 ASLIQKMLQTDPTARPTINELLNDEFFTSGY 265
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
 101-272 3.44e-22

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


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 93.38  E-value: 3.44e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 101 DMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKlRKFIFKDEERTRVKLESLEDAYILRgdDDSLSDKHGC 180
Cdd:cd14101   94 DLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIK-DENILVDLRTGDIKLIDFGSGATLK--DSMYTDFDGT 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 181 PAYVSPEILNTSgSYSGKAADVWSLGVMLYTMLVGRYPFHDIEpsslfsKIRRGQFNIPETLSPKAKCLIRSILRREPSE 260
Cdd:cd14101  171 RVYSPPEWILYH-QYHALPATVWSLGILLYDMVCGDIPFERDT------DILKAKPSFNKRVSNDCRSLIRSCLAYNPSD 243

                        170
                 ....*....|..
gi 568977678 261 RLTSQEILDHPW 272
Cdd:cd14101  244 RPSLEQILLHPW 255
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
 75-276 3.72e-22

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: 93.52  E-value: 3.72e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFER-SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEER 153
Cdd:cd14183   63 HPNIVLLIEEMDMPTELYLVMELvKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQD 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 154 TRVKLEsLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSGSysGKAADVWSLGVMLYTMLVGRYPFHDI--EPSSLFSKI 231
Cdd:cd14183  143 GSKSLK-LGDFGLATVVDGPLYTVCGTPTYVAPEIIAETGY--GLKVDIWAAGVITYILLCGFPPFRGSgdDQEVLFDQI 219

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568977678 232 RRGQFNIP----ETLSPKAKCLIRSILRREPSERLTSQEILDHPWFSTD 276
Cdd:cd14183  220 LMGQVDFPspywDNVSDSAKELITMMLQVDVDQRYSALQVLEHPWVNDD 268
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
 110-274 4.00e-22

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: 93.93  E-value: 4.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 110 KKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERT--RVKLESLEDAYILRGDDDSLSDKHGCPAYVSPE 187
Cdd:cd14177   93 KFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSANadSIRICDFGFAKQLRGENGLLLTPCYTANFVAPE 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 188 ILNTSGsYSGkAADVWSLGVMLYTMLVGRYPFH---DIEPSSLFSKIRRGQFNIP----ETLSPKAKCLIRSILRREPSE 260
Cdd:cd14177  173 VLMRQG-YDA-ACDIWSLGVLLYTMLAGYTPFAngpNDTPEEILLRIGSGKFSLSggnwDTVSDAAKDLLSHMLHVDPHQ 250

                        170
                 ....*....|....
gi 568977678 261 RLTSQEILDHPWFS 274
Cdd:cd14177  251 RYTAEQVLKHSWIA 264
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
 88-273 4.13e-22

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: 94.61  E-value: 4.13e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  88 ETKAYVFFERSY---GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDA 164
Cdd:cd05619   76 QTKENLFFVMEYlngGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKE 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 165 YILrgDDDSLSDKHGCPAYVSPEILntSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSP 244
Cdd:cd05619  156 NML--GDAKTSTFCGTPDYIAPEIL--LGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRMDNPFYPRWLEK 231

                        170       180       190
                 ....*....|....*....|....*....|
gi 568977678 245 KAKCLIRSILRREPSERLTSQ-EILDHPWF 273
Cdd:cd05619  232 EAKDILVKLFVREPERRLGVRgDIRQHPFF 261
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
 55-306 5.36e-22

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


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 94.71  E-value: 5.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  55 HVFEiscyQESLAPcFCLSAHSNInqiteillgETKAYVFFERSY---GDMHSFVRTCKKLREEEAARLFYQIASAVAHC 131
Cdd:cd05618   72 HVFE----QASNHP-FLVGLHSCF---------QTESRLFFVIEYvngGDLMFHMQRQRKLPEEHARFYSAEISLALNYL 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 132 HDGGLVLRDLKLRKFIFKDEerTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNtsGSYSGKAADVWSLGVMLYT 211
Cdd:cd05618  138 HERGIIYRDLKLDNVLLDSE--GHIKLTDYGMCKEGLRPGDTTSTFCGTPNYIAPEILR--GEDYGFSVDWWALGVLMFE 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 212 MLVGRYPFhDIEPSS----------LFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQ------EILDHPWF-S 274
Cdd:cd05618  214 MMAGRSPF-DIVGSSdnpdqntedyLFQVILEKQIRIPRSLSVKAASVLKSFLNKDPKERLGCHpqtgfaDIQGHPFFrN 292

                        250       260       270
                 ....*....|....*....|....*....|..
gi 568977678 275 TDFSVSNSgfgaKEACDQLVPDVNMEENLDPF 306
Cdd:cd05618  293 VDWDLMEQ----KQVVPPFKPNISGEFGLDNF 320
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
 75-272 6.24e-22

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: 92.71  E-value: 6.24e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFERS-YGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEER 153
Cdd:cd14116   64 HPNILRLYGYFHDATRVYLILEYApLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGE 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 154 TRVKleslEDAYILRGDDDSLSDKHGCPAYVSPEILntSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRR 233
Cdd:cd14116  144 LKIA----DFGWSVHAPSSRRTTLCGTLDYLPPEMI--EGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISR 217

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568977678 234 GQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14116  218 VEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVLEHPW 256
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
 114-273 6.25e-22

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: 92.39  E-value: 6.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 114 EEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEiLNTSG 193
Cdd:cd14069   99 EDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATVFRYKGKERLLNKMCGTLPYVAPE-LLAKK 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 194 SYSGKAADVWSLGVMLYTMLVGRYPFHdiEPS------SLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEI 267
Cdd:cd14069  178 KYRAEPVDVWSCGIVLFAMLAGELPWD--QPSdscqeySDWKENKKTYLTPWKKIDTAALSLLRKILTENPNKRITIEDI 255


                 ....*.
gi 568977678 268 LDHPWF 273
Cdd:cd14069  256 KKHPWY 261
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
 110-272 6.96e-22

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: 93.16  E-value: 6.96e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 110 KKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERT--RVKLESLEDAYILRGDDDSLSDKHGCPAYVSPE 187
Cdd:cd14178   92 KCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESGNpeSIRICDFGFAKQLRAENGLLMTPCYTANFVAPE 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 188 ILNTSGsYSGkAADVWSLGVMLYTMLVGRYPFH---DIEPSSLFSKIRRGQFNIP----ETLSPKAKCLIRSILRREPSE 260
Cdd:cd14178  172 VLKRQG-YDA-ACDIWSLGILLYTMLAGFTPFAngpDDTPEEILARIGSGKYALSggnwDSISDAAKDIVSKMLHVDPHQ 249

                        170
                 ....*....|..
gi 568977678 261 RLTSQEILDHPW 272
Cdd:cd14178  250 RLTAPQVLRHPW 261
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
 75-272 7.86e-22

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: 92.40  E-value: 7.86e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFERSYG-DMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDeeR 153
Cdd:cd14088   58 HPNILQLVDVFETRKEYFIFLELATGrEVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYN--R 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 154 TRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSgsYSGKAADVWSLGVMLYTMLVGRYPFHD--------IEPS 225
Cdd:cd14088  136 LKNSKIVISDFHLAKLENGLIKEPCGTPEYLAPEVVGRQ--RYGRPVDCWAIGVIMYILLSGNPPFYDeaeeddyeNHDK 213

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568977678 226 SLFSKIRRG--QFNIP--ETLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14088  214 NLFRKILAGdyEFDSPywDDISQAAKDLVTRLMEVEQDQRITAEEAISHEW 264
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
 115-275 8.82e-22

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: 93.19  E-value: 8.82e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 115 EEAARlFY--QIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDAYILRGDddSLSDKHGCPAYVSPEILNTS 192
Cdd:cd05571   94 EDRTR-FYgaEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGA--TTKTFCGTPEYLAPEVLEDN 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 193 gSYsGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTS-----QEI 267
Cdd:cd05571  171 -DY-GRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPSTLSPEAKSLLAGLLKKDPKKRLGGgprdaKEI 248


                 ....*...
gi 568977678 268 LDHPWFST 275
Cdd:cd05571  249 MEHPFFAS 256
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
 100-272 1.14e-21

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: 91.97  E-value: 1.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFV--RTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRV---------KLESLEDAyilr 168
Cdd:cd14172   86 GELFSRIqeRGDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKDAVlkltdfgfaKETTVQNA---- 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 169 gdddsLSDKHGCPAYVSPEILNTSgSYSgKAADVWSLGVMLYTMLVGRYPFHD-----IEPSsLFSKIRRGQFNIPE--- 240
Cdd:cd14172  162 -----LQTPCYTPYYVAPEVLGPE-KYD-KSCDMWSLGVIMYILLCGFPPFYSntgqaISPG-MKRRIRMGQYGFPNpew 233

                        170       180       190
                 ....*....|....*....|....*....|...
gi 568977678 241 -TLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14172  234 aEVSEEAKQLIRHLLKTDPTERMTITQFMNHPW 266
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
 114-278 1.32e-21

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: 93.12  E-value: 1.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 114 EEEAARlFY--QIASAVAHCHDGGLVLRDLK------------------LRKFIFKDEERTRVKLESLEDAYILRGDDDS 173
Cdd:cd05573   99 PEETAR-FYiaELVLALDSLHKLGFIHRDIKpdnilldadghikladfgLCTKMNKSGDRESYLNDSVNTLFQDNVLARR 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 174 LSDKH---------GCPAYVSPEILntSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQ--FNIP--E 240
Cdd:cd05573  178 RPHKQrrvraysavGTPDYIAPEVL--RGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVETYSKIMNWKesLVFPddP 255

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568977678 241 TLSPKAKCLIRSILrREPSERLTS-QEILDHPWFS-TDFS 278
Cdd:cd05573  256 DVSPEAIDLIRRLL-CDPEDRLGSaEEIKAHPFFKgIDWE 294
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 28-273 1.70e-21

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: 92.24  E-value: 1.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  28 GETEREQARRARtHTRTHSRARSEIPGHVFEISCYQESLAPCFClSAHSNINQITEILLGETKAYVFFER-SYGDMHSFV 106
Cdd:cd14180   15 GEGSFSVCRKCR-HRQSGQEYAVKIISRRMEANTQREVAALRLC-QSHPNIVALHEVLHDQYHTYLVMELlRGGELLDRI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 107 RTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDE-ERTRVKLESLEDAYILRGDDDSLSDKHGCPAYVS 185
Cdd:cd14180   93 KKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADEsDGAVLKVIDFGFARLRPQGSRPLQTPCFTLQYAA 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 186 PEILNTSGsYSgKAADVWSLGVMLYTMLVGRYPFHDIE-------PSSLFSKIRRGQFNIP----ETLSPKAKCLIRSIL 254
Cdd:cd14180  173 PELFSNQG-YD-ESCDLWSLGVILYTMLSGQVPFQSKRgkmfhnhAADIMHKIKEGDFSLEgeawKGVSEEAKDLVRGLL 250

                        250
                 ....*....|....*....
gi 568977678 255 RREPSERLTSQEILDHPWF 273
Cdd:cd14180  251 TVDPAKRLKLSELRESDWL 269
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
 74-272 1.96e-21

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: 91.16  E-value: 1.96e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  74 AHSNINQITEILLGETKAYVFFER-SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFK--D 150
Cdd:cd14185   56 SHPNIVKLFEVYETEKEIYLILEYvRGGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQhnP 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 151 EERTRVKLESLEDAYILRGDDDSLSdkhGCPAYVSPEILNTSGsySGKAADVWSLGVMLYTMLVGRYPFH--DIEPSSLF 228
Cdd:cd14185  136 DKSTTLKLADFGLAKYVTGPIFTVC---GTPTYVAPEILSEKG--YGLEVDMWAAGVILYILLCGFPPFRspERDQEELF 210

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 568977678 229 SKIRRGQFN-IP---ETLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14185  211 QIIQLGHYEfLPpywDNISEAAKDLISRLLVVDPEKRYTAKQVLQHPW 258
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
 75-273 3.40e-21

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: 90.43  E-value: 3.40e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEIL-LGETKAYVFFERSY-GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEE 152
Cdd:cd14163   59 HKNIIHVYEMLeSADGKIYLVMELAEdGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGFT 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 153 rtrVKLESLEDAYILRGDDDSLSDKH-GCPAYVSPEILNTSgSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKI 231
Cdd:cd14163  139 ---LKLTDFGFAKQLPKGGRELSQTFcGSTAYAAPEVLQGV-PHDSRKGDIWSMGVVLYVMLCAQLPFDDTDIPKMLCQQ 214

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 568977678 232 RRGqFNIPETLSPKAKC--LIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd14163  215 QKG-VSLPGHLGVSRTCqdLLKRLLEPDMVLRPSIEEVSWHPWL 257
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
 112-273 3.60e-21

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: 90.49  E-value: 3.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 112 LREEEAARLFYQIASAVAHCHDGGLVLRDLKLR------KFIFKDeertrVKLESLEDAYILrGDDDSLSDKHGCPAYVS 185
Cdd:cd14106  105 LTEADVRRLMRQILEGVQYLHERNIVHLDLKPQnilltsEFPLGD-----IKLCDFGISRVI-GEGEEIREILGTPDYVA 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 186 PEILntsgSYS--GKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETL----SPKAKCLIRSILRREPS 259
Cdd:cd14106  179 PEIL----SYEpiSLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPEELfkdvSPLAIDFIKRLLVKDPE 254

                        170
                 ....*....|....
gi 568977678 260 ERLTSQEILDHPWF 273
Cdd:cd14106  255 KRLTAKECLEHPWL 268
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
100-269 3.68e-21

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 93.15  E-value: 3.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLK-----LRkfifkdeERTRVKL-----------ESLED 163
Cdd:COG0515   92 ESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKpanilLT-------PDGRVKLidfgiaralggATLTQ 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 164 AYILRGDddslsdkhgcPAYVSPEILntSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQF------- 236
Cdd:COG0515  165 TGTVVGT----------PGYMAPEQA--RGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPpppselr 232

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568977678 237 -NIPETLSPkakcLIRSILRREPSERLTS-QEILD 269
Cdd:COG0515  233 pDLPPALDA----IVLRALAKDPEERYQSaAELAA 263
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
 75-273 4.79e-21

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: 89.98  E-value: 4.79e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNInqITEILLGETKAYVFFERSYGDMHSFVRTCKK---LREEEAARLFYQIASAVAHCHDGGLVLRDLK----LrkfI 147
Cdd:cd06627   58 HPNI--VKYIGSVKTKDSLYIILEYVENGSLASIIKKfgkFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKganiL---T 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 148 FKDEErtrVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSGSYSgkAADVWSLGVMLYTMLVGRYPFHDIEP-SS 226
Cdd:cd06627  133 TKDGL---VKLADFGVATKLNEVEKDENSVVGTPYWMAPEVIEMSGVTT--ASDIWSVGCTVIELLTGNPPYYDLQPmAA 207

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 568977678 227 LFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd06627  208 LFRIVQDDHPPLPENISPELRDFLLQCFQKDPTLRPSAKELLKHPWL 254
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
 100-271 5.19e-21

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: 89.78  E-value: 5.19e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRT--CKKLREEEAARLFYQIASAVAHCHDGGLVLRDLK-LRKFIFKDEErtrVKLESLEDAYILRGDDDSLSD 176
Cdd:cd08529   84 GDLHSLIKSqrGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKsMNIFLDKGDN---VKIGDLGVAKILSDTTNFAQT 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 177 KHGCPAYVSPEiLNTSGSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFN-IPETLSPKAKCLIRSILR 255
Cdd:cd08529  161 IVGTPYYLSPE-LCEDKPYNEKS-DVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYPpISASYSQDLSQLIDSCLT 238

                        170
                 ....*....|....*.
gi 568977678 256 REPSERLTSQEILDHP 271
Cdd:cd08529  239 KDYRQRPDTTELLRNP 254
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
 100-274 8.16e-21

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 90.65  E-value: 8.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCKKLREEEAArlFY--QIASAVAHCHDGGLVLRDLKLRKFIFkdEERTRVKLESLEDAYILRGDDDSLSdk 177
Cdd:PTZ00263 103 GELFTHLRKAGRFPNDVAK--FYhaELVLAFEYLHSKDIIYRDLKPENLLL--DNKGHVKVTDFGFAKKVPDRTFTLC-- 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 178 hGCPAYVSPEILNTSGSysGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRRE 257
Cdd:PTZ00263 177 -GTPEYLAPEVIQSKGH--GKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGLLQTD 253

                        170       180
                 ....*....|....*....|..
gi 568977678 258 PSERLTS-----QEILDHPWFS 274
Cdd:PTZ00263 254 HTKRLGTlkggvADVKNHPYFH 275
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
 100-275 8.19e-21

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: 90.19  E-value: 8.19e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCKKLREEEAarLFY--QIASAVAHCHDGGLVLRDLKLRKFIFKDEerTRVKLESLEDAYILRGDDDSLSdk 177
Cdd:cd05612   86 GELFSYLRNSGRFSNSTG--LFYasEIVCALEYLHSKEIVYRDLKPENILLDKE--GHIKLTDFGFAKKLRDRTWTLC-- 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 178 hGCPAYVSPEILNTSGSysGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRRE 257
Cdd:cd05612  160 -GTPEYLAPEVIQSKGH--NKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFPRHLDLYAKDLIKKLLVVD 236

                        170       180
                 ....*....|....*....|...
gi 568977678 258 PSERL-----TSQEILDHPWFST 275
Cdd:cd05612  237 RTRRLgnmknGADDVKNHRWFKS 259
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
 72-273 8.71e-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: 8.71e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  72 LSAHSNInqITEILLGETKAYVF--FE-RSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIF 148
Cdd:cd14181   72 VSGHPSI--ITLIDSYESSTFIFlvFDlMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILL 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 149 KDEerTRVKLESLEDAYILrGDDDSLSDKHGCPAYVSPEILNTSGSYS----GKAADVWSLGVMLYTMLVGRYPFHDIEP 224
Cdd:cd14181  150 DDQ--LHIKLSDFGFSCHL-EPGEKLRELCGTPGYLAPEILKCSMDEThpgyGKEVDLWACGVILFTLLAGSPPFWHRRQ 226

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568977678 225 SSLFSKIRRG--QFNIPE--TLSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd14181  227 MLMLRMIMEGryQFSSPEwdDRSSTVKDLISRLLVVDPEIRLTAEQALQHPFF 279
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
 100-275 1.08e-20

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: 90.15  E-value: 1.08e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMhsFVRTCKKLREEEAARLFY--QIASAVAHCHDGGLVLRDLKLRKfIFKDEErTRVKL-------ESLED---AYIL 167
Cdd:cd05582   82 GDL--FTRLSKEVMFTEEDVKFYlaELALALDHLHSLGIIYRDLKPEN-ILLDED-GHIKLtdfglskESIDHekkAYSF 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 168 RGDDDslsdkhgcpaYVSPEILNTSGSysGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAK 247
Cdd:cd05582  158 CGTVE----------YMAPEVVNRRGH--TQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMPQFLSPEAQ 225

                        170       180       190
                 ....*....|....*....|....*....|...
gi 568977678 248 CLIRSILRREPSERLTS-----QEILDHPWFST 275
Cdd:cd05582  226 SLLRALFKRNPANRLGAgpdgvEEIKRHPFFAT 258
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
 75-272 1.26e-20

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: 88.94  E-value: 1.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFER-SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFI---FKD 150
Cdd:cd14184   58 HPNIIMLIEEMDTPAELYLVMELvKGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLvceYPD 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 151 EERTrVKLESLEDAYILRGdddSLSDKHGCPAYVSPEILNTSGsySGKAADVWSLGVMLYTMLVGRYPFHDIE--PSSLF 228
Cdd:cd14184  138 GTKS-LKLGDFGLATVVEG---PLYTVCGTPTYVAPEIIAETG--YGLKVDIWAAGVITYILLCGFPPFRSENnlQEDLF 211

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 568977678 229 SKIRRGQFNIP----ETLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14184  212 DQILLGKLEFPspywDNITDSAKELISHMLQVNVEARYTAEQILSHPW 259
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
 100-277 1.28e-20

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: 89.39  E-value: 1.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCKKLREEEAArlFY--QIASAVAHCHDGGLVLRDLKLRKFIFkdEERTRVKLESLEDAYILRGDDDSLSdk 177
Cdd:cd14209   86 GEMFSHLRRIGRFSEPHAR--FYaaQIVLAFEYLHSLDLIYRDLKPENLLI--DQQGYIKVTDFGFAKRVKGRTWTLC-- 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 178 hGCPAYVSPEILNTSGsYsGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRRE 257
Cdd:cd14209  160 -GTPEYLAPEIILSKG-Y-NKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVD 236

                        170       180
                 ....*....|....*....|....*.
gi 568977678 258 PSERL-----TSQEILDHPWF-STDF 277
Cdd:cd14209  237 LTKRFgnlknGVNDIKNHKWFaTTDW 262
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
 110-274 2.83e-20

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: 89.37  E-value: 2.83e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 110 KKLREEEAARLF-YQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDAYILrgDDDSLSDKHGCPAYVSPEI 188
Cdd:cd05593  109 ERVFSEDRTRFYgAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGIT--DAATMKTFCGTPEYLAPEV 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 189 LNTSGSysGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERL-----T 263
Cdd:cd05593  187 LEDNDY--GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSADAKSLLSGLLIKDPNKRLgggpdD 264

                        170
                 ....*....|.
gi 568977678 264 SQEILDHPWFS 274
Cdd:cd05593  265 AKEIMRHSFFT 275
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
 57-272 4.09e-20

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: 87.38  E-value: 4.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  57 FEISCYqeslapcfcLSAHSNINQITEILLGETKAYVFFER--SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDG 134
Cdd:cd13987   40 YNISLE---------LSVHPHIIKTYDVAFETEDYYVFAQEyaPYGDLFSIIPPQVGLPEERVKRCAAQLASALDFMHSK 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 135 GLVLRDLKLRKFIFKDEERTRVKLEsledayilrgdDDSLSDKHGCPA--------YVSPEILNTS--GSYS-GKAADVW 203
Cdd:cd13987  111 NLVHRDIKPENVLLFDKDCRRVKLC-----------DFGLTRRVGSTVkrvsgtipYTAPEVCEAKknEGFVvDPSIDVW 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 204 SLGVMLYTMLVGRYPF----HDIEPSSLFSKIRRGQFNIP----ETLSPKAKCLIRSILRREPSERLTSQEI---LDHPW 272
Cdd:cd13987  180 AFGVLLFCCLTGNFPWekadSDDQFYEEFVRWQKRKNTAVpsqwRRFTPKALRMFKKLLAPEPERRCSIKEVfkyLGDRW 259
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
 115-273 4.53e-20

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: 87.31  E-value: 4.53e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 115 EEAARLFY-QIASAVAHCHDGGLVLRDLKLRKFIFkdEERTRVKLESLEDAYILRgDDDSLSDKHGCPAYVSPEILNTSG 193
Cdd:cd05578   99 EETVKFYIcEIVLALDYLHSKNIIHRDIKPDNILL--DEQGHVHITDFNIATKLT-DGTLATSTSGTKPYMAPEVFMRAG 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 194 SysGKAADVWSLGVMLYTMLVGRYPFHdIEPSSLFSKIRRGQFN----IPETLSPKAKCLIRSILRREPSERL-TSQEIL 268
Cdd:cd05578  176 Y--SFAVDWWSLGVTAYEMLRGKRPYE-IHSRTSIEEIRAKFETasvlYPAGWSEEAIDLINKLLERDPQKRLgDLSDLK 252


                 ....*
gi 568977678 269 DHPWF 273
Cdd:cd05578  253 NHPYF 257
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
 115-275 4.95e-20

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: 88.93  E-value: 4.95e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 115 EEAARLF-YQIASAVAHCH-DGGLVLRDLKLRKFIFKDEERTRVKLESLEDAYIlrGDDDSLSDKHGCPAYVSPEILNTS 192
Cdd:cd05594  124 EDRARFYgAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGI--KDGATMKTFCGTPEYLAPEVLEDN 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 193 GSysGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERL-----TSQEI 267
Cdd:cd05594  202 DY--GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLSPEAKSLLSGLLKKDPKQRLgggpdDAKEI 279


                 ....*...
gi 568977678 268 LDHPWFST 275
Cdd:cd05594  280 MQHKFFAG 287
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
 100-274 6.39e-20

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: 88.14  E-value: 6.39e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCKKLREEEAARlFY--QIASAVAHCHDGGLVLRDLKLRKfIFKDeeRT-RVKLESLEDAYILRGDDDSLSD 176
Cdd:cd05601   86 GDLLSLLSRYDDIFEESMAR-FYlaELVLAIHSLHSMGYVHRDIKPEN-ILID--RTgHIKLADFGSAAKLSSDKTVTSK 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 177 KH-GCPAYVSPEIL----NTSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQ--FNIPE--TLSPKAK 247
Cdd:cd05601  162 MPvGTPDYIAPEVLtsmnGGSKGTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMNFKkfLKFPEdpKVSESAV 241

                        170       180
                 ....*....|....*....|....*..
gi 568977678 248 CLIRSILrREPSERLTSQEILDHPWFS 274
Cdd:cd05601  242 DLIKGLL-TDAKERLGYEGLCCHPFFS 267
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
 75-272 6.97e-20

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: 87.32  E-value: 6.97e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFER-SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEE- 152
Cdd:cd14196   67 HPNIITLHDVYENRTDVVLILELvSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNi 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 153 -RTRVKLESLEDAYILRgDDDSLSDKHGCPAYVSPEILNtsgsYS--GKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFS 229
Cdd:cd14196  147 pIPHIKLIDFGLAHEIE-DGVEFKNIFGTPEFVAPEIVN----YEplGLEADMWSIGVITYILLSGASPFLGDTKQETLA 221

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 568977678 230 KIRRGQFNIPETL----SPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14196  222 NITAVSYDFDEEFfshtSELAKDFIRKLLVKETRKRLTIQEALRHPW 268
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
 114-279 7.05e-20

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: 87.78  E-value: 7.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 114 EEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRV-KLESLEDAYILRgDDDSLSDKHGCPAYVSPEILNTS 192
Cdd:cd14170  100 EREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAIlKLTDFGFAKETT-SHNSLTTPCYTPYYVAPEVLGPE 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 193 gSYSgKAADVWSLGVMLYTMLVGRYPFHD-----IEPSsLFSKIRRGQFNIPET----LSPKAKCLIRSILRREPSERLT 263
Cdd:cd14170  179 -KYD-KSCDMWSLGVIMYILLCGYPPFYSnhglaISPG-MKTRIRMGQYEFPNPewseVSEEVKMLIRNLLKTEPTQRMT 255

                        170
                 ....*....|....*.
gi 568977678 264 SQEILDHPWFSTDFSV 279
Cdd:cd14170  256 ITEFMNHPWIMQSTKV 271
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
 110-269 1.01e-19

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: 86.62  E-value: 1.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 110 KKLREEEAARLFYQIASAVAHCHDGG--LVLRDLKLRKFIFKDEerTRVKL-------------ESLEDayilRGDDDSL 174
Cdd:cd13985   98 SPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNT--GRFKLcdfgsattehyplERAEE----VNIIEEE 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 175 SDKHGCPAYVSPEILNTSGSYS-GKAADVWSLGVMLYTMLVGRYPFhdiEPSSLFsKIRRGQFNIPET--LSPKAKCLIR 251
Cdd:cd13985  172 IQKNTTPMYRAPEMIDLYSKKPiGEKADIWALGCLLYKLCFFKLPF---DESSKL-AIVAGKYSIPEQprYSPELHDLIR 247

                        170
                 ....*....|....*...
gi 568977678 252 SILRREPSERLTSQEILD 269
Cdd:cd13985  248 HMLTPDPAERPDIFQVIN 265
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
 123-272 1.02e-19

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: 87.21  E-value: 1.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 123 QIASAVAHCHDGGLVLRDLKLRKFIFKDEERTR-VKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILnTSGSYsGKAAD 201
Cdd:cd14094  117 QILEALRYCHDNNIIHRDVKPHCVLLASKENSApVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVV-KREPY-GKPVD 194

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568977678 202 VWSLGVMLYTMLVGRYPFHDIEpSSLFSKIRRGQFNIP----ETLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14094  195 VWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMNprqwSHISESAKDLVRRMLMLDPAERITVYEALNHPW 268
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
 88-275 1.42e-19

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: 87.31  E-value: 1.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  88 ETKAYVFFERSY---GDMHSFVRtcKKLREEEAARLFY--QIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESL- 161
Cdd:cd05620   66 QTKEHLFFVMEFlngGDLMFHIQ--DKGRFDLYRATFYaaEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMc 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 162 -EDAYilrgDDDSLSDKHGCPAYVSPEILNtsGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPE 240
Cdd:cd05620  144 kENVF----GDNRASTFCGTPDYIAPEILQ--GLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPR 217

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 568977678 241 TLSPKAKCLIRSILRREPSERL-TSQEILDHPWFST 275
Cdd:cd05620  218 WITKESKDILEKLFERDPTRRLgVVGNIRGHPFFKT 253
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
 88-273 1.64e-19

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: 87.06  E-value: 1.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  88 ETKAYVFFERSY---GDMHSFVRTCKKLREEEAArlFY--QIASAVAHCHDGGLVLRDLKLrkfifkdeerTRVKLESle 162
Cdd:cd05587   67 QTMDRLYFVMEYvngGDLMYHIQQVGKFKEPVAV--FYaaEIAVGLFFLHSKGIIYRDLKL----------DNVMLDA-- 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 163 DAYILRGD-----DDSLSDKH-----GCPAYVSPEILntSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIR 232
Cdd:cd05587  133 EGHIKIADfgmckEGIFGGKTtrtfcGTPDYIAPEII--AYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIM 210

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568977678 233 RGQFNIPETLSPKAKCLIRSILRREPSERL-----TSQEILDHPWF 273
Cdd:cd05587  211 EHNVSYPKSLSKEAVSICKGLLTKHPAKRLgcgptGERDIKEHPFF 256
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
 75-273 2.49e-19

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: 85.26  E-value: 2.49e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFER--SYGDMHS--FVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKD 150
Cdd:cd14109   55 HPNIVQMHDAYDDEKLAVTVIDNlaSTIELVRdnLLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQD 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 151 EertRVKLESLEDAYILRGDDDSLSDKhGCPAYVSPEILNTSGSysGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSK 230
Cdd:cd14109  135 D---KLKLADFGQSRRLLRGKLTTLIY-GSPEFVSPEIVNSYPV--TLATDMWSVGVLTYVLLGGISPFLGDNDRETLTN 208

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 568977678 231 IRRGQFNIPET----LSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd14109  209 VRSGKWSFDSSplgnISDDARDFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
 75-271 3.50e-19

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: 84.75  E-value: 3.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFERS-YGDMHSFVRTCKKLR----EEEAARLFYQIASAVAHCHDGGLVLRDLKLRK-FIF 148
Cdd:cd08530   58 HPNIIRYKEAFLDGNRLCIVMEYApFGDLSKLISKRKKKRrlfpEDDIWRIFIQMLRGLKALHDQKILHRDLKSANiLLS 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 149 KDEErtrVKLESLEDAYILRGDddSLSDKHGCPAYVSPEILNtSGSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPSSLF 228
Cdd:cd08530  138 AGDL---VKIGDLGISKVLKKN--LAKTQIGTPLYAAPEVWK-GRPYDYKS-DIWSLGCLLYEMATFRPPFEARTMQELR 210

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 568977678 229 SKIRRGQFN-IPETLSPKAKCLIRSILRREPSERLTSQEILDHP 271
Cdd:cd08530  211 YKVCRGKFPpIPPVYSQDLQQIIRSLLQVNPKKRPSCDKLLQSP 254
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
 115-274 7.98e-19

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: 84.20  E-value: 7.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 115 EEAARlFY--QIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRV-------KLESLEDAYILRGDddslsdkhgcPAYVS 185
Cdd:cd05572   92 EYTAR-FYtaCVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLvdfgfakKLGSGRKTWTFCGT----------PEYVA 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 186 PEILNTSGsYsGKAADVWSLGVMLYTMLVGRYPFH--DIEPSSLFSKIRRGQFNI--PETLSPKAKCLIRSILRREPSER 261
Cdd:cd05572  161 PEIILNKG-Y-DFSVDYWSLGILLYELLTGRPPFGgdDEDPMKIYNIILKGIDKIefPKYIDKNAKNLIKQLLRRNPEER 238

                        170
                 ....*....|....*...
gi 568977678 262 LTSQ-----EILDHPWFS 274
Cdd:cd05572  239 LGYLkggirDIKKHKWFE 256
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
 75-272 9.30e-19

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: 84.28  E-value: 9.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFER-SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEE- 152
Cdd:cd14195   67 HPNIITLHDIFENKTDVVLILELvSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNv 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 153 -RTRVKLESLEDAYILRGDDDsLSDKHGCPAYVSPEILNTSGSysGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKI 231
Cdd:cd14195  147 pNPRIKLIDFGIAHKIEAGNE-FKNIFGTPEFVAPEIVNYEPL--GLEADMWSIGVITYILLSGASPFLGETKQETLTNI 223

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 568977678 232 RRGQFNIPE----TLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14195  224 SAVNYDFDEeyfsNTSELAKDFIRRLLVKDPKKRMTIAQSLEHSW 268
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
 55-307 9.60e-19

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


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 84.78  E-value: 9.60e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  55 HVFEiscyQESLAPcFCLSAHSNInqiteillgETKAYVFFERSY---GDMHSFVRTCKKLREEEAArlFY--QIASAVA 129
Cdd:cd05588   47 HVFE----TASNHP-FLVGLHSCF---------QTESRLFFVIEFvngGDLMFHMQRQRRLPEEHAR--FYsaEISLALN 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 130 HCHDGGLVLRDLKLRKFIFKDEerTRVKL-------ESLEDAyilrgddDSLSDKHGCPAYVSPEILNtsGSYSGKAADV 202
Cdd:cd05588  111 FLHEKGIIYRDLKLDNVLLDSE--GHIKLtdygmckEGLRPG-------DTTSTFCGTPNYIAPEILR--GEDYGFSVDW 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 203 WSLGVMLYTMLVGRYPFhDIEPSS----------LFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQ------E 266
Cdd:cd05588  180 WALGVLMFEMLAGRSPF-DIVGSSdnpdqntedyLFQVILEKPIRIPRSLSVKAASVLKGFLNKNPAERLGCHpqtgfaD 258

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 568977678 267 ILDHPWFSTdfsVSNSGFGAKEACDQLVPDVNME---ENLDPFF 307
Cdd:cd05588  259 IQSHPFFRT---IDWEQLEQKQVTPPYKPRIESErdlENFDPQF 299
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
 115-271 1.06e-18

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: 83.57  E-value: 1.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 115 EEAARLFY-QIASAVAHCHDGGLVLRDLKLRKFIFKDEERT-------RVKLESLEDAYILRGDDDSLSdKHGCPAYVSP 186
Cdd:cd14120   91 EDTIRVFLqQIAAAMKALHSKGIVHRDLKPQNILLSHNSGRkpspndiRLKIADFGFARFLQDGMMAAT-LCGSPMYMAP 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 187 EILnTSGSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPSSL---FSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLT 263
Cdd:cd14120  170 EVI-MSLQYDAKA-DLWSIGTIVYQCLTGKAPFQAQTPQELkafYEKNANLRPNIPSGTSPALKDLLLGLLKRNPKDRID 247


                 ....*...
gi 568977678 264 SQEILDHP 271
Cdd:cd14120  248 FEDFFSHP 255
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
 29-273 1.11e-18

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: 83.83  E-value: 1.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  29 ETEREQARRARTHTRTHSRARSEIpghVFEISCYQESLAPCFCLSAHSNINQITEILL-------GEtkayvFFERSYGD 101
Cdd:cd14197   32 DSGKEFAAKFMRKRRKGQDCRMEI---IHEIAVLELAQANPWVINLHEVYETASEMILvleyaagGE-----IFNQCVAD 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 102 MHsfvrtcKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERT-RVKLESLEDAYILRGDDDsLSDKHGC 180
Cdd:cd14197  104 RE------EAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPLgDIKIVDFGLSRILKNSEE-LREIMGT 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 181 PAYVSPEILntsgSYS--GKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIrrGQFNIP------ETLSPKAKCLIRS 252
Cdd:cd14197  177 PEYVAPEIL----SYEpiSTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNI--SQMNVSyseeefEHLSESAIDFIKT 250

                        250       260
                 ....*....|....*....|.
gi 568977678 253 ILRREPSERLTSQEILDHPWF 273
Cdd:cd14197  251 LLIKKPENRATAEDCLKHPWL 271
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
 75-272 1.13e-18

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: 83.92  E-value: 1.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFER-SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEE- 152
Cdd:cd14194   67 HPNVITLHEVYENKTDVILILELvAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNv 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 153 -RTRVKLESLEDAYILRGDDDsLSDKHGCPAYVSPEILNtsgsYS--GKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFS 229
Cdd:cd14194  147 pKPRIKIIDFGLAHKIDFGNE-FKNIFGTPEFVAPEIVN----YEplGLEADMWSIGVITYILLSGASPFLGDTKQETLA 221

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 568977678 230 KIRRGQFNIPETL----SPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14194  222 NVSAVNYEFEDEYfsntSALAKDFIRRLLVKDPKKRMTIQDSLQHPW 268
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
 88-307 1.74e-18

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: 84.19  E-value: 1.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  88 ETKAYVFFERSY---GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDA 164
Cdd:cd05590   66 QTPDRLFFVMEFvngGDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKE 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 165 YILRGDddSLSDKHGCPAYVSPEILNTSgsYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSP 244
Cdd:cd05590  146 GIFNGK--TTSTFCGTPDYIAPEILQEM--LYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLSQ 221

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568977678 245 KAKCLIRSILRREPSERLTS------QEILDHPWFS-TDFSVSNSgfgaKEACDQLVPDVNMEE---NLDPFF 307
Cdd:cd05590  222 DAVDILKAFMTKNPTMRLGSltlggeEAILRHPFFKeLDWEKLNR----RQIEPPFRPRIKSREdvsNFDPDF 290
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
 100-275 2.60e-18

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: 82.96  E-value: 2.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCKKLREEEAARLFY--QIASAVAHCHDGGLVLRDLKLRKFIFKDEerTRVKLESLEDAYILRGDDdSLSDK 177
Cdd:cd05577   78 GDLKYHIYNVGTRGFSEARAIFYaaEIICGLEHLHNRFIVYRDLKPENILLDDH--GHVRISDLGLAVEFKGGK-KIKGR 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 178 HGCPAYVSPEILNTSGSYSgKAADVWSLGVMLYTMLVGRYPFHD----IEPSSLFSKIRRGQFNIPETLSPKAKCLIRSI 253
Cdd:cd05577  155 VGTHGYMAPEVLQKEVAYD-FSVDWFALGCMLYEMIAGRSPFRQrkekVDKEELKRRTLEMAVEYPDSFSPEARSLCEGL 233

                        170       180
                 ....*....|....*....|....*..
gi 568977678 254 LRREPSERL-----TSQEILDHPWFST 275
Cdd:cd05577  234 LQKDPERRLgcrggSADEVKEHPFFRS 260
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
 72-273 2.69e-18

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: 83.04  E-value: 2.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  72 LSAHSNINQITEILlgETKAY---VFFERSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIF 148
Cdd:cd14182   66 VSGHPNIIQLKDTY--ETNTFfflVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILL 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 149 KDEerTRVKLESLEDAYILrGDDDSLSDKHGCPAYVSPEILNTSGSYS----GKAADVWSLGVMLYTMLVGRYPFHDIEP 224
Cdd:cd14182  144 DDD--MNIKLTDFGFSCQL-DPGEKLREVCGTPGYLAPEIIECSMDDNhpgyGKEVDMWSTGVIMYTLLAGSPPFWHRKQ 220

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568977678 225 SSLFSKIRRG--QFNIPE--TLSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd14182  221 MLMLRMIMSGnyQFGSPEwdDRSDTVKDLISRFLVVQPQKRYTAEEALAHPFF 273
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
 55-275 4.38e-18

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


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 83.53  E-value: 4.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  55 HVFEiscyQESLAPcFCLSAHSNInqiteillgETKAYVFFERSY---GDMHSFVRTCKKLREEEAARLFYQIASAVAHC 131
Cdd:cd05617   67 HVFE----QASSNP-FLVGLHSCF---------QTTSRLFLVIEYvngGDLMFHMQRQRKLPEEHARFYAAEICIALNFL 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 132 HDGGLVLRDLKLRKFIFkdEERTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNtsGSYSGKAADVWSLGVMLYT 211
Cdd:cd05617  133 HERGIIYRDLKLDNVLL--DADGHIKLTDYGMCKEGLGPGDTTSTFCGTPNYIAPEILR--GEEYGFSVDWWALGVLMFE 208

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568977678 212 MLVGRYPFHDIEPSS-------LFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQ------EILDHPWFST 275
Cdd:cd05617  209 MMAGRSPFDIITDNPdmntedyLFQVILEKPIRIPRFLSVKASHVLKGFLNKDPKERLGCQpqtgfsDIKSHTFFRS 285
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
 114-272 4.72e-18

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 83.33  E-value: 4.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 114 EEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFkdEERTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTS- 192
Cdd:PLN00034 167 EQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLI--NSAKNVKIADFGVSRILAQTMDPCNSSVGTIAYMSPERINTDl 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 193 --GSYSGKAADVWSLGVMLYTMLVGRYPF---HDIEPSSLFSKIRRGQF-NIPETLSPKAKCLIRSILRREPSERLTSQE 266
Cdd:PLN00034 245 nhGAYDGYAGDIWSLGVSILEFYLGRFPFgvgRQGDWASLMCAICMSQPpEAPATASREFRHFISCCLQREPAKRWSAMQ 324


                 ....*.
gi 568977678 267 ILDHPW 272
Cdd:PLN00034 325 LLQHPF 330
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
 75-273 5.44e-18

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: 81.98  E-value: 5.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEilLGETKAYVFFERSY---GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFK-- 149
Cdd:cd14202   60 HENIVALYD--FQEIANSVYLVMEYcngGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSys 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 150 -----DEERTRVKLESLEDAYILRGDDDSlSDKHGCPAYVSPEILnTSGSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEP 224
Cdd:cd14202  138 ggrksNPNNIRIKIADFGFARYLQNNMMA-ATLCGSPMYMAPEVI-MSQHYDAKA-DLWSIGTIIYQCLTGKAPFQASSP 214

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568977678 225 SSL---FSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd14202  215 QDLrlfYEKNKSLSPNIPRETSSHLRQLLLGLLQRNQKDRMDFDEFFHHPFL 266
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
 74-273 5.51e-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: 81.51  E-value: 5.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  74 AHSNINQITEI--LLGETKAYVFFERSYGDMHSFVRTCKKLREEEAARLF-YQIASAVAHCHDGGLVLRDLKLRKfIFKD 150
Cdd:cd05118   57 GHPNIVKLLDVfeHRGGNHLCLVFELMGMNLYELIKDYPRGLPLDLIKSYlYQLLQALDFLHSNGIIHRDLKPEN-ILIN 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 151 EERTRVKLESLEDAYILrgdDDSLSDKHGCP-AYVSPEILNTSGSYsGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFS 229
Cdd:cd05118  136 LELGQLKLADFGLARSF---TSPPYTPYVATrWYRAPEVLLGAKPY-GSSIDIWSLGCILAELLTGRPLFPGDSEVDQLA 211

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 568977678 230 KIRRgqfnipeTL-SPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd05118  212 KIVR-------LLgTPEALDLLSKMLKYDPAKRITASQALAHPYF 249
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
 90-272 5.60e-18

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: 81.58  E-value: 5.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  90 KAYVFFER-SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKfIFKDEeRTRVKLESLEDAYILR 168
Cdd:cd06626   73 EVYIFMEYcQEGTLEELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPAN-IFLDS-NGLIKLGDFGSAVKLK 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 169 GDDDSLSDKH-----GCPAYVSPE-ILNTSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIE-PSSLFSKIRRGQF-NIPE 240
Cdd:cd06626  151 NNTTTMAPGEvnslvGTPAYMAPEvITGNKGEGHGRAADIWSLGCVVLEMATGKRPWSELDnEWAIMYHVGMGHKpPIPD 230

                        170       180       190
                 ....*....|....*....|....*....|....
gi 568977678 241 TL--SPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd06626  231 SLqlSPEGKDFLSRCLESDPKKRPTASELLDHPF 264
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 114-274 8.95e-18

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: 81.29  E-value: 8.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 114 EEEAARLFY-QIASAVAHCHDGGLVLRDLKLRKfIFKDEErTRVKLE----SLEdayILRGDDDSLSDKHGCPAYVSPEI 188
Cdd:cd05583   97 TESEVRIYIgEIVLALEHLHKLGIIYRDIKLEN-ILLDSE-GHVVLTdfglSKE---FLPGENDRAYSFCGTIEYMAPEV 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 189 LNTSGSYSGKAADVWSLGVMLYTMLVGRYPF----HDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTS 264
Cdd:cd05583  172 VRGGSDGHDKAVDWWSLGVLTYELLTGASPFtvdgERNSQSEISKRILKSHPPIPKTFSAEAKDFILKLLEKDPKKRLGA 251

                        170
                 ....*....|....*
gi 568977678 265 -----QEILDHPWFS 274
Cdd:cd05583  252 gprgaHEIKEHPFFK 266
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
 88-273 8.99e-18

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: 81.30  E-value: 8.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  88 ETKAYVFFERSY---GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLK--------LRKFIFKDEERTRV 156
Cdd:cd05609   70 ETKRHLCMVMEYvegGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKpdnllitsMGHIKLTDFGLSKI 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 157 KLESLE----DAYILRgDDDSLSDKH--GCPAYVSPEILNTSGsYsGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSK 230
Cdd:cd05609  150 GLMSLTtnlyEGHIEK-DTREFLDKQvcGTPEYIAPEVILRQG-Y-GKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQ 226

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568977678 231 IRRGQFNIPE---TLSPKAKCLIRSILRREPSERL---TSQEILDHPWF 273
Cdd:cd05609  227 VISDEIEWPEgddALPDDAQDLITRLLQQNPLERLgtgGAEEVKQHPFF 275
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
 100-272 1.01e-17

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: 81.10  E-value: 1.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCKKLREEEAARLFYQIASAVAHCH-DGGLVLRDLK----LrkfIFKDEErtrVKLEsleDAYILRGDDDSL 174
Cdd:cd06623   84 GSLADLLKKVGKIPEPVLAYIARQILKGLDYLHtKRHIIHRDIKpsnlL---INSKGE---VKIA---DFGISKVLENTL 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 175 SDKH---GCPAYVSPEILNtsGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRR-GQFNIPE----TLSPKA 246
Cdd:cd06623  155 DQCNtfvGTVTYMSPERIQ--GESYSYAADIWSLGLTLLECALGKFPFLPPGQPSFFELMQAiCDGPPPSlpaeEFSPEF 232

                        170       180
                 ....*....|....*....|....*.
gi 568977678 247 KCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd06623  233 RDFISACLQKDPKKRPSAAELLQHPF 258
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
 75-273 1.15e-17

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: 81.21  E-value: 1.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEIllGETKAYVFFERSY---GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDE 151
Cdd:cd14201   64 HENIVALYDV--QEMPNSVFLVMEYcngGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYA 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 152 ER-------TRVKLESLEDAYILRGDDDSlSDKHGCPAYVSPEILnTSGSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEP 224
Cdd:cd14201  142 SRkkssvsgIRIKIADFGFARYLQSNMMA-ATLCGSPMYMAPEVI-MSQHYDAKA-DLWSIGTVIYQCLVGKPPFQANSP 218

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568977678 225 SSL---FSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd14201  219 QDLrmfYEKNKNLQPSIPRETSPYLADLLLGLLQRNQKDRMDFEAFFSHPFL 270
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 75-272 1.78e-17

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: 80.17  E-value: 1.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETkAYVFFERSY---GDMHSFVRTCKK--LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKfIFK 149
Cdd:cd08223   58 HPNIVSYKESFEGED-GFLYIVMGFcegGDLYTRLKEQKGvlLEERQVVEWFVQIAMALQYMHERNILHRDLKTQN-IFL 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 150 DEERTrVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEiLNTSGSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPSSLFS 229
Cdd:cd08223  136 TKSNI-IKVGDLGIARVLESSSDMATTLIGTPYYMSPE-LFSNKPYNHKS-DVWALGCCVYEMATLKHAFNAKDMNSLVY 212

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 568977678 230 KIRRGQF-NIPETLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd08223  213 KILEGKLpPMPKQYSPELGELIKAMLHQDPEKRPSVKRILRQPY 256
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 93-273 2.22e-17

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: 79.78  E-value: 2.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  93 VFFERSY---GDMHS-FVRTCKKLREEE-AARLFYQIASAVAHCHDGGLVLRDLK-LRKFIFKDEertRVKLESLEDAYI 166
Cdd:cd08221   74 LFIEMEYcngGNLHDkIAQQKNQLFPEEvVLWYLYQIVSAVSHIHKAGILHRDIKtLNIFLTKAD---LVKLGDFGISKV 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 167 LRGDDDSLSDKHGCPAYVSPEILNtSGSYSGKaADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQF-NIPETLSPK 245
Cdd:cd08221  151 LDSESSMAESIVGTPYYMSPELVQ-GVKYNFK-SDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQGEYeDIDEQYSEE 228

                        170       180
                 ....*....|....*....|....*...
gi 568977678 246 AKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd08221  229 IIQLVHDCLHQDPEDRPTAEELLERPLL 256
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
 107-271 2.23e-17

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 82.22  E-value: 2.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 107 RTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSP 186
Cdd:PTZ00283 135 KTNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSKMYAATVSDDVGRTFCGTPYYVAP 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 187 EILNTSgSYSgKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFN-IPETLSPKAKCLIRSILRREPSERLTSQ 265
Cdd:PTZ00283 215 EIWRRK-PYS-KKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAGRYDpLPPSISPEMQEIVTALLSSDPKRRPSSS 292


                 ....*.
gi 568977678 266 EILDHP 271
Cdd:PTZ00283 293 KLLNMP 298
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 32-273 2.28e-17

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: 81.12  E-value: 2.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  32 REQARRARTHTRTHSRARSEIPGHVFEiscyqeslAPcFCLSAHSNINqiTEILLGETKAYVfferSYGDMHSFVRTCKK 111
Cdd:cd05614   37 RKAALVQKAKTVEHTRTERNVLEHVRQ--------SP-FLVTLHYAFQ--TDAKLHLILDYV----SGGELFTHLYQRDH 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 112 LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDAYILRGDDDSLSdKHGCPAYVSPEILNT 191
Cdd:cd05614  102 FSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFLTEEKERTYS-FCGTIEYMAPEIIRG 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 192 SGSYsGKAADVWSLGVMLYTMLVGRYPF----HDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTS--- 264
Cdd:cd05614  181 KSGH-GKAVDWWSLGILMFELLTGASPFtlegEKNTQSEVSRRILKCDPPFPSFIGPVARDLLQKLLCKDPKKRLGAgpq 259

                        250
                 ....*....|.
gi 568977678 265 --QEILDHPWF 273
Cdd:cd05614  260 gaQEIKEHPFF 270
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
 72-271 2.56e-17

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: 79.95  E-value: 2.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  72 LSAHSNINQI--TEILLGETKAYVFFERSYGDMHSFV--RTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFI 147
Cdd:cd14131   56 LKGSDRIIQLydYEVTDEDDYLYMVMECGEIDLATILkkKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFL 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 148 FKDeerTRVKLESLEDAYILRGDDDS-LSDKH-GCPAYVSPE-ILNTSGSYS-------GKAADVWSLGVMLYTMLVGRY 217
Cdd:cd14131  136 LVK---GRLKLIDFGIAKAIQNDTTSiVRDSQvGTLNYMSPEaIKDTSASGEgkpkskiGRPSDVWSLGCILYQMVYGKT 212

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568977678 218 PFHDIepSSLFSKIRR---GQFNI--PETLSPKAKCLIRSILRREPSERLTSQEILDHP 271
Cdd:cd14131  213 PFQHI--TNPIAKLQAiidPNHEIefPDIPNPDLIDVMKRCLQRDPKKRPSIPELLNHP 269
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
 100-272 2.70e-17

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: 80.03  E-value: 2.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFkdEERTRVKL----------ESLEDAYILRG 169
Cdd:cd14010   79 GDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILL--DGNGTLKLsdfglarregEILKELFGQFS 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 170 DDDSLSD------KHGCPAYVSPEILnTSGSYSgKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIrrgQFNIPETLS 243
Cdd:cd14010  157 DEGNVNKvskkqaKRGTPYYMAPELF-QGGVHS-FASDLWALGCVLYEMFTGKPPFVAESFTELVEKI---LNEDPPPPP 231

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568977678 244 PKAKC--------LIRSILRREPSERLTSQEILDHP-W 272
Cdd:cd14010  232 PKVSSkpspdfksLLKGLLEKDPAKRLSWDELVKHPfW 269
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
 75-271 2.78e-17

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: 79.60  E-value: 2.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFERSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRK-FIFKDeer 153
Cdd:cd14002   59 HPNIIEMLDSFETKKEFVVVTEYAQGELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNiLIGKG--- 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 154 TRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSgSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRR 233
Cdd:cd14002  136 GVVKLCDFGFARAMSCNTLVLTSIKGTPLYMAPELVQEQ-PYDHTA-DLWSLGCILYELFVGQPPFYTNSIYQLVQMIVK 213

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568977678 234 GQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHP 271
Cdd:cd14002  214 DPVKWPSNMSPEFKSFLQGLLNKDPSKRLSWPDLLEHP 251
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 100-272 3.03e-17

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: 79.77  E-value: 3.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCKKLREEEAARL----FYQIASAVAHCHDGGLVLRDLKLRKFIFKdeeRTRVKLESLEDAYILRGDDDSLS 175
Cdd:cd08222   87 GDLDDKISEYKKSGTTIDENQildwFIQLLLAVQYMHERRILHRDLKAKNIFLK---NNVIKVGDFGISRILMGTSDLAT 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 176 DKHGCPAYVSPEILNTSGsYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQF-NIPETLSPKAKCLIRSIL 254
Cdd:cd08222  164 TFTGTPYYMSPEVLKHEG-YNSKS-DIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETpSLPDKYSKELNAIYSRML 241

                        170
                 ....*....|....*...
gi 568977678 255 RREPSERLTSQEILDHPW 272
Cdd:cd08222  242 NKDPALRPSAAEILKIPF 259
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
 58-273 3.60e-17

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: 79.83  E-value: 3.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  58 EISCYQEslapcfcLSaHSNINQITEILLGETKAYVFFERSYGDMHSFVRTC-KKLREEEAARLFYQIASAVAHCHDGGL 136
Cdd:cd07829   48 EISLLKE-------LK-HPNIVKLLDVIHTENKLYLVFEYCDQDLKKYLDKRpGPLPPNLIKSIMYQLLRGLAYCHSHRI 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 137 VLRDLKLRKfIFKDEERTrVKLEsledayilrgdDDSLSDKHGCPA-----------YVSPEILNTSGSYSgKAADVWSL 205
Cdd:cd07829  120 LHRDLKPQN-LLINRDGV-LKLA-----------DFGLARAFGIPLrtythevvtlwYRAPEILLGSKHYS-TAVDIWSV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 206 GVMLYTMLVGRYPFH-DIEPSSLF-----------------SKIRRGQFNIP-----------ETLSPKAKCLIRSILRR 256
Cdd:cd07829  186 GCIFAELITGKPLFPgDSEIDQLFkifqilgtpteeswpgvTKLPDYKPTFPkwpkndlekvlPRLDPEGIDLLSKMLQY 265

                        250
                 ....*....|....*..
gi 568977678 257 EPSERLTSQEILDHPWF 273
Cdd:cd07829  266 NPAKRISAKEALKHPYF 282
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
 110-268 6.12e-17

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: 78.87  E-value: 6.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 110 KKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKfIFKDEERTRVKL--------------ESLEDAYILRGDDDSLS 175
Cdd:cd13996  102 SKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSN-IFLDNDDLQVKIgdfglatsignqkrELNNLNNNNNGNTSNNS 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 176 DKHGCPAYVSPEILntSGSYSGKAADVWSLGVMLYTMLVGRYPFHdiEPSSLFSKIRRGQFniPETLS---PKAKCLIRS 252
Cdd:cd13996  181 VGIGTPLYASPEQL--DGENYNEKADIYSLGIILFEMLHPFKTAM--ERSTILTDLRNGIL--PESFKakhPKEADLIQS 254

                        170
                 ....*....|....*.
gi 568977678 253 ILRREPSERLTSQEIL 268
Cdd:cd13996  255 LLSKNPEERPSAEQLL 270
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
 88-273 6.71e-17

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: 79.66  E-value: 6.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  88 ETKAYVFFERSY---GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDA 164
Cdd:cd05616   71 QTMDRLYFVMEYvngGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKE 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 165 YILrgddDSLSDKHGC--PAYVSPEILntsgSYS--GKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPE 240
Cdd:cd05616  151 NIW----DGVTTKTFCgtPDYIAPEII----AYQpyGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPK 222

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568977678 241 TLSPKAKCLIRSILRREPSERL-----TSQEILDHPWF 273
Cdd:cd05616  223 SMSKEAVAICKGLMTKHPGKRLgcgpeGERDIKEHAFF 260
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 112-271 7.24e-17

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: 78.62  E-value: 7.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 112 LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKfIFKDEERTRVKLESLedayilrGDDDSLSDKH------GCPAYVS 185
Cdd:cd08220   98 LSEEEILHFFVQILLALHHVHSKQILHRDLKTQN-ILLNKKRTVVKIGDF-------GISKILSSKSkaytvvGTPCYIS 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 186 PEIlnTSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFN-IPETLSPKAKCLIRSILRREPSERLTS 264
Cdd:cd08220  170 PEL--CEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGTFApISDRYSEELRHLILSMLHLDPNKRPTL 247


                 ....*..
gi 568977678 265 QEILDHP 271
Cdd:cd08220  248 SEIMAQP 254
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
 88-274 7.71e-17

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: 79.20  E-value: 7.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  88 ETKAYVFFERSY---GDMHSFVRTCKKLR-EEEAARlFY--QIASAVAHCHDGGLVLRDLK------------------- 142
Cdd:cd05574   71 QTSTHLCFVMDYcpgGELFRLLQKQPGKRlPEEVAR-FYaaEVLLALEYLHLLGFVYRDLKpenillhesghimltdfdl 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 143 ---------LRKFIFKDEERTRVKLESLEDAYILRGDDDSLSDKhGCPAYVSPEILNTSGSysGKAADVWSLGVMLYTML 213
Cdd:cd05574  150 skqssvtppPVRKSLRKGSRRSSVKSIEKETFVAEPSARSNSFV-GTEEYIAPEVIKGDGH--GSAVDWWTLGILLYEML 226

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568977678 214 VGRYPFHDIEPSSLFSKIRRGQFNIPE--TLSPKAKCLIRSILRREPSERLTS----QEILDHPWFS 274
Cdd:cd05574  227 YGTTPFKGSNRDETFSNILKKELTFPEspPVSSEAKDLIRKLLVKDPSKRLGSkrgaSEIKRHPFFR 293
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
 72-269 8.61e-17

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: 78.55  E-value: 8.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  72 LSAHSNINQITEILlgETKAYVFFERSY---GDMHSFVRTCK--KLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKF 146
Cdd:cd13993   61 VSRHPNIITLHDVF--ETEVAIYIVLEYcpnGDLFEAITENRiyVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENI 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 147 IFKDEErTRVKLesledayilrGD-----DDSLSDKHGCPA--YVSPEILNTSG----SYSGKAADVWSLGVMLYTMLVG 215
Cdd:cd13993  139 LLSQDE-GTVKL----------CDfglatTEKISMDFGVGSefYMAPECFDEVGrslkGYPCAAGDIWSLGIILLNLTFG 207

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568977678 216 RYPFH--DIEPSSLFSKIRRGQ--FNIPETLSPKAKCLIRSILRREPSERLTSQEILD 269
Cdd:cd13993  208 RNPWKiaSESDPIFYDYYLNSPnlFDVILPMSDDFYNLLRQIFTVNPNNRILLPELQL 265
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
 121-274 8.66e-17

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


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 79.15  E-value: 8.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 121 FY--QIASAVAHCHDGGLVLRDLKLRKFIFkdEERTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSGsYSgK 198
Cdd:cd05585   98 FYtaELLCALECLHKFNVIYRDLKPENILL--DYTGHIALCDFGLCKLNMKDDDKTNTFCGTPEYLAPELLLGHG-YT-K 173

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568977678 199 AADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTS---QEILDHPWFS 274
Cdd:cd05585  174 AVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPDGFDRDAKDLLIGLLNRDPTKRLGYngaQEIKNHPFFD 252
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 100-273 1.05e-16

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: 78.50  E-value: 1.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDAYILRGDDDSLSdKHG 179
Cdd:cd05613   90 GELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFLLDENERAYS-FCG 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 180 CPAYVSPEILNTSGSYSGKAADVWSLGVMLYTMLVGRYPFH-DIEPSS---LFSKIRRGQFNIPETLSPKAKCLIRSILR 255
Cdd:cd05613  169 TIEYMAPEIVRGGDSGHDKAVDWWSLGVLMYELLTGASPFTvDGEKNSqaeISRRILKSEPPYPQEMSALAKDIIQRLLM 248

                        170       180
                 ....*....|....*....|...
gi 568977678 256 REPSERLTS-----QEILDHPWF 273
Cdd:cd05613  249 KDPKKRLGCgpngaDEIKKHPFF 271
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
 75-273 1.13e-16

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: 78.17  E-value: 1.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFE-RSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLK----LRkfifk 149
Cdd:cd06625   61 HERIVQYYGCLQDEKSLSIFMEyMPGGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKganiLR----- 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 150 dEERTRVKLESLEDAYILRG--DDDSLSDKHGCPAYVSPEILNTSGsYsGKAADVWSLGVMLYTMLVGRYPFHDIEPSSL 227
Cdd:cd06625  136 -DSNGNVKLGDFGASKRLQTicSSTGMKSVTGTPYWMSPEVINGEG-Y-GRKADIWSVGCTVVEMLTTKPPWAEFEPMAA 212

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 568977678 228 FSKI--RRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd06625  213 IFKIatQPTNPQLPPHVSEDARDFLSLIFVRNKKQRPSAEELLSHSFV 260
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
 75-271 1.69e-16

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: 77.40  E-value: 1.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNIN-----QITEILLGET-KAYVFFERS-YGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKL-RKF 146
Cdd:cd14012   57 HPNLVsylafSIERRGRSDGwKVYLLTEYApGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAgNVL 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 147 IFKDEERTRVKL-ESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSGSYsGKAADVWSLGVMLYTMLVGRYPFHDIEPS 225
Cdd:cd14012  137 LDRDAGTGIVKLtDYSLGKTLLDMCSRGSLDEFKQTYWLPPELAQGSKSP-TRKTDVWDLGLLFLQMLFGLDVLEKYTSP 215

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568977678 226 SLFSkirrgqfnIPETLSPKAKCLIRSILRREPSERLTSQEILDHP 271
Cdd:cd14012  216 NPVL--------VSLDLSASLQDFLSKCLSLDPKKRPTALELLPHE 253
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
 108-273 1.71e-16

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: 77.24  E-value: 1.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 108 TCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEerTRVKL------ESLEDayilRGDDDSLSdkhGCP 181
Cdd:cd05122   91 TNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSD--GEVKLidfglsAQLSD----GKTRNTFV---GTP 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 182 AYVSPEILNtSGSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQ---FNIPETLSPKAKCLIRSILRREP 258
Cdd:cd05122  162 YWMAPEVIQ-GKPYGFKA-DIWSLGITAIEMAEGKPPYSELPPMKALFLIATNGppgLRNPKKWSKEFKDFLKKCLQKDP 239

                        170
                 ....*....|....*
gi 568977678 259 SERLTSQEILDHPWF 273
Cdd:cd05122  240 EKRPTAEQLLKHPFI 254
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
 100-274 1.72e-16

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 78.48  E-value: 1.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFkdEERTRVKLESLEDAYILRGDDDSLSdkhG 179
Cdd:PTZ00426 116 GEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLL--DKDGFIKMTDFGFAKVVDTRTYTLC---G 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 180 CPAYVSPEILNTSGSysGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPS 259
Cdd:PTZ00426 191 TPEYIAPEILLNVGH--GKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGIIYFPKFLDNNCKHLMKKLLSHDLT 268

                        170       180
                 ....*....|....*....|
gi 568977678 260 ERL-----TSQEILDHPWFS 274
Cdd:PTZ00426 269 KRYgnlkkGAQNVKEHPWFG 288
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
 88-307 3.26e-16

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: 77.73  E-value: 3.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  88 ETKAYVFFERSY---GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDA 164
Cdd:cd05615   81 QTVDRLYFVMEYvngGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKE 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 165 YILRGDddSLSDKHGCPAYVSPEILntsgSYS--GKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETL 242
Cdd:cd05615  161 HMVEGV--TTRTFCGTPDYIAPEII----AYQpyGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSL 234

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568977678 243 SPKAKCLIRSILRREPSERL-----TSQEILDHPWFStdfSVSNSGFGAKEACDQLVPDV--NMEENLDPFF 307
Cdd:cd05615  235 SKEAVSICKGLMTKHPAKRLgcgpeGERDIREHAFFR---RIDWDKLENREIQPPFKPKVcgKGAENFDKFF 303
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
 115-307 3.65e-16

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: 77.36  E-value: 3.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 115 EEAARlFY--QIASAVAHCHDGGLVLRDLKLRKFIFKDEerTRVKL-------ESLEDAyilrgddDSLSDKHGCPAYVS 185
Cdd:cd05575   95 EPRAR-FYaaEIASALGYLHSLNIIYRDLKPENILLDSQ--GHVVLtdfglckEGIEPS-------DTTSTFCGTPEYLA 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 186 PEILNTSgSYsGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTS- 264
Cdd:cd05575  165 PEVLRKQ-PY-DRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLRTNVSPSARDLLEGLLQKDRTKRLGSg 242

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568977678 265 ---QEILDHPWFStdfSVSNSGFGAKEACDQLVPDVNME---ENLDPFF 307
Cdd:cd05575  243 ndfLEIKNHSFFR---PINWDDLEAKKIPPPFNPNVSGPldlRNIDPEF 288
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
 75-272 3.94e-16

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: 76.83  E-value: 3.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFERS-YGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFI--FKDE 151
Cdd:cd14117   65 HPNILRLYNYFHDRKRIYLILEYApRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLmgYKGE 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 152 ERTRVKLESLEDAyilrgdddSLSDKHGCPA--YVSPEILntSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFS 229
Cdd:cd14117  145 LKIADFGWSVHAP--------SLRRRTMCGTldYLPPEMI--EGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYR 214

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 568977678 230 KIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14117  215 RIVKVDLKFPPFLSDGSRDLISKLLRYHPSERLPLKGVMEHPW 257
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
 111-273 4.26e-16

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: 76.47  E-value: 4.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 111 KLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDAYILrGDDDSLSDKHGCPAYVSPEILN 190
Cdd:cd14114   96 KMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRSNEVKLIDFGLATHL-DPKESVKVTTGTAEFAAPEIVE 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 191 tsGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPET----LSPKAKCLIRSILRREPSERLTSQE 266
Cdd:cd14114  175 --REPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDDSafsgISEEAKDFIRKLLLADPNKRMTIHQ 252


                 ....*..
gi 568977678 267 ILDHPWF 273
Cdd:cd14114  253 ALEHPWL 259
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
 111-272 7.47e-16

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: 75.38  E-value: 7.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 111 KLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERT-RVKLESLEDAYILRGDDdSLSDKHGCPAYVSPEIL 189
Cdd:cd14115   85 ELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVpRVKLIDLEDAVQISGHR-HVHHLLGNPEFAAPEVI 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 190 NtsGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPET----LSPKAKCLIRSILRREPSERLTSQ 265
Cdd:cd14115  164 Q--GTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDEyfgdVSQAARDFINVILQEDPRRRPTAA 241


                 ....*..
gi 568977678 266 EILDHPW 272
Cdd:cd14115  242 TCLQHPW 248
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
 100-269 1.71e-15

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: 74.61  E-value: 1.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCKKLR----EEEAARLFYQIASAVAHCHDGGLVLRDLKLRK-FIFKDeerTRVKLESLedayilrGDDDSL 174
Cdd:cd08224   85 GDLSRLIKHFKKQKrlipERTIWKYFVQLCSALEHMHSKRIMHRDIKPANvFITAN---GVVKLGDL-------GLGRFF 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 175 SDK----H---GCPAYVSPEILNTSGsYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPS--SLFSKIRRGQFN-IPETL-S 243
Cdd:cd08224  155 SSKttaaHslvGTPYYMSPERIREQG-YDFKS-DIWSLGCLLYEMAALQSPFYGEKMNlySLCKKIEKCEYPpLPADLyS 232

                        170       180
                 ....*....|....*....|....*.
gi 568977678 244 PKAKCLIRSILRREPSERLTSQEILD 269
Cdd:cd08224  233 QELRDLVAACIQPDPEKRPDISYVLD 258
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 75-268 2.27e-15

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: 74.24  E-value: 2.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFErsYGDMHSFVRTCKKLR-----EEEAARLFYQIASAVAHCHDGGLVLRDLKlRKFIFK 149
Cdd:cd08219   57 HPNIVAFKESFEADGHLYIVME--YCDGGDLMQKIKLQRgklfpEDTILQWFVQMCLGVQHIHEKRVLHRDIK-SKNIFL 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 150 dEERTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSgSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPSSLFS 229
Cdd:cd08219  134 -TQNGKVKLGDFGSARLLTSPGAYACTYVGTPYYVPPEIWENM-PYNNKS-DIWSLGCILYELCTLKHPFQANSWKNLIL 210

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568977678 230 KIRRGQFN-IPETLSPKAKCLIRSILRREPSERLTSQEIL 268
Cdd:cd08219  211 KVCQGSYKpLPSHYSYELRSLIKQMFKRNPRSRPSATTIL 250
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
 179-274 3.14e-15

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: 75.05  E-value: 3.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 179 GCPAYVSPEILNTSGsYsGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIR--RGQFNIPET--LSPKAKCLIRSIL 254
Cdd:cd05598  167 GTPNYIAPEVLLRTG-Y-TQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKVInwRTTLKIPHEanLSPEAKDLILRLC 244

                         90       100
                 ....*....|....*....|...
gi 568977678 255 rREPSERLTS---QEILDHPWFS 274
Cdd:cd05598  245 -CDAEDRLGRngaDEIKAHPFFA 266
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
 174-272 3.28e-15

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: 73.70  E-value: 3.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 174 LSDKHGCPAYVSPEILNtsGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNiPETLSPK----AKCL 249
Cdd:cd14111  157 LGRRTGTLEYMAPEMVK--GEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAKFD-AFKLYPNvsqsASLF 233

                         90       100
                 ....*....|....*....|...
gi 568977678 250 IRSILRREPSERLTSQEILDHPW 272
Cdd:cd14111  234 LKKVLSSYPWSRPTTKDCFAHAW 256
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
 88-272 4.46e-15

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: 73.60  E-value: 4.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  88 ETKAYVF--FERSYGDMHSFVRTCKKLREEEAARLFY--QIASAVAHCHDGGLVLRDLKLRK-FIFKDEERTRVKLESLE 162
Cdd:cd14082   72 ETPERVFvvMEKLHGDMLEMILSSEKGRLPERITKFLvtQILVALRYLHSKNIVHCDLKPENvLLASAEPFPQVKLCDFG 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 163 DAYILrGDDDSLSDKHGCPAYVSPEILNTSGsYSgKAADVWSLGVMLYTMLVGRYPFHdiEPSSLFSKIRRGQFNIPET- 241
Cdd:cd14082  152 FARII-GEKSFRRSVVGTPAYLAPEVLRNKG-YN-RSLDMWSVGVIIYVSLSGTFPFN--EDEDINDQIQNAAFMYPPNp 226

                        170       180       190
                 ....*....|....*....|....*....|....
gi 568977678 242 ---LSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14082  227 wkeISPDAIDLINNLLQVKMRKRYSVDKSLSHPW 260
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
 108-273 4.78e-15

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: 73.45  E-value: 4.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 108 TCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKfIFKDEERTrVKLESLEDAYILRGDDDSLSDKHGCPAYVSPE 187
Cdd:cd06612   92 TNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGN-ILLNEEGQ-AKLADFGVSGQLTDTMAKRNTVIGTPFWMAPE 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 188 ILNTSGsYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQ---FNIPETLSPKAKCLIRSILRREPSERLTS 264
Cdd:cd06612  170 VIQEIG-YNNKA-DIWSLGITAIEMAEGKPPYSDIHPMRAIFMIPNKPpptLSDPEKWSPEFNDFVKKCLVKDPEERPSA 247


                 ....*....
gi 568977678 265 QEILDHPWF 273
Cdd:cd06612  248 IQLLQHPFI 256
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
 75-272 5.08e-15

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: 73.62  E-value: 5.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFE-RSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLK----------L 143
Cdd:cd06631   62 HVNIVGYLGTCLEDNVVSIFMEfVPGGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKgnnimlmpngV 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 144 RKFI-FKDEERTRVKLESLEDAYILRgdddslsDKHGCPAYVSPEILNTSGSysGKAADVWSLGVMLYTMLVGRYPFHDI 222
Cdd:cd06631  142 IKLIdFGCAKRLCINLSSGSQSQLLK-------SMRGTPYWMAPEVINETGH--GRKSDIWSIGCTVFEMATGKPPWADM 212

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568977678 223 EPSSLFSKI--RRGQF-NIPETLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd06631  213 NPMAAIFAIgsGRKPVpRLPDKFSPEARDFVHACLTRDQDERPSAEQLLKHPF 265
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
 108-273 7.15e-15

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: 72.86  E-value: 7.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 108 TCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEerTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPE 187
Cdd:cd06648   96 THTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSD--GRVKLSDFGFCAQVSKEVPRRKSLVGTPYWMAPE 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 188 ILntSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQ---FNIPETLSPKAKCLIRSILRREPSERLTS 264
Cdd:cd06648  174 VI--SRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNEppkLKNLHKVSPRLRSFLDRMLVRDPAQRATA 251


                 ....*....
gi 568977678 265 QEILDHPWF 273
Cdd:cd06648  252 AELLNHPFL 260
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
 111-273 9.06e-15

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: 72.73  E-value: 9.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 111 KLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDAYILRgDDDSLSDKHGCPAYVSPEILN 190
Cdd:cd14191   96 ELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTKIKLIDFGLARRLE-NAGSLKVLFGTPEFVAPEVIN 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 191 TSGSysGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPET----LSPKAKCLIRSILRREPSERLTSQE 266
Cdd:cd14191  175 YEPI--GYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEafdeISDDAKDFISNLLKKDMKARLTCTQ 252


                 ....*..
gi 568977678 267 ILDHPWF 273
Cdd:cd14191  253 CLQHPWL 259
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
 119-273 1.24e-14

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: 72.30  E-value: 1.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 119 RLFYQIASAVAHCHDGGLVLRDLKLRK-FIFKDEERTRVKLEsLEDAYI---LRGDDDSLSDKHGCP---AYVSPEILNT 191
Cdd:cd13982  103 RLLRQIASGLAHLHSLNIVHRDLKPQNiLISTPNAHGNVRAM-ISDFGLckkLDVGRSSFSRRSGVAgtsGWIAPEMLSG 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 192 SGSY-SGKAADVWSLG-VMLYTMLVGRYPFHDiePSSLFSKIRRGQFNIPETLS-----PKAKCLIRSILRREPSERLTS 264
Cdd:cd13982  182 STKRrQTRAVDIFSLGcVFYYVLSGGSHPFGD--KLEREANILKGKYSLDKLLSlgehgPEAQDLIERMIDFDPEKRPSA 259


                 ....*....
gi 568977678 265 QEILDHPWF 273
Cdd:cd13982  260 EEVLNHPFF 268
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
 60-268 1.24e-14

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 73.90  E-value: 1.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  60 SCYQESLAPCFCLSAHSNINQITEILLGETKAYVFFER-SYGDMHSFVRTCKK----LREEEAARLFYQIASAVAHCHDG 134
Cdd:PTZ00267 109 AAYARSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYgSGGDLNKQIKQRLKehlpFQEYEVGLLFYQIVLALDEVHSR 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 135 GLVLRDLK-------------LRKFIFKDEERTRVKLesledayilrgddDSLSDKHGCPAYVSPEILNTSgSYSgKAAD 201
Cdd:PTZ00267 189 KMMHRDLKsaniflmptgiikLGDFGFSKQYSDSVSL-------------DVASSFCGTPYYLAPELWERK-RYS-KKAD 253

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568977678 202 VWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFN-IPETLSPKAKCLIRSILRREPSERLTSQEIL 268
Cdd:PTZ00267 254 MWSLGVILYELLTLHRPFKGPSQREIMQQVLYGKYDpFPCPVSSGMKALLDPLLSKNPALRPTTQQLL 321
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
 88-273 1.28e-14

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: 72.91  E-value: 1.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  88 ETKAYVFFERSY---GDMHSFVRTCKKLREEEAArlFY--QIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLE 162
Cdd:cd05591   66 QTKDRLFFVMEYvngGDLMFQIQRARKFDEPRAR--FYaaEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMC 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 163 DAYILrgDDDSLSDKHGCPAYVSPEILNTSgSYsGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETL 242
Cdd:cd05591  144 KEGIL--NGKTTTTFCGTPDYIAPEILQEL-EY-GPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWL 219

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568977678 243 SPKAKCLIRSILRREPSERL-------TSQEILDHPWF 273
Cdd:cd05591  220 SKEAVSILKAFMTKNPAKRLgcvasqgGEDAIRQHPFF 257
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
 116-270 1.49e-14

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: 72.40  E-value: 1.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 116 EAARLFYQIASAVAHCHDGGLVLRDLKLRKfIFKDEER----------TRVKLEsLEDAYIL--------RGDDDSLSDK 177
Cdd:cd14046  105 RLWRLFRQILEGLAYIHSQGIIHRDLKPVN-IFLDSNGnvkigdfglaTSNKLN-VELATQDinkstsaaLGSSGDLTGN 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 178 HGCPAYVSPEIL-NTSGSYSGKaADVWSLGVMLYTMLvgrYPFHD-IEPSSLFSKIRRGQFNIPETL----SPKAKCLIR 251
Cdd:cd14046  183 VGTALYVAPEVQsGTKSTYNEK-VDMYSLGIIFFEMC---YPFSTgMERVQILTALRSVSIEFPPDFddnkHSKQAKLIR 258

                        170
                 ....*....|....*....
gi 568977678 252 SILRREPSERLTSQEILDH 270
Cdd:cd14046  259 WLLNHDPAKRPSAQELLKS 277
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
 115-273 1.58e-14

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: 72.36  E-value: 1.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 115 EEAARLFY--QIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEdayILRGDDDSLSDKHGCPAYVSPEIL-NT 191
Cdd:cd05630  100 PEARAVFYaaEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLA---VHVPEGQTIKGRVGTVGYMAPEVVkNE 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 192 SGSYSgkaADVWSLGVMLYTMLVGRYPFHD----IEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERL----- 262
Cdd:cd05630  177 RYTFS---PDWWALGCLLYEMIAGQSPFQQrkkkIKREEVERLVKEVPEEYSEKFSPQARSLCSMLLCKDPAERLgcrgg 253

                        170
                 ....*....|.
gi 568977678 263 TSQEILDHPWF 273
Cdd:cd05630  254 GAREVKEHPLF 264
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
 75-273 1.96e-14

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: 72.33  E-value: 1.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFERSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEerT 154
Cdd:cd06659   77 HPNVVEMYKSYLVGEELWVLMEYLQGGALTDIVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLD--G 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 155 RVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSgSYsGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRG 234
Cdd:cd06659  155 RVKLSDFGFCAQISKDVPKRKSLVGTPYWMAPEVISRC-PY-GTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDS 232

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 568977678 235 QfniPETL------SPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd06659  233 P---PPKLknshkaSPVLRDFLERMLVRDPQERATAQELLDHPFL 274
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
 115-273 2.00e-14

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: 72.65  E-value: 2.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 115 EEAARlFY--QIASAVAHCHDGGLVLRDLKLRKFIFkdEERTRVKLEsleDAYILRGdddsLSDKH------GCPAYVSP 186
Cdd:cd05599  100 EEETR-FYiaETVLAIESIHKLGYIHRDIKPDNLLL--DARGHIKLS---DFGLCTG----LKKSHlaystvGTPDYIAP 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 187 EILNTSGsYsGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIR--RGQFNIPE--TLSPKAKCLIRSILrREPSERL 262
Cdd:cd05599  170 EVFLQKG-Y-GKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMnwRETLVFPPevPISPEAKDLIERLL-CDAEHRL 246

                        170
                 ....*....|....
gi 568977678 263 TS---QEILDHPWF 273
Cdd:cd05599  247 GAngvEEIKSHPFF 260
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
 115-276 2.90e-14

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: 72.41  E-value: 2.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 115 EEAARlFY--QIASAVAHCHDGGLVLRDLKLRKFIFkdEERTRVKLESLedAYILRGDDDSL--SDKH-GCPAYVSPEIL 189
Cdd:cd05596  124 EKWAR-FYtaEVVLALDAIHSMGFVHRDVKPDNMLL--DASGHLKLADF--GTCMKMDKDGLvrSDTAvGTPDYISPEVL 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 190 NTSG--SYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQ----FNIPETLSPKAKCLIRSILrREPSERLT 263
Cdd:cd05596  199 KSQGgdGVYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIMNHKnslqFPDDVEISKDAKSLICAFL-TDREVRLG 277

                        170
                 ....*....|....*.
gi 568977678 264 S---QEILDHPWFSTD 276
Cdd:cd05596  278 RngiEEIKAHPFFKND 293
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
 111-271 5.28e-14

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: 70.49  E-value: 5.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 111 KLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDeeRTRVKLESLEDAYILrgdDDSLSDKHGCPAYVSPEILN 190
Cdd:cd13997   99 KLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISN--KGTCKIGDFGLATRL---ETSGDVEEGDSRYLAPELLN 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 191 TSGSYSgKAADVWSLGVMLYTMlVGRYPFHDIEPSSLfsKIRRGQFNIPET--LSPKAKCLIRSILRREPSERLTSQEIL 268
Cdd:cd13997  174 ENYTHL-PKADIFSLGVTVYEA-ATGEPLPRNGQQWQ--QLRQGKLPLPPGlvLSQELTRLLKVMLDPDPTRRPTADQLL 249


                 ...
gi 568977678 269 DHP 271
Cdd:cd13997  250 AHD 252
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
 75-273 5.92e-14

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: 70.84  E-value: 5.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFERSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEerT 154
Cdd:cd06658   78 HENVVDMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSD--G 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 155 RVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILntSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRrg 234
Cdd:cd06658  156 RIKLSDFGFCAQVSKEVPKRKSLVGTPYWMAPEVI--SRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIR-- 231

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568977678 235 qfnipETLSPKAKCL--IRSILR--------REPSERLTSQEILDHPWF 273
Cdd:cd06658  232 -----DNLPPRVKDShkVSSVLRgfldlmlvREPSQRATAQELLQHPFL 275
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
 95-272 6.09e-14

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: 69.95  E-value: 6.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  95 FERSYGDmhSFVRTckklrEEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDAYILRGDDDsL 174
Cdd:cd14103   78 FERVVDD--DFELT-----ERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSRTGNQIKIIDFGLARKYDPDKK-L 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 175 SDKHGCPAYVSPEILNtsgsYS--GKAADVWSLGVMLYTMLVGRYPF---HDIEPsslFSKIRRGQFN----IPETLSPK 245
Cdd:cd14103  150 KVLFGTPEFVAPEVVN----YEpiSYATDMWSVGVICYVLLSGLSPFmgdNDAET---LANVTRAKWDfddeAFDDISDE 222

                        170       180
                 ....*....|....*....|....*..
gi 568977678 246 AKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14103  223 AKDFISKLLVKDPRKRMSAAQCLQHPW 249
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
 88-273 1.24e-13

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: 70.02  E-value: 1.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  88 ETKAYVFFERSY---GDM----HSFVRTckklreEEAARlFYqiASAVA----HCHDGGLVLRDLKLRKFIFKDEerTRV 156
Cdd:cd05589   72 QTPEHVCFVMEYaagGDLmmhiHEDVFS------EPRAV-FY--AACVVlglqFLHEHKIVYRDLKLDNLLLDTE--GYV 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 157 KL-------ESLedayilrGDDDSLSDKHGCPAYVSPEILnTSGSYSgKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFS 229
Cdd:cd05589  141 KIadfglckEGM-------GFGDRTSTFCGTPEFLAPEVL-TDTSYT-RAVDWWGLGVLIYEMLVGESPFPGDDEEEVFD 211

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568977678 230 KIRRGQFNIPETLSPKAKCLIRSILRREPSERLTS-----QEILDHPWF 273
Cdd:cd05589  212 SIVNDEVRYPRFLSTEAISIMRRLLRKNPERRLGAserdaEDVKKQPFF 260
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
 75-274 1.83e-13

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: 69.28  E-value: 1.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFERSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEerT 154
Cdd:cd06657   76 HENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHD--G 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 155 RVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILntSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRg 234
Cdd:cd06657  154 RVKLSDFGFCAQVSKEVPRRKSLVGTPYWMAPELI--SRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRD- 230

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568977678 235 qfNIPETL------SPKAKCLIRSILRREPSERLTSQEILDHPWFS 274
Cdd:cd06657  231 --NLPPKLknlhkvSPSLKGFLDRLLVRDPAQRATAAELLKHPFLA 274
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
 115-274 1.91e-13

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: 69.14  E-value: 1.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 115 EEAARLFY--QIASAVAHCHDGGLVLRDLKLRKFIFKDEerTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNts 192
Cdd:cd05608  103 QEPRACFYtaQIISGLEHLHQRRIIYRDLKPENVLLDDD--GNVRISDLGLAVELKDGQTKTKGYAGTPGFMAPELLL-- 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 193 GSYSGKAADVWSLGVMLYTMLVGRYPF----HDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERL-----T 263
Cdd:cd05608  179 GEEYDYSVDYFTLGVTLYEMIAARGPFrargEKVENKELKQRILNDSVTYSEKFSPASKSICEALLAKDPEKRLgfrdgN 258

                        170
                 ....*....|.
gi 568977678 264 SQEILDHPWFS 274
Cdd:cd05608  259 CDGLRTHPFFR 269
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
 114-273 2.60e-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: 68.38  E-value: 2.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 114 EEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDAYILRGDDDSLSdKHGCPAYVSPEILntSG 193
Cdd:cd14107   97 EAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTREDIKICDFGFAQEITPSEHQFS-KYGSPEFVAPEIV--HQ 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 194 SYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQ--FNIPE--TLSPKAKCLIRSILRREPSERLTSQEILD 269
Cdd:cd14107  174 EPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVvsWDTPEitHLSEDAKDFIKRVLQPDPEKRPSASECLS 253


                 ....
gi 568977678 270 HPWF 273
Cdd:cd14107  254 HEWF 257
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
 114-272 2.75e-13

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: 68.41  E-value: 2.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 114 EEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKdeERTRVKLESLEDAYILRGDDDSLSDKhgCPAYV---SPEILN 190
Cdd:cd14110   98 EAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIIT--EKNLLKIVDLGNAQPFNQGKVLMTDK--KGDYVetmAPELLE 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 191 TSGSysGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPET---LSPKAKCLIRSILRREPSERLTSQEI 267
Cdd:cd14110  174 GQGA--GPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQLSRCyagLSGGAVNFLKSTLCAKPWGRPTASEC 251


                 ....*
gi 568977678 268 LDHPW 272
Cdd:cd14110  252 LQNPW 256
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 75-273 3.00e-13

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: 68.45  E-value: 3.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFErsYGDMHSFVRTCKKLR-----EEEAARLFYQIASAVAHCHDGGLVLRDLKLRK-FIF 148
Cdd:cd08225   58 HPNIVTFFASFQENGRLFIVME--YCDGGDLMKRINRQRgvlfsEDQILSWFVQISLGLKHIHDRKILHRDIKSQNiFLS 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 149 KDEertrvKLESLEDAYILRGDDDSLSDKHGC---PAYVSPEILNTSgSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPS 225
Cdd:cd08225  136 KNG-----MVAKLGDFGIARQLNDSMELAYTCvgtPYYLSPEICQNR-PYNNKT-DIWSLGCVLYELCTLKHPFEGNNLH 208

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568977678 226 SLFSKIRRGQFN-IPETLSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd08225  209 QLVLKICQGYFApISPNFSRDLRSLISQLFKVSPRDRPSITSILKRPFL 257
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
 100-274 3.29e-13

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: 68.62  E-value: 3.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCKKLREEEAArlFY--QIASAVAHCHDGGLVLRDLKLRKFIFkdEERTRVKLESLEDAYilrgdDDSLSDK 177
Cdd:cd05606   83 GDLHYHLSQHGVFSEAEMR--FYaaEVILGLEHMHNRFIVYRDLKPANILL--DEHGHVRISDLGLAC-----DFSKKKP 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 178 H---GCPAYVSPEILNTSGSYSgKAADVWSLGVMLYTMLVGRYPF--------HDIEPSSLFSKIrrgqfNIPETLSPKA 246
Cdd:cd05606  154 HasvGTHGYMAPEVLQKGVAYD-SSADWFSLGCMLYKLLKGHSPFrqhktkdkHEIDRMTLTMNV-----ELPDSFSPEL 227

                        170       180       190
                 ....*....|....*....|....*....|...
gi 568977678 247 KCLIRSILRREPSERL-----TSQEILDHPWFS 274
Cdd:cd05606  228 KSLLEGLLQRDVSKRLgclgrGATEVKEHPFFK 260
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 74-271 3.32e-13

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: 68.30  E-value: 3.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  74 AHSNINQITEILlgETKAYVFFERSY---GDMHSFVRTCKKL--REEEAARLFYQIASAVAHCHDGGLVLRDLKLRK-FI 147
Cdd:cd08218   57 KHPNIVQYQESF--EENGNLYIVMDYcdgGDLYKRINAQRGVlfPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNiFL 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 148 FKDeerTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSgSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPSSL 227
Cdd:cd08218  135 TKD---GIIKLGDFGIARVLNSTVELARTCIGTPYYLSPEICENK-PYNNKS-DIWALGCVLYEMCTLKHAFEAGNMKNL 209

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 568977678 228 FSKIRRGQF-NIPETLSPKAKCLIRSILRREPSERLTSQEILDHP 271
Cdd:cd08218  210 VLKIIRGSYpPVPSRYSYDLRSLVSQLFKRNPRDRPSINSILEKP 254
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
 75-273 4.01e-13

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: 68.50  E-value: 4.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFERSYGDMHSFVRTCKKLREEEAARLF-YQIASAVAHCHDGGLVLRDLKLRKfIFKDEER 153
Cdd:cd07833   59 HENIVNLKEAFRRKGRLYLVFEYVERTLLELLEASPGGLPPDAVRSYiWQLLQAIAYCHSHNIIHRDIKPEN-ILVSESG 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 154 TrVKLESLEDAYILRGDDDS-LSDKHGCPAYVSPEILNTSGSYsGKAADVWSLGVMLYTMLVGRYPF-----HD------ 221
Cdd:cd07833  138 V-LKLCDFGFARALTARPASpLTDYVATRWYRAPELLVGDTNY-GKPVDVWAIGCIMAELLDGEPLFpgdsdIDqlyliq 215

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568977678 222 -----IEPS--SLFSK---IRRGQF---NIPETL--------SPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd07833  216 kclgpLPPShqELFSSnprFAGVAFpepSQPESLerrypgkvSSPALDFLKACLRMDPKERLTCDELLQHPYF 288
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
 72-273 4.38e-13

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: 68.07  E-value: 4.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  72 LSAHSNINQITEILLGETKAYV--FFERSYGDMHSFVRTCKK-LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIF 148
Cdd:cd07831   54 LSPHPNILRLIEVLFDRKTGRLalVFELMDMNLYELIKGRKRpLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILI 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 149 KDEErtrVKLESLedayilrGDDDSLSDKHGCPAYVS------PEILNTSGSYSGKAaDVWSLGVMLYTMLVGRYPF--- 219
Cdd:cd07831  134 KDDI---LKLADF-------GSCRGIYSKPPYTEYIStrwyraPECLLTDGYYGPKM-DIWAVGCVFFEILSLFPLFpgt 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 220 ---------HDI---EPSSLFSKIRRG---QFNIPE-----------TLSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd07831  203 neldqiakiHDVlgtPDAEVLKKFRKSrhmNYNFPSkkgtglrkllpNASAEGLDLLKKLLAYDPDERITAKQALRHPYF 282
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
 100-273 5.59e-13

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


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 68.55  E-value: 5.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDAYILRGDDDSLsdkhG 179
Cdd:cd05633   93 GDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSKKKPHASV----G 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 180 CPAYVSPEILNTSGSYSgKAADVWSLGVMLYTMLVGRYPF--------HDIEPSSLFSKIRrgqfnIPETLSPKAKCLIR 251
Cdd:cd05633  169 THGYMAPEVLQKGTAYD-SSADWFSLGCMLFKLLRGHSPFrqhktkdkHEIDRMTLTVNVE-----LPDSFSPELKSLLE 242

                        170       180
                 ....*....|....*....|....*..
gi 568977678 252 SILRREPSERL-----TSQEILDHPWF 273
Cdd:cd05633  243 GLLQRDVSKRLgchgrGAQEVKEHSFF 269
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
 114-274 6.07e-13

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: 68.37  E-value: 6.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 114 EEEAARlFY--QIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDAYIlrGDDDSLSDKHGCPAYVSPEILNT 191
Cdd:cd05586   94 SEDRAK-FYiaELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKADL--TDNKTTNTFCGTTEYLAPEVLLD 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 192 SGSYsGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIP-ETLSPKAKCLIRSILRREPSERLTS----QE 266
Cdd:cd05586  171 EKGY-TKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPkDVLSDEGRSFVKGLLNRNPKHRLGAhddaVE 249


                 ....*...
gi 568977678 267 ILDHPWFS 274
Cdd:cd05586  250 LKEHPFFA 257
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
 179-274 6.55e-13

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: 68.14  E-value: 6.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 179 GCPAYVSPEILNTS----GSYsGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKI--RRGQFNIP---ETLSPKAKCL 249
Cdd:cd05597  165 GTPDYISPEILQAMedgkGRY-GPECDWWSLGVCMYEMLYGETPFYAESLVETYGKImnHKEHFSFPddeDDVSEEAKDL 243

                         90       100
                 ....*....|....*....|....*...
gi 568977678 250 IRSILRRePSERLTS---QEILDHPWFS 274
Cdd:cd05597  244 IRRLICS-RERRLGQngiDDFKKHPFFE 270
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
 120-270 8.20e-13

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


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 67.21  E-value: 8.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 120 LFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRV-------KLESLEDAYILRGDDDSlSDKH----GCPAYVSPEI 188
Cdd:cd14048  123 IFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVgdfglvtAMDQGEPEQTVLTPMPA-YAKHtgqvGTRLYMSPEQ 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 189 LNTSgSYSGKaADVWSLGVMLYTMLvgrYPFH-DIEPSSLFSKIRRGQFNIPETLS-PKAKCLIRSILRREPSERLTSQE 266
Cdd:cd14048  202 IHGN-QYSEK-VDIFALGLILFELI---YSFStQMERIRTLTDVRKLKFPALFTNKyPEERDMVQQMLSPSPSERPEAHE 276


                 ....
gi 568977678 267 ILDH 270
Cdd:cd14048  277 VIEH 280
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
 121-276 9.55e-13

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: 68.10  E-value: 9.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 121 FY--QIASAVAHCHDGGLVLRDLKLRKFIFkdEERTRVKLESLEDAYILRGDDDSLSDKH-GCPAYVSPEILNTSGS--Y 195
Cdd:cd05621  155 FYtaEVVLALDAIHSMGLIHRDVKPDNMLL--DKYGHLKLADFGTCMKMDETGMVHCDTAvGTPDYISPEVLKSQGGdgY 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 196 SGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKI--RRGQFNIPE--TLSPKAKCLIRSIL--RREPSERLTSQEILD 269
Cdd:cd05621  233 YGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKImdHKNSLNFPDdvEISKHAKNLICAFLtdREVRLGRNGVEEIKQ 312


                 ....*..
gi 568977678 270 HPWFSTD 276
Cdd:cd05621  313 HPFFRND 319
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
 75-273 9.74e-13

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: 67.01  E-value: 9.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFErsYGD---MHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRK-FIFKD 150
Cdd:cd07847   59 HPNLVNLIEVFRRKRKLHLVFE--YCDhtvLNELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENiLITKQ 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 151 EErtrVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSGSYsGKAADVWSLGVMLYTMLVG--------------- 215
Cdd:cd07847  137 GQ---IKLCDFGFARILTGPGDDYTDYVATRWYRAPELLVGDTQY-GPPVDVWAIGCVFAELLTGqplwpgksdvdqlyl 212

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568977678 216 -RYPFHDIEP--SSLFS--KIRRGQfNIPE------------TLSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd07847  213 iRKTLGDLIPrhQQIFStnQFFKGL-SIPEpetrepleskfpNISSPALSFLKGCLQMDPTERLSCEELLEHPYF 286
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
 119-269 1.03e-12

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: 67.15  E-value: 1.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 119 RLFYQIASAVAHCHDGG--LVLRDLKLRKFIFKDEERtrVKL--------ESLEDAYILRGDDDSLSD----KHGCPAYV 184
Cdd:cd14036  112 KIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQ--IKLcdfgsattEAHYPDYSWSAQKRSLVEdeitRNTTPMYR 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 185 SPEILNTSGSYS-GKAADVWSLGVMLYTMLVGRYPFHDiepsSLFSKIRRGQFNIPETlSPKAKC---LIRSILRREPSE 260
Cdd:cd14036  190 TPEMIDLYSNYPiGEKQDIWALGCILYLLCFRKHPFED----GAKLRIINAKYTIPPN-DTQYTVfhdLIRSTLKVNPEE 264


                 ....*....
gi 568977678 261 RLTSQEILD 269
Cdd:cd14036  265 RLSITEIVE 273
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
 112-273 1.08e-12

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: 66.87  E-value: 1.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 112 LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKdeertrvKLESLEDAYILR-------GDDDSLSDKHGCPAYV 184
Cdd:cd14198  107 VSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLS-------SIYPLGDIKIVDfgmsrkiGHACELREIMGTPEYL 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 185 SPEILNTSGSYSgkAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIrrGQFNIP---ET---LSPKAKCLIRSILRREP 258
Cdd:cd14198  180 APEILNYDPITT--ATDMWNIGVIAYMLLTHESPFVGEDNQETFLNI--SQVNVDyseETfssVSQLATDFIQKLLVKNP 255

                        170
                 ....*....|....*
gi 568977678 259 SERLTSQEILDHPWF 273
Cdd:cd14198  256 EKRPTAEICLSHSWL 270
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
 120-271 1.65e-12

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: 66.47  E-value: 1.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 120 LFY--QIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRvkLESLEDAYILRgDDDSLSDKHGCPAYVSPEILnTSGSYSg 197
Cdd:cd05607  107 IFYsaQITCGILHLHSLKIVYRDMKPENVLLDDNGNCR--LSDLGLAVEVK-EGKPITQRAGTNGYMAPEIL-KEESYS- 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 198 KAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRG------QFNIPeTLSPKAKCLIRSILRREPSERLTSQEILDHP 271
Cdd:cd05607  182 YPVDWFAMGCSIYEMVAGRTPFRDHKEKVSKEELKRRtledevKFEHQ-NFTEEAKDICRLFLAKKPENRLGSRTNDDDP 260
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
 63-268 1.80e-12

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: 66.32  E-value: 1.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  63 QESLApcFCLSAHSNINQITE--ILLGETKAYVFFERSYGDMHSFVRTCK--------KLREEEAARLFYQIASAVAHCH 132
Cdd:cd05043   56 QESSL--LYGLSHQNLLPILHvcIEDGEKPMVLYPYMNWGNLKLFLQQCRlseannpqALSTQQLVHMALQIACGMSYLH 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 133 DGGLVLRDLKLRKFIFKDEERTRVKLESL-EDayILRGDDDSLSDKHGCP-AYVSPEILNTSgSYSgKAADVWSLGVMLY 210
Cdd:cd05043  134 RRGVIHKDIAARNCVIDDELQVKITDNALsRD--LFPMDYHCLGDNENRPiKWMSLESLVNK-EYS-SASDVWSFGVLLW 209

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568977678 211 T-MLVGRYPFHDIEPSSLFSKIRRGQ-----FNIPETLSPKAKCLIRSilrrEPSERLTSQEIL 268
Cdd:cd05043  210 ElMTLGQTPYVEIDPFEMAAYLKDGYrlaqpINCPDELFAVMACCWAL----DPEERPSFQQLV 269
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
 75-273 1.90e-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: 66.16  E-value: 1.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFERSYGDMHSFVRTCKK--LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEE 152
Cdd:cd07835   57 HPNIVRLLDVVHSENKLYLVFEFLDLDLKKYMDSSPLtgLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEG 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 153 rtrvklesledayILRGDDDSLSDKHGCPA-----------YVSPEILNTSGSYSgKAADVWSLGVMLYTMLVGRYPFH- 220
Cdd:cd07835  137 -------------ALKLADFGLARAFGVPVrtythevvtlwYRAPEILLGSKHYS-TPVDIWSVGCIFAEMVTRRPLFPg 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 221 DIEPSSLFsKIRR-----------GQFNIPE------------------TLSPKAKCLIRSILRREPSERLTSQEILDHP 271
Cdd:cd07835  203 DSEIDQLF-RIFRtlgtpdedvwpGVTSLPDykptfpkwarqdlskvvpSLDEDGLDLLSQMLVYDPAKRISAKAALQHP 281


                 ..
gi 568977678 272 WF 273
Cdd:cd07835  282 YF 283
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
 75-270 2.04e-12

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: 65.80  E-value: 2.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFERSYG-DMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEER 153
Cdd:cd13995   55 HENIAELYGALLWEETVHLFMEAGEGgSVLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKA 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 154 TRV----KLESLEDAYILRgdddslsDKHGCPAYVSPEILNTSGsYSGKAaDVWSLGVMLYTMLVG------RYPfHDIE 223
Cdd:cd13995  135 VLVdfglSVQMTEDVYVPK-------DLRGTEIYMSPEVILCRG-HNTKA-DIYSLGATIIHMQTGsppwvrRYP-RSAY 204

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568977678 224 PSSLFskIRRGQF----NIPETLSPKAKCLIRSILRREPSERLTSQEILDH 270
Cdd:cd13995  205 PSYLY--IIHKQAppleDIAQDCSPAMRELLEAALERNPNHRSSAAELLKH 253
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
 72-274 2.31e-12

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: 66.43  E-value: 2.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  72 LSAHSNINQITEILLGETKA--YVFFERSYGDMHSFVRtcKKLREEEAAR-LFYQIASAVAHCHDGGLVLRDLKLRKfIF 148
Cdd:cd07852   63 LNDHPNIIKLLNVIRAENDKdiYLVFEYMETDLHAVIR--ANILEDIHKQyIMYQLLKALKYLHSGGVIHRDLKPSN-IL 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 149 KDEErTRVKL------ESLEDAYILRGDDDsLSDkhgcpaYV------SPEILNTSGSYSgKAADVWSLGVMLYTMLVGR 216
Cdd:cd07852  140 LNSD-CRVKLadfglaRSLSQLEEDDENPV-LTD------YVatrwyrAPEILLGSTRYT-KGVDMWSVGCILGEMLLGK 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 217 YPF------HDIE--------PSS--------------LFSKIRRGQFNIPETL---SPKAKCLIRSILRREPSERLTSQ 265
Cdd:cd07852  211 PLFpgtstlNQLEkiievigrPSAediesiqspfaatmLESLPPSRPKSLDELFpkaSPDALDLLKKLLVFNPNKRLTAE 290


                 ....*....
gi 568977678 266 EILDHPWFS 274
Cdd:cd07852  291 EALRHPYVA 299
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
 58-273 2.62e-12

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


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 65.81  E-value: 2.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  58 EISCYQEslapcfcLSAHSNINQITEILLGETKAYVFFERSYGDMHSFVRTCKK-LREEEAARLFYQIASAVAHCHDGGL 136
Cdd:cd07832   49 EIKALQA-------CQGHPYVVKLRDVFPHGTGFVLVFEYMLSSLSEVLRDEERpLTEAQVKRYMRMLLKGVAYMHANRI 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 137 VLRDLKLRKFIFKDEErtRVKLESLEDAYILRGDDDSL-SDKHGCPAYVSPEILNTSGSYsGKAADVWSLGVMLYTMLVG 215
Cdd:cd07832  122 MHRDLKPANLLISSTG--VLKIADFGLARLFSEEDPRLySHQVATRWYRAPELLYGSRKY-DEGVDLWAVGCIFAELLNG 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 216 RYPF---HDIE-----------------P--SSL--FSKIR-------RGQFNIPETlSPKAKCLIRSILRREPSERLTS 264
Cdd:cd07832  199 SPLFpgeNDIEqlaivlrtlgtpnektwPelTSLpdYNKITfpeskgiRLEEIFPDC-SPEAIDLLKGLLVYNPKKRLSA 277


                 ....*....
gi 568977678 265 QEILDHPWF 273
Cdd:cd07832  278 EEALRHPYF 286
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
 114-275 2.94e-12

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: 65.84  E-value: 2.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 114 EEEAARlFY--QIASAVAHCHDGGLVLRDLKLRKFIFKDeeRTRVKLESLEDAYILRgDDDSLSDKHGCPAYVSPEIL-N 190
Cdd:cd05605  100 EEERAV-FYaaEITCGLEHLHSERIVYRDLKPENILLDD--HGHVRISDLGLAVEIP-EGETIRGRVGTVGYMAPEVVkN 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 191 TSGSYSgkaADVWSLGVMLYTMLVGRYPF----HDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERL---- 262
Cdd:cd05605  176 ERYTFS---PDWWGLGCLIYEMIEGQAPFrarkEKVKREEVDRRVKEDQEEYSEKFSEEAKSICSQLLQKDPKTRLgcrg 252

                        170
                 ....*....|....
gi 568977678 263 -TSQEILDHPWFST 275
Cdd:cd05605  253 eGAEDVKSHPFFKS 266
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
 116-270 3.04e-12

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: 65.59  E-value: 3.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 116 EAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDAyilRGDDDSLSDKHGCPAYVSPEILNtSGSY 195
Cdd:cd14047  118 LALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGDFGLVTS---LKNDGKRTKSKGTLSYMSPEQIS-SQDY 193

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568977678 196 sGKAADVWSLGVMLYTMLvgrYPFHDI-EPSSLFSKIRRGQfnIPETLS---PKAKCLIRSILRREPSERLTSQEILDH 270
Cdd:cd14047  194 -GKEVDIYALGLILFELL---HVCDSAfEKSKFWTDLRNGI--LPDIFDkryKIEKTIIKKMLSKKPEDRPNASEILRT 266
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
 75-272 3.25e-12

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: 65.48  E-value: 3.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQiteiLLG--ETKAY--VFFER-SYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKfIFK 149
Cdd:cd06629   67 HPNIVQ----YLGfeETEDYfsIFLEYvPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADN-ILV 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 150 DEERTrVKL------ESLEDAYilrgDDDSLSDKHGCPAYVSPEILNTSG-SYSGKAaDVWSLGVMLYTMLVGRYPFHDI 222
Cdd:cd06629  142 DLEGI-CKIsdfgisKKSDDIY----GNNGATSMQGSVFWMAPEVIHSQGqGYSAKV-DIWSLGCVVLEMLAGRRPWSDD 215

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568977678 223 EPSSLFSKI--RRGQFNIPE--TLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd06629  216 EAIAAMFKLgnKRSAPPVPEdvNLSPEALDFLNACFAIDPRDRPTAAELLSHPF 269
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
 127-273 3.36e-12

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: 65.46  E-value: 3.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 127 AVAHCHDGGLVLRDLKLRKfIFKDEERTrVKLESLE-DAYILRGDDDSLSDKH---GCPAYVSPEILNTSGSYSGKAaDV 202
Cdd:cd06610  114 GLEYLHSNGQIHRDVKAGN-ILLGEDGS-VKIADFGvSASLATGGDRTRKVRKtfvGTPCWMAPEVMEQVRGYDFKA-DI 190

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568977678 203 WSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKC------LIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd06610  191 WSFGITAIELATGAAPYSKYPPMKVLMLTLQNDPPSLETGADYKKYsksfrkMISLCLQKDPSKRPTAEELLKHKFF 267
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
 111-261 3.72e-12

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: 65.38  E-value: 3.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 111 KLREEEAARLFYQIASAVAHCH--DGGLVLRDLKL--------RKFIFKDEERTRVKLESLEDAYILRGDDDSLSdKHGC 180
Cdd:cd14037  104 GLTESEILKIFCDVCEAVAAMHylKPPLIHRDLKVenvlisdsGNYKLCDFGSATTKILPPQTKQGVTYVEEDIK-KYTT 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 181 PAYVSPEILNTsgsYSGKA----ADVWSLGVMLYTMLVGRYPFHDIEPSSlfskIRRGQFNIPE--TLSPKAKCLIRSIL 254
Cdd:cd14037  183 LQYRAPEMIDL---YRGKPitekSDIWALGCLLYKLCFYTTPFEESGQLA----ILNGNFTFPDnsRYSKRLHKLIRYML 255


                 ....*..
gi 568977678 255 RREPSER 261
Cdd:cd14037  256 EEDPEKR 262
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
 115-276 4.28e-12

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: 66.18  E-value: 4.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 115 EEAARLFY-QIASAVAHCHDGGLVLRDLKLRKFIFkdEERTRVKLESLEDAYILRGDDDSLSDKH-GCPAYVSPEILNTS 192
Cdd:cd05622  171 EKWARFYTaEVVLALDAIHSMGFIHRDVKPDNMLL--DKSGHLKLADFGTCMKMNKEGMVRCDTAvGTPDYISPEVLKSQ 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 193 GS--YSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKI--RRGQFNIPE--TLSPKAKCLIRSIL--RREPSERLTS 264
Cdd:cd05622  249 GGdgYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKImnHKNSLTFPDdnDISKEAKNLICAFLtdREVRLGRNGV 328

                        170
                 ....*....|..
gi 568977678 265 QEILDHPWFSTD 276
Cdd:cd05622  329 EEIKRHLFFKND 340
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
 46-275 5.08e-12

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: 65.05  E-value: 5.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  46 SRARSEIPGHVFEIscyqESLAPCfclsAHSNINQITEILLGETKAYVFFERSYGDMHSFV--RTCKKLREEEAARLFYQ 123
Cdd:cd06643   40 TKSEEELEDYMVEI----DILASC----DHPNIVKLLDAFYYENNLWILIEFCAGGAVDAVmlELERPLTEPQIRVVCKQ 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 124 IASAVAHCHDGGLVLRDLKLRKFIFKDEerTRVKLE----SLEDAYILRGDDDSLsdkhGCPAYVSPEILNTSGS----Y 195
Cdd:cd06643  112 TLEALVYLHENKIIHRDLKAGNILFTLD--GDIKLAdfgvSAKNTRTLQRRDSFI----GTPYWMAPEVVMCETSkdrpY 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 196 SGKAaDVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQ---FNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd06643  186 DYKA-DVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEpptLAQPSRWSPEFKDFLRKCLEKNVDARWTTSQLLQHPF 264


                 ...
gi 568977678 273 FST 275
Cdd:cd06643  265 VSV 267
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
 112-271 5.70e-12

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: 64.74  E-value: 5.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 112 LREEEAARLFY--QIASAVAHCHDGGLVLRDLKLRKfIFKDEERTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEIL 189
Cdd:cd06624  103 LKDNENTIGYYtkQILEGLKYLHDNKIVHRDIKGDN-VLVNTYSGVVKISDFGTSKRLAGINPCTETFTGTLQYMAPEVI 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 190 NTSGSYSGKAADVWSLGVMLYTMLVGRYPFHDI-EPSSLFSKIrrGQF----NIPETLSPKAKCLIRSILRREPSERLTS 264
Cdd:cd06624  182 DKGQRGYGPPADIWSLGCTIIEMATGKPPFIELgEPQAAMFKV--GMFkihpEIPESLSEEAKSFILRCFEPDPDKRATA 259


                 ....*..
gi 568977678 265 QEILDHP 271
Cdd:cd06624  260 SDLLQDP 266
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
 115-274 6.78e-12

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: 64.99  E-value: 6.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 115 EEAARlFY--QIASAVAHCHDGGLVLRDLKLRKFIFkdEERTRVKL-------ESLEDayilrgdDDSLSDKHGCPAYVS 185
Cdd:cd05603   95 EPRAR-FYaaEVASAIGYLHSLNIIYRDLKPENILL--DCQGHVVLtdfglckEGMEP-------EETTSTFCGTPEYLA 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 186 PEILNTSgSYSgKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTS- 264
Cdd:cd05603  165 PEVLRKE-PYD-RTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLPGGKTVAACDLLQGLLHKDQRRRLGAk 242

                        170
                 ....*....|...
gi 568977678 265 ---QEILDHPWFS 274
Cdd:cd05603  243 adfLEIKNHVFFS 255
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
 98-269 7.67e-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: 64.11  E-value: 7.67e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678    98 SYGDMHSFVRTCKK--LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRV------KLESLEDAYILRG 169
Cdd:smart00221  84 PGGDLLDYLRKNRPkeLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKIsdfglsRDLYDDDYYKVKG 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678   170 DDdslsdkhgCP-AYVSPEILNTsGSYSgKAADVWSLGVMLYTML-VGRYPFHDIEPSSLFSKIRRGQFN-IPETLSPKA 246
Cdd:smart00221 164 GK--------LPiRWMAPESLKE-GKFT-SKSDVWSFGVLLWEIFtLGEEPYPGMSNAEVLEYLKKGYRLpKPPNCPPEL 233

                          170       180
                   ....*....|....*....|...
gi 568977678   247 KCLIRSILRREPSERLTSQEILD 269
Cdd:smart00221 234 YKLMLQCWAEDPEDRPTFSELVE 256
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
 98-269 1.47e-11

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 63.32  E-value: 1.47e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678    98 SYGDMHSFVRTCK-KLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRV------KLESLEDAYILRGD 170
Cdd:smart00219  84 EGGDLLSYLRKNRpKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKIsdfglsRDLYDDDYYRKRGG 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678   171 DdslsdkhgCP-AYVSPEILNTsGSYSgKAADVWSLGVMLYTML-VGRYPFHDIEPSSLFSKIRRGQFN-IPETLSPKAK 247
Cdd:smart00219 164 K--------LPiRWMAPESLKE-GKFT-SKSDVWSFGVLLWEIFtLGEQPYPGMSNEEVLEYLKNGYRLpQPPNCPPELY 233

                          170       180
                   ....*....|....*....|..
gi 568977678   248 CLIRSILRREPSERLTSQEILD 269
Cdd:smart00219 234 DLMLQCWAEDPEDRPTFSELVE 255
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
 72-273 1.82e-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: 63.32  E-value: 1.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  72 LSAHSNINQITEILLGETKAYVFFERSYGDMHSFV--RTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFK 149
Cdd:cd07830   54 LNEHPNIVKLKEVFRENDELYFVFEYMEGNLYQLMkdRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVS 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 150 DEErtRVKLEsledayilrgdDDSLSDK-HGCP---AYVS------PEILNTSGSYSgKAADVWSLGVMLYTMLVGR--Y 217
Cdd:cd07830  134 GPE--VVKIA-----------DFGLAREiRSRPpytDYVStrwyraPEILLRSTSYS-SPVDIWALGCIMAELYTLRplF 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 218 P-------FHDI-------------EPSSLFSKIrrgQFNIPE-----------TLSPKAKCLIRSILRREPSERLTSQE 266
Cdd:cd07830  200 PgsseidqLYKIcsvlgtptkqdwpEGYKLASKL---GFRFPQfaptslhqlipNASPEAIDLIKDMLRWDPKKRPTASQ 276


                 ....*..
gi 568977678 267 ILDHPWF 273
Cdd:cd07830  277 ALQHPYF 283
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
 116-307 1.97e-11

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: 63.83  E-value: 1.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 116 EAARLFY--QIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDAYIlrGDDDSLSDKHGCPAYVSPEILNTSg 193
Cdd:cd05604   96 EPRARFYaaEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGI--SNSDTTTTFCGTPEYLAPEVIRKQ- 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 194 SYSgKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTS----QEILD 269
Cdd:cd05604  173 PYD-NTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLRPGISLTAWSILEELLEKDRQLRLGAkedfLEIKN 251

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 568977678 270 HPWFStdfSVSNSGFGAKEACDQLVPDVNMEE---NLDPFF 307
Cdd:cd05604  252 HPFFE---SINWTDLVQKKIPPPFNPNVNGPDdisNFDAEF 289
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
 109-271 2.08e-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: 62.71  E-value: 2.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 109 CKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTR-------VKLESLEDAYILRGDddslsdkhgcP 181
Cdd:cd14050   94 THSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKlgdfglvVELDKEDIHDAQEGD----------P 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 182 AYVSPEILNtsGSYsGKAADVWSLGVMLYTMLVgrypfhDIE-PS--SLFSKIRRGQfnIPET----LSPKAKCLIRSIL 254
Cdd:cd14050  164 RYMAPELLQ--GSF-TKAADIFSLGITILELAC------NLElPSggDGWHQLRQGY--LPEEftagLSPELRSIIKLMM 232

                        170
                 ....*....|....*..
gi 568977678 255 RREPSERLTSQEILDHP 271
Cdd:cd14050  233 DPDPERRPTAEDLLALP 249
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
 74-275 2.13e-11

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: 63.54  E-value: 2.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  74 AHSNINQITEIL-----LGETK-AYVFFERSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFI 147
Cdd:cd07855   62 KHDNIIAIRDILrpkvpYADFKdVYVVLDLMESDLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLL 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 148 FKDEERTRVKlesleDAYILRGDDDSlSDKH--------GCPAYVSPEILNTSGSYSgKAADVWSLGVMLYTMLV----- 214
Cdd:cd07855  142 VNENCELKIG-----DFGMARGLCTS-PEEHkyfmteyvATRWYRAPELMLSLPEYT-QAIDMWSVGCIFAEMLGrrqlf 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 215 -GRYPFHDIE--------PSSLF------SKIRRGQFNIP-------ETLSPKAKC----LIRSILRREPSERLTSQEIL 268
Cdd:cd07855  215 pGKNYVHQLQliltvlgtPSQAVinaigaDRVRRYIQNLPnkqpvpwETLYPKADQqaldLLSQMLRFDPSERITVAEAL 294


                 ....*..
gi 568977678 269 DHPWFST 275
Cdd:cd07855  295 QHPFLAK 301
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
 115-273 2.67e-11

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: 63.07  E-value: 2.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 115 EEAARLFY--QIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEdayILRGDDDSLSDKHGCPAYVSPEILNTS 192
Cdd:cd05632  102 EEERALFYaaEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLA---VKIPEGESIRGRVGTVGYMAPEVLNNQ 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 193 gsYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPK----AKCLIRSILRREPSERLTSQ--- 265
Cdd:cd05632  179 --RYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVDRRVLETEEVYSAKfseeAKSICKMLLTKDPKQRLGCQeeg 256

                        170
                 ....*....|
gi 568977678 266 --EILDHPWF 273
Cdd:cd05632  257 agEVKRHPFF 266
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
 112-273 2.74e-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: 62.68  E-value: 2.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 112 LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKfIFKDEERTR--VKLESLEDAYILrgddDSLSDKH---GCPAYVSP 186
Cdd:cd14113  100 LTEEKIRFYLREILEALQYLHNCRIAHLDLKPEN-ILVDQSLSKptIKLADFGDAVQL----NTTYYIHqllGSPEFAAP 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 187 EILntSGSYSGKAADVWSLGVMLYTMLVGRYPFHD--IEPSSLfsKIRRGQFNIPET----LSPKAKCLIRSILRREPSE 260
Cdd:cd14113  175 EII--LGNPVSLTSDLWSIGVLTYVLLSGVSPFLDesVEETCL--NICRLDFSFPDDyfkgVSQKAKDFVCFLLQMDPAK 250

                        170
                 ....*....|...
gi 568977678 261 RLTSQEILDHPWF 273
Cdd:cd14113  251 RPSAALCLQEQWL 263
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
 179-274 3.03e-11

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: 63.36  E-value: 3.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 179 GCPAYVSPEILNTSGSysGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGqfNIP-----ETLSPKAKCLIRSI 253
Cdd:cd05610  219 GTPDYLAPELLLGKPH--GPAVDWWALGVCLFEFLTGIPPFNDETPQQVFQNILNR--DIPwpegeEELSVNAQNAIEIL 294

                         90       100
                 ....*....|....*....|.
gi 568977678 254 LRREPSERLTSQEILDHPWFS 274
Cdd:cd05610  295 LTMDPTKRAGLKELKQHPLFH 315
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
 111-272 3.08e-11

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: 62.65  E-value: 3.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 111 KLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEerTRVKLESLEDAYILRgddDSLSDKH---GCPAYVSPE 187
Cdd:cd06609   94 PLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEE--GDVKLADFGVSGQLT---STMSKRNtfvGTPFWMAPE 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 188 ILNTSGsYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRgqfNIPETL-----SPKAKCLIRSILRREPSERL 262
Cdd:cd06609  169 VIKQSG-YDEKA-DIWSLGITAIELAKGEPPLSDLHPMRVLFLIPK---NNPPSLegnkfSKPFKDFVELCLNKDPKERP 243

                        170
                 ....*....|
gi 568977678 263 TSQEILDHPW 272
Cdd:cd06609  244 SAKELLKHKF 253
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
 122-273 5.08e-11

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: 62.06  E-value: 5.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 122 YQIASAVAHCHDGGLVLRDLKLRKfIFKDEERTRVKLESLEDAYILR----GDDDSLSDKHGCPAYVSPEILNtsGSYSG 197
Cdd:cd06630  110 LQILRGLAYLHDNQIIHRDLKGAN-LLVDSTGQRLRIADFGAAARLAskgtGAGEFQGQLLGTIAFMAPEVLR--GEQYG 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 198 KAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRR-----GQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd06630  187 RSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIFKiasatTPPPIPEHLSPGLRDVTLRCLELQPEDRPPARELLKHPV 266


                 .
gi 568977678 273 F 273
Cdd:cd06630  267 F 267
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
 111-272 5.39e-11

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: 61.85  E-value: 5.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 111 KLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLES--LEDAYILRgddDSLSDKHGCPAYVSPEI 188
Cdd:cd14193   98 NLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSREANQVKIIDfgLARRYKPR---EKLRVNFGTPEFLAPEV 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 189 LNTSgsYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPET----LSPKAKCLIRSILRREPSERLTS 264
Cdd:cd14193  175 VNYE--FVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFEDEefadISEEAKDFISKLLIKEKSWRMSA 252


                 ....*...
gi 568977678 265 QEILDHPW 272
Cdd:cd14193  253 SEALKHPW 260
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
 75-273 5.97e-11

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 62.14  E-value: 5.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFERSYGDMHSFVRTCKKL-REEEAARLF-YQIASAVAHCHDGGLVLRDLKLRKFIFkDEE 152
Cdd:PLN00009  60 HGNIVRLQDVVHSEKRLYLVFEYLDLDLKKHMDSSPDFaKNPRLIKTYlYQILRGIAYCHSHRVLHRDLKPQNLLI-DRR 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 153 RTRVKLEsledayilrgdDDSLSDKHGCPA-----------YVSPEILNTSGSYSgKAADVWSLGVMLYTMLVGRYPF-H 220
Cdd:PLN00009 139 TNALKLA-----------DFGLARAFGIPVrtfthevvtlwYRAPEILLGSRHYS-TPVDIWSVGCIFAEMVNQKPLFpG 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 221 DIEPSSLFSKIR----------RGQFNIPE------------------TLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:PLN00009 207 DSEIDELFKIFRilgtpneetwPGVTSLPDyksafpkwppkdlatvvpTLEPAGVDLLSKMLRLDPSKRITARAALEHEY 286


                 .
gi 568977678 273 F 273
Cdd:PLN00009 287 F 287
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
 179-273 6.70e-11

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: 61.59  E-value: 6.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 179 GCPAYVSPEILNtSGSYSGKAaDVWSLGVMLYTMLVGRYPF--HDIEPS----SLFSKIRRGQfniPETL-----SPKAK 247
Cdd:cd06605  160 GTRSYMAPERIS-GGKYTVKS-DIWSLGLSLVELATGRFPYppPNAKPSmmifELLSYIVDEP---PPLLpsgkfSPDFQ 234

                         90       100
                 ....*....|....*....|....*.
gi 568977678 248 CLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd06605  235 DFVSQCLQKDPTERPSYKELMEHPFI 260
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
 179-276 6.97e-11

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 61.79  E-value: 6.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 179 GCPAYVSPEIL-----NTSGSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPSSLFSK---IRRGQ-FNIPETLSPKAKCL 249
Cdd:cd06622  163 GCQSYMAPERIksggpNQNPTYTVQS-DVWSLGLSILEMALGRYPYPPETYANIFAQlsaIVDGDpPTLPSGYSDDAQDF 241

                         90       100
                 ....*....|....*....|....*..
gi 568977678 250 IRSILRREPSERLTSQEILDHPWFSTD 276
Cdd:cd06622  242 VAKCLNKIPNRRPTYAQLLEHPWLVKY 268
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
 106-275 8.52e-11

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: 61.34  E-value: 8.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 106 VRTCKK---LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERtrVKLESLEDAYILRGDDDSLSDKHGCPA 182
Cdd:cd06917   89 IRTLMRagpIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGN--VKLCDFGVAASLNQNSSKRSTFVGTPY 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 183 YVSPEILNTSGSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPS---SLFSKIRRGQFNIpETLSPKAKCLIRSILRREPS 259
Cdd:cd06917  167 WMAPEVITEGKYYDTKA-DIWSLGITTYEMATGNPPYSDVDALravMLIPKSKPPRLEG-NGYSPLLKEFVAACLDEEPK 244

                        170
                 ....*....|....*.
gi 568977678 260 ERLTSQEILDHPWFST 275
Cdd:cd06917  245 DRLSADELLKSKWIKQ 260
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
 99-270 8.83e-11

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 60.97  E-value: 8.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678   99 YGDMHSFVRTCK-KLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKfIFKDEERTrVKLEsleD---AYILRGDDDSL 174
Cdd:pfam07714  85 GGDLLDFLRKHKrKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARN-CLVSENLV-VKIS---DfglSRDIYDDDYYR 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  175 SDKHG--CPAYVSPEILNTsGSYSGKAaDVWSLGVMLYTML-VGRYPFHDIEPSSLFSKIRRG-QFNIPETLSPKAKCLI 250
Cdd:pfam07714 160 KRGGGklPIKWMAPESLKD-GKFTSKS-DVWSFGVLLWEIFtLGEQPYPGMSNEEVLEFLEDGyRLPQPENCPDELYDLM 237

                         170       180
                  ....*....|....*....|
gi 568977678  251 RSILRREPSERLTSQEILDH 270
Cdd:pfam07714 238 KQCWAYDPEDRPTFSELVED 257
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
 51-274 9.76e-11

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: 61.30  E-value: 9.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  51 EIPGHVFEIscyqESLAPCfclsAHSNINQITEILLGETKAYVFFER-SYGDMHSF-VRTCKKLREEEAARLFYQIASAV 128
Cdd:cd06611   45 ELEDFMVEI----DILSEC----KHPNIVGLYEAYFYENKLWILIEFcDGGALDSImLELERGLTEPQIRYVCRQMLEAL 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 129 AHCHDGGLVLRDLKLRKFIFKDEerTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNT----SGSYSGKAaDVWS 204
Cdd:cd06611  117 NFLHSHKVIHRDLKAGNILLTLD--GDVKLADFGVSAKNKSTLQKRDTFIGTPYWMAPEVVACetfkDNPYDYKA-DIWS 193

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568977678 205 LGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQ---FNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPWFS 274
Cdd:cd06611  194 LGITLIELAQMEPPHHELNPMRVLLKILKSEpptLDQPSKWSSSFNDFLKSCLVKDPDDRPTAAELLKHPFVS 266
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
 115-274 1.85e-10

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: 60.80  E-value: 1.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 115 EEAARLFY-QIASAVAHCHDGGLVLRDLKLRKFIFKDEERTrvkleSLEDAYILRGD---DDSLSDKHGCPAYVSPEILN 190
Cdd:cd05602  107 EPRARFYAaEIASALGYLHSLNIVYRDLKPENILLDSQGHI-----VLTDFGLCKENiepNGTTSTFCGTPEYLAPEVLH 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 191 TSgSYSgKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQ----E 266
Cdd:cd05602  182 KQ-PYD-RTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSARHLLEGLLQKDRTKRLGAKddftE 259


                 ....*...
gi 568977678 267 ILDHPWFS 274
Cdd:cd05602  260 IKNHIFFS 267
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
 100-274 1.87e-10

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: 60.82  E-value: 1.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRtCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKlesleDAYILRGDDDSLSDKHG 179
Cdd:cd07877  106 ADLNNIVK-CQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKIL-----DFGLARHTDDEMTGYVA 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 180 CPAYVSPEILNTSGSYSgKAADVWSLGVMLYTMLVGR--YPFHD-------------IEPSSLFSKI------------- 231
Cdd:cd07877  180 TRWYRAPEIMLNWMHYN-QTVDIWSVGCIMAELLTGRtlFPGTDhidqlklilrlvgTPGAELLKKIssesarnyiqslt 258

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568977678 232 ---RRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPWFS 274
Cdd:cd07877  259 qmpKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHAYFA 304
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
 91-272 2.00e-10

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: 60.24  E-value: 2.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  91 AYVFFERSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDAYILRGD 170
Cdd:cd14112   75 AYLVMEKLQEDVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSWQVKLVDFGRAQKVSKL 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 171 DDSLSDkhGCPAYVSPEILNTSGSYSGKaADVWSLGVMLYTMLVGRYPF-------HDIEPSSLFSKIRRGqfNIPETLS 243
Cdd:cd14112  155 GKVPVD--GDTDWASPEFHNPETPITVQ-SDIWGLGVLTFCLLSGFHPFtseyddeEETKENVIFVKCRPN--LIFVEAT 229

                        170       180
                 ....*....|....*....|....*....
gi 568977678 244 PKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd14112  230 QEALRFATWALKKSPTRRMRTDEALEHRW 258
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 75-261 2.35e-10

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: 60.04  E-value: 2.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFE-RSYGDMHSFVRTCKKLR----EEEAARLFYQIASAVAHCHDGGLVLRDLK-LRKFIF 148
Cdd:cd08228   61 HPNVIKYLDSFIEDNELNIVLElADAGDLSQMIKYFKKQKrlipERTVWKYFVQLCSAVEHMHSRRVMHRDIKpANVFIT 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 149 KDEErtrVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSGsYSGKAaDVWSLGVMLYTMLVGRYPFHDiEPSSLF 228
Cdd:cd08228  141 ATGV---VKLGDLGLGRFFSSKTTAAHSLVGTPYYMSPERIHENG-YNFKS-DIWSLGCLLYEMAALQSPFYG-DKMNLF 214

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568977678 229 S---KIRRGQF-NIP-ETLSPKAKCLIRSILRREPSER 261
Cdd:cd08228  215 SlcqKIEQCDYpPLPtEHYSEKLRELVSMCIYPDPDQR 252
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
 114-270 2.36e-10

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: 60.00  E-value: 2.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 114 EEEAARLFYQIASAVAHCHDGGLV---LRDLKLRKFIFKDEER-----------TRVKLESLEDAyILRGDDDSlsdKHG 179
Cdd:cd13986  105 EDRILHIFLGICRGLKAMHEPELVpyaHRDIKPGNVLLSEDDEpilmdlgsmnpARIEIEGRREA-LALQDWAA---EHC 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 180 CPAYVSPEILNT-SGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPS--SLFSKIRRGQFNIPET--LSPKAKCLIRSIL 254
Cdd:cd13986  181 TMPYRAPELFDVkSHCTIDEKTDIWSLGCTLYALMYGESPFERIFQKgdSLALAVLSGNYSFPDNsrYSEELHQLVKSML 260

                        170
                 ....*....|....*.
gi 568977678 255 RREPSERLTSQEILDH 270
Cdd:cd13986  261 VVNPAERPSIDDLLSR 276
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
 75-273 2.49e-10

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: 60.19  E-value: 2.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFERSYGDMHSFVRTCKKLREEEA--ARLF-YQIASAVAHCHDGGLVLRDLKLRKFIFKde 151
Cdd:cd07836   57 HENIVRLHDVIHTENKLMLVFEYMDKDLKKYMDTHGVRGALDPntVKSFtYQLLKGIAFCHENRVLHRDLKPQNLLIN-- 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 152 ERTRVKLEsledayilrgdDDSLSDKHGCPA-----------YVSPEILNTSGSYSgKAADVWSLGVMLYTMLVGRYPF- 219
Cdd:cd07836  135 KRGELKLA-----------DFGLARAFGIPVntfsnevvtlwYRAPDVLLGSRTYS-TSIDIWSVGCIMAEMITGRPLFp 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 220 --------------------HDIEPSSLFSKIRRG---------QFNIPeTLSPKAKCLIRSILRREPSERLTSQEILDH 270
Cdd:cd07836  203 gtnnedqllkifrimgtpteSTWPGISQLPEYKPTfpryppqdlQQLFP-HADPLGIDLLHRLLQLNPELRISAHDALQH 281


                 ...
gi 568977678 271 PWF 273
Cdd:cd07836  282 PWF 284
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
 47-273 2.72e-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: 60.02  E-value: 2.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  47 RARSEIPGHVF---EISCYQESLAPCFCLS--------AHSNINQITEILLGETKAYVFFERSYGDMHSFVRTCKKLREE 115
Cdd:cd07871   23 KGRSKLTENLValkEIRLEHEEGAPCTAIRevsllknlKHANIVTLHDIIHTERCLTLVFEYLDSDLKQYLDNCGNLMSM 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 116 EAARLF-YQIASAVAHCHDGGLVLRDLKLRKFIFKdeERTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSGS 194
Cdd:cd07871  103 HNVKIFmFQLLRGLSYCHKRKILHRDLKPQNLLIN--EKGELKLADFGLARAKSVPTKTYSNEVVTLWYRPPDVLLGSTE 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 195 YSgKAADVWSLGVMLYTMLVGR--------------------YPFHDIEPS-SLFSKIRRGQF---------NIPETLSP 244
Cdd:cd07871  181 YS-TPIDMWGVGCILYEMATGRpmfpgstvkeelhlifrllgTPTEETWPGvTSNEEFRSYLFpqyraqpliNHAPRLDT 259

                        250       260
                 ....*....|....*....|....*....
gi 568977678 245 KAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd07871  260 DGIDLLSSLLLYETKSRISAEAALRHSYF 288
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
 100-274 2.76e-10

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 59.87  E-value: 2.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFkDEERTRVKL-----------ESLEDayilr 168
Cdd:PHA03390  94 GDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLY-DRAKDRIYLcdyglckiigtPSCYD----- 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 169 gdddslsdkhGCPAYVSPE-ILNTSGSYSgkaADVWSLGVMLYTMLVGRYPF-----HDIEPSSLFSKIRRgQFNIPETL 242
Cdd:PHA03390 168 ----------GTLDYFSPEkIKGHNYDVS---FDWWAVGVLTYELLTGKHPFkededEELDLESLLKRQQK-KLPFIKNV 233

                        170       180       190
                 ....*....|....*....|....*....|...
gi 568977678 243 SPKAKCLIRSILRREPSERLTS-QEILDHPWFS 274
Cdd:PHA03390 234 SKNANDFVQSMLKYNINYRLTNyNEIIKHPFLK 266
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
 100-275 3.15e-10

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: 60.06  E-value: 3.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDAYILRGDDDSLsdkhG 179
Cdd:cd14223   88 GDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDFSKKKPHASV----G 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 180 CPAYVSPEILNTSGSYSgKAADVWSLGVMLYTMLVGRYPF--------HDIEPSSLFSKIRrgqfnIPETLSPKAKCLIR 251
Cdd:cd14223  164 THGYMAPEVLQKGVAYD-SSADWFSLGCMLFKLLRGHSPFrqhktkdkHEIDRMTLTMAVE-----LPDSFSPELRSLLE 237

                        170       180
                 ....*....|....*....|....*....
gi 568977678 252 SILRREPSERL-----TSQEILDHPWFST 275
Cdd:cd14223  238 GLLQRDVNRRLgcmgrGAQEVKEEPFFRG 266
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 75-261 3.23e-10

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: 59.44  E-value: 3.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFE----RSYGDMHSFVRTCK-KLREEEAARLFYQIASAVAHCH-DGGLVLRDLKLRKFIF 148
Cdd:cd08528   68 HPNIVRYYKTFLENDRLYIVMEliegAPLGEHFSSLKEKNeHFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIML 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 149 KDEERTRVKLESLedAYILRGDDDSLSDKHGCPAYVSPEILNtSGSYsGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLF 228
Cdd:cd08528  148 GEDDKVTITDFGL--AKQKGPESSKMTSVVGTILYSCPEIVQ-NEPY-GEKADIWALGCILYQMCTLQPPFYSTNMLTLA 223

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568977678 229 SKIRRGQFN-IPETL-SPKAKCLIRSILRREPSER 261
Cdd:cd08528  224 TKIVEAEYEpLPEGMySDDITFVIRSCLTPDPEAR 258
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
 114-273 3.60e-10

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: 59.15  E-value: 3.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 114 EEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDAYILRGDDDSLSdKHGCPAYVSPEILNTSG 193
Cdd:cd14108   96 ESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTDQVRICDFGNAQELTPNEPQYC-KYGTPEFVAPEIVNQSP 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 194 SysGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPET----LSPKAKCLIRSILRREpSERLTSQEILD 269
Cdd:cd14108  175 V--SKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYNVAFEESmfkdLCREAKGFIIKVLVSD-RLRPDAEETLE 251


                 ....
gi 568977678 270 HPWF 273
Cdd:cd14108  252 HPWF 255
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
 115-274 3.77e-10

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: 59.79  E-value: 3.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 115 EEAARLF-YQIASAVAHCHDGGLVLRDLKLRKfIFKDEERTRVKLESLEDAYILRGD---DDSLSDKHGCPAYVSPEILN 190
Cdd:cd07854  113 EEHARLFmYQLLRGLKYIHSANVLHRDLKPAN-VFINTEDLVLKIGDFGLARIVDPHyshKGYLSEGLVTKWYRSPRLLL 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 191 TSGSYSgKAADVWSLGVMLYTMLVGRYPF---HDIEPSSLF---------------------------SKIRRGQFNIPE 240
Cdd:cd07854  192 SPNNYT-KAIDMWAAGCIFAEMLTGKPLFagaHELEQMQLIlesvpvvreedrnellnvipsfvrndgGEPRRPLRDLLP 270

                        170       180       190
                 ....*....|....*....|....*....|....
gi 568977678 241 TLSPKAKCLIRSILRREPSERLTSQEILDHPWFS 274
Cdd:cd07854  271 GVNPEALDFLEQILTFNPMDRLTAEEALMHPYMS 304
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
 58-273 6.33e-10

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: 58.86  E-value: 6.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  58 EISCYQESLAPCFCLS--------AHSNINQITEILLGETKAYVFFERSYGDMHSFVRTCKKLREEEAARLF-YQIASAV 128
Cdd:cd07873   34 EIRLEHEEGAPCTAIRevsllkdlKHANIVTLHDIIHTEKSLTLVFEYLDKDLKQYLDDCGNSINMHNVKLFlFQLLRGL 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 129 AHCHDGGLVLRDLKLRKFIFKdeERTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSGSYSGKaADVWSLGVM 208
Cdd:cd07873  114 AYCHRRKVLHRDLKPQNLLIN--ERGELKLADFGLARAKSIPTKTYSNEVVTLWYRPPDILLGSTDYSTQ-IDMWGVGCI 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 209 LYTMLVGR--YPFHDIE------------PSS-----LFSKIRRGQFNIPE-----------TLSPKAKCLIRSILRREP 258
Cdd:cd07873  191 FYEMSTGRplFPGSTVEeqlhfifrilgtPTEetwpgILSNEEFKSYNYPKyradalhnhapRLDSDGADLLSKLLQFEG 270

                        250
                 ....*....|....*
gi 568977678 259 SERLTSQEILDHPWF 273
Cdd:cd07873  271 RKRISAEEAMKHPYF 285
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
 75-270 6.38e-10

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 60.14  E-value: 6.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678   75 HSNINQITEILLGET--KAYVFFER-SYGDMHSFVRTCKKL----REEEAARLFYQIASAVAHCHD------GGLVL-RD 140
Cdd:PTZ00266   71 HKNIVRYIDRFLNKAnqKLYILMEFcDAGDLSRNIQKCYKMfgkiEEHAIVDITRQLLHALAYCHNlkdgpnGERVLhRD 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  141 LKLRKFIFKDEERTRVKL----ESLEDAYILRGDDDSLSDK-------HGC---PAYVSPEIL-NTSGSYSGKAaDVWSL 205
Cdd:PTZ00266  151 LKPQNIFLSTGIRHIGKItaqaNNLNGRPIAKIGDFGLSKNigiesmaHSCvgtPYYWSPELLlHETKSYDDKS-DMWAL 229

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568977678  206 GVMLYTMLVGRYPFHDIEP-SSLFSKIRRGQfNIP-ETLSPKAKCLIRSILRREPSERLTSQEILDH 270
Cdd:PTZ00266  230 GCIIYELCSGKTPFHKANNfSQLISELKRGP-DLPiKGKSKELNILIKNLLNLSAKERPSALQCLGY 295
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
 110-272 6.71e-10

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: 58.85  E-value: 6.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 110 KKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEerTRVKLEsleDAYILRGDDDSLSDKH---GCPAYVSP 186
Cdd:cd06608  108 KRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEE--AEVKLV---DFGVSAQLDSTLGRRNtfiGTPYWMAP 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 187 EIL----NTSGSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRgqfNIPETLSPKAKC------LIRSILRR 256
Cdd:cd06608  183 EVIacdqQPDASYDARC-DVWSLGITAIELADGKPPLCDMHPMRALFKIPR---NPPPTLKSPEKWskefndFISECLIK 258

                        170
                 ....*....|....*.
gi 568977678 257 EPSERLTSQEILDHPW 272
Cdd:cd06608  259 NYEQRPFTEELLEHPF 274
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
 179-272 7.12e-10

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: 58.92  E-value: 7.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 179 GCPAYVSPEIL--NTSGSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPS-SLFSKIRrgQFNIP-----ETLSPKAKCLI 250
Cdd:cd06618  176 GCAAYMAPERIdpPDNPKYDIRA-DVWSLGISLVELATGQFPYRNCKTEfEVLTKIL--NEEPPslppnEGFSPDFCSFV 252

                         90       100
                 ....*....|....*....|..
gi 568977678 251 RSILRREPSERLTSQEILDHPW 272
Cdd:cd06618  253 DLCLTKDHRYRPKYRELLQHPF 274
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
 46-279 7.18e-10

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: 58.89  E-value: 7.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  46 SRARSEIPGHVFEIscyqESLAPCfclsAHSNINQITEILLGETKAYVFFERSYGDM--HSFVRTCKKLREEEAARLFYQ 123
Cdd:cd06644   47 TKSEEELEDYMVEI----EILATC----NHPYIVKLLGAFYWDGKLWIMIEFCPGGAvdAIMLELDRGLTEPQIQVICRQ 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 124 IASAVAHCHDGGLVLRDLKLRKFIFKDEerTRVKLE----SLEDAYILRGDDDSLsdkhGCPAYVSPEIL------NTSG 193
Cdd:cd06644  119 MLEALQYLHSMKIIHRDLKAGNVLLTLD--GDIKLAdfgvSAKNVKTLQRRDSFI----GTPYWMAPEVVmcetmkDTPY 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 194 SYSgkaADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQ---FNIPETLSPKAKCLIRSILRREPSERLTSQEILDH 270
Cdd:cd06644  193 DYK---ADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEpptLSQPSKWSMEFRDFLKTALDKHPETRPSAAQLLEH 269


                 ....*....
gi 568977678 271 PWFSTDFSV 279
Cdd:cd06644  270 PFVSSVTSN 278
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
 100-274 7.63e-10

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: 59.26  E-value: 7.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCKKLREEEAARLFY-QIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVK-----LESLEDAYIlrgdddS 173
Cdd:cd05623  157 GDLLTLLSKFEDRLPEDMARFYLaEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLAdfgscLKLMEDGTV------Q 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 174 LSDKHGCPAYVSPEILNT----SGSYsGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKI--RRGQFNIPETL---SP 244
Cdd:cd05623  231 SSVAVGTPDYISPEILQAmedgKGKY-GPECDWWSLGVCMYEMLYGETPFYAESLVETYGKImnHKERFQFPTQVtdvSE 309

                        170       180       190
                 ....*....|....*....|....*....|....
gi 568977678 245 KAKCLIRS-ILRREpsERLTSQEILD---HPWFS 274
Cdd:cd05623  310 NAKDLIRRlICSRE--HRLGQNGIEDfknHPFFV 341
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
 75-273 7.79e-10

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: 58.67  E-value: 7.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFERSYGDMHSFVRTCKK--LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFkdEE 152
Cdd:cd07860   58 HPNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALtgIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLI--NT 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 153 RTRVKLEsledayilrgdDDSLSDKHGCPA-----------YVSPEILNTSGSYSgKAADVWSLGVMLYTMLVGRYPF-H 220
Cdd:cd07860  136 EGAIKLA-----------DFGLARAFGVPVrtythevvtlwYRAPEILLGCKYYS-TAVDIWSLGCIFAEMVTRRALFpG 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 221 DIEPSSLFSKIRR----------GQFNIPE------------------TLSPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd07860  204 DSEIDQLFRIFRTlgtpdevvwpGVTSMPDykpsfpkwarqdfskvvpPLDEDGRDLLSQMLHYDPNKRISAKAALAHPF 283


                 .
gi 568977678 273 F 273
Cdd:cd07860  284 F 284
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
 75-273 8.97e-10

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: 58.01  E-value: 8.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGetkayvffersyGDMHSFVRTCKKLREEEAARLFYQIASAVA--HCHDGGLVLRDLKLRKfIFKDEE 152
Cdd:cd13983   74 KKEVIFITELMTS------------GTLKQYLKRFKRLKLKVIKSWCRQILEGLNylHTRDPPIIHRDLKCDN-IFINGN 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 153 RTRVKLESLEDAYILRGdddslSDKH---GCPAYVSPEILntSGSYsGKAADVWSLGVMLYTMLVGRYPFHD-IEPSSLF 228
Cdd:cd13983  141 TGEVKIGDLGLATLLRQ-----SFAKsviGTPEFMAPEMY--EEHY-DEKVDIYAFGMCLLEMATGEYPYSEcTNAAQIY 212

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568977678 229 SKIRRGQFniPETLS----PKAKCLIRSILRRePSERLTSQEILDHPWF 273
Cdd:cd13983  213 KKVTSGIK--PESLSkvkdPELKDFIEKCLKP-PDERPSARELLEHPFF 258
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
 92-274 9.09e-10

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: 58.89  E-value: 9.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  92 YVFFERSY---GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIF-------------------- 148
Cdd:cd05600   85 NVYLAMEYvpgGDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIdssghikltdfglasgtlsp 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 149 KDEERTRVKLESLEDAY-----------ILRGDDDSLSDKH----GCPAYVSPEILNTSGsYSgKAADVWSLGVMLYTML 213
Cdd:cd05600  165 KKIESMKIRLEEVKNTAfleltakerrnIYRAMRKEDQNYAnsvvGSPDYMAPEVLRGEG-YD-LTVDYWSLGCILFECL 242

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568977678 214 VGRYPFHDIEPSSLFSKIRR--------------GQFNIP-ETLSPKAKCLIrsilrrEPSERLTS-QEILDHPWFS 274
Cdd:cd05600  243 VGFPPFSGSTPNETWANLYHwkktlqrpvytdpdLEFNLSdEAWDLITKLIT------DPQDRLQSpEQIKNHPFFK 313
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
 98-270 1.01e-09

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: 57.93  E-value: 1.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  98 SYGDMHSFVRTCKKLREEEAARLF---------YQIASAVAHCHDGGLVLRDLKLRKfIFKDEERTrVKLeS----LEDA 164
Cdd:cd00192   79 EGGDLLDFLRKSRPVFPSPEPSTLslkdllsfaIQIAKGMEYLASKKFVHRDLAARN-CLVGEDLV-VKI-SdfglSRDI 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 165 YilrgDDDSLSDKHGCPAYV---SPEILNTsGSYSGKaADVWSLGVMLYTMLV-GRYPFHDIEPSSLFSKIRRGQF-NIP 239
Cdd:cd00192  156 Y----DDDYYRKKTGGKLPIrwmAPESLKD-GIFTSK-SDVWSFGVLLWEIFTlGATPYPGLSNEEVLEYLRKGYRlPKP 229

                        170       180       190
                 ....*....|....*....|....*....|.
gi 568977678 240 ETLSPKAKCLIRSILRREPSERLTSQEILDH 270
Cdd:cd00192  230 ENCPDELYELMLSCWQLDPEDRPTFSELVER 260
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
 75-273 1.24e-09

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: 58.20  E-value: 1.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFErsYGDmHSFV----RTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFkd 150
Cdd:cd07846   59 HENLVNLIEVFRRKKRWYLVFE--FVD-HTVLddleKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILV-- 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 151 EERTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSGSYsGKAADVWSLGVMLYTMLVGRYPF---HDIE---- 223
Cdd:cd07846  134 SQSGVVKLCDFGFARTLAAPGEVYTDYVATRWYRAPELLVGDTKY-GKAVDVWAVGCLVTEMLTGEPLFpgdSDIDqlyh 212

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568977678 224 -----------------PSSLFSKIRRGQFNIPE-------TLSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd07846  213 iikclgnliprhqelfqKNPLFAGVRLPEVKEVEplerrypKLSGVVIDLAKKCLHIDPDKRPSCSELLHHEFF 286
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
 179-278 1.51e-09

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: 58.52  E-value: 1.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 179 GCPAYVSPEILNTSGsYSgKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQ--FNIP--ETLSPKAKCLIRSiL 254
Cdd:cd05625  210 GTPNYIAPEVLLRTG-YT-QLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQtsLHIPpqAKLSPEASDLIIK-L 286

                         90       100
                 ....*....|....*....|....*...
gi 568977678 255 RREPSERLTSQ---EILDHPWFST-DFS 278
Cdd:cd05625  287 CRGPEDRLGKNgadEIKAHPFFKTiDFS 314
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
 115-273 1.53e-09

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: 57.70  E-value: 1.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 115 EEAARLFY--QIASAVAHCHDGGLVLRDLKLRKFIFKDeeRTRVKLESLEDAYILRgDDDSLSDKHGCPAYVSPEILNTS 192
Cdd:cd05631  100 DEQRAIFYaaELCCGLEDLQRERIVYRDLKPENILLDD--RGHIRISDLGLAVQIP-EGETVRGRVGTVGYMAPEVINNE 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 193 gSYSgKAADVWSLGVMLYTMLVGRYPF----HDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERL-----T 263
Cdd:cd05631  177 -KYT-FSPDWWGLGCLIYEMIQGQSPFrkrkERVKREEVDRRVKEDQEEYSEKFSEDAKSICRMLLTKNPKERLgcrgnG 254

                        170
                 ....*....|
gi 568977678 264 SQEILDHPWF 273
Cdd:cd05631  255 AAGVKQHPIF 264
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
 123-269 2.70e-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: 2.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 123 QIASAVAHCHDGG---LVLRDLKLrKFIFKDEertRVKLESLEDAyILRGDDDSLSDKH---------GCPAYVSPEILN 190
Cdd:cd14061  100 QIARGMNYLHNEApvpIIHRDLKS-SNILILE---AIENEDLENK-TLKITDFGLAREWhkttrmsaaGTYAWMAPEVIK 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 191 TSgSYSgKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFN--IPETLSPKAKCLIRSILRREPSERLTSQEIL 268
Cdd:cd14061  175 SS-TFS-KASDVWSYGVLLWELLTGEVPYKGIDGLAVAYGVAVNKLTlpIPSTCPEPFAQLMKDCWQPDPHDRPSFADIL 252


                 .
gi 568977678 269 D 269
Cdd:cd14061  253 K 253
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
 100-272 3.26e-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: 57.04  E-value: 3.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCK--KLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKdeERTRVKLESLEDAYILrgdDDSLSDK 177
Cdd:cd06637   94 GSVTDLIKNTKgnTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLT--ENAEVKLVDFGVSAQL---DRTVGRR 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 178 H---GCPAYVSPEIL----NTSGSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPsslfskiRRGQFNIPETLSPKAK--- 247
Cdd:cd06637  169 NtfiGTPYWMAPEVIacdeNPDATYDFKS-DLWSLGITAIEMAEGAPPLCDMHP-------MRALFLIPRNPAPRLKskk 240

                        170       180       190
                 ....*....|....*....|....*....|.
gi 568977678 248 ------CLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd06637  241 wskkfqSFIESCLVKNHSQRPSTEQLMKHPF 271
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
 78-273 4.91e-09

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: 56.27  E-value: 4.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  78 INQITEILLGEtKAYVFFERSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEerTRVK 157
Cdd:cd06655   79 VNFLDSFLVGD-ELFVVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMD--GSVK 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 158 LESLEDAYILRGDDDSLSDKHGCPAYVSPEILnTSGSYsGKAADVWSLGVMLYTMLVGRYPFHDIEP-SSLFSKIRRG-- 234
Cdd:cd06655  156 LTDFGFCAQITPEQSKRSTMVGTPYWMAPEVV-TRKAY-GPKVDIWSLGIMAIEMVEGEPPYLNENPlRALYLIATNGtp 233

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568977678 235 QFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd06655  234 ELQNPEKLSPIFRDFLNRCLEMDVEKRGSAKELLQHPFL 272
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
 123-273 5.00e-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: 5.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 123 QIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLesledayILRGDDDSLSDkhGCPAYV------SPEILntSGSYS 196
Cdd:cd14133  110 QILEALVFLHSLGLIHCDLKPENILLASYSRCQIKI-------IDFGSSCFLTQ--RLYSYIqsryyrAPEVI--LGLPY 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 197 GKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKC-------LIRSILRREPSERLTSQEILD 269
Cdd:cd14133  179 DEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPAHMLDQGKAddelfvdFLKKLLEIDPKERPTASQALS 258


                 ....
gi 568977678 270 HPWF 273
Cdd:cd14133  259 HPWL 262
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
 58-275 5.64e-09

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: 56.15  E-value: 5.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  58 EISCYQESLAPCFCLS--------AHSNINQITEILLGETKAYVFFERSYGDMHSFVRTCKKLREEEAARLF-YQIASAV 128
Cdd:cd07872   38 EIRLEHEEGAPCTAIRevsllkdlKHANIVTLHDIVHTDKSLTLVFEYLDKDLKQYMDDCGNIMSMHNVKIFlYQILRGL 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 129 AHCHDGGLVLRDLKLRKFIFKdeERTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSGSYSGKaADVWSLGVM 208
Cdd:cd07872  118 AYCHRRKVLHRDLKPQNLLIN--ERGELKLADFGLARAKSVPTKTYSNEVVTLWYRPPDVLLGSSEYSTQ-IDMWGVGCI 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 209 LYTMLVGR--YPFHDIE------------PSS-----LFSKIRRGQFNIPE-----------TLSPKAKCLIRSILRREP 258
Cdd:cd07872  195 FFEMASGRplFPGSTVEdelhlifrllgtPTEetwpgISSNDEFKNYNFPKykpqplinhapRLDTEGIELLTKFLQYES 274

                        250
                 ....*....|....*..
gi 568977678 259 SERLTSQEILDHPWFST 275
Cdd:cd07872  275 KKRISAEEAMKHAYFRS 291
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
 100-274 6.59e-09

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: 56.56  E-value: 6.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCKKLREEEAARlFY--QIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVK-----LESLEDAYIlrgddd 172
Cdd:cd05624  157 GDLLTLLSKFEDKLPEDMAR-FYigEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLAdfgscLKMNDDGTV------ 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 173 SLSDKHGCPAYVSPEILNTS----GSYsGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKI--RRGQFNIPE---TLS 243
Cdd:cd05624  230 QSSVAVGTPDYISPEILQAMedgmGKY-GPECDWWSLGVCMYEMLYGETPFYAESLVETYGKImnHEERFQFPShvtDVS 308

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568977678 244 PKAKCLI-RSILRREpsERLTSQEILD---HPWFS 274
Cdd:cd05624  309 EEAKDLIqRLICSRE--RRLGQNGIEDfkkHAFFE 341
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
 101-272 8.59e-09

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: 55.40  E-value: 8.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 101 DMHSFVRTCKKLREEEAARLFYQIASAVAHC--HDGGLVLRDLKLRKFIFKDEERT-RVKLESLEDAYILRGDDDSL--- 174
Cdd:cd13990   91 DLDFYLKQHKSIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHSGNVSgEIKITDFGLSKIMDDESYNSdgm 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 175 ---SDKHGCPAYVSPEILNTSG---SYSGKAaDVWSLGVMLYTMLVGRYPF-HDIEPSS-LFSKI----RRGQFNIPETL 242
Cdd:cd13990  171 eltSQGAGTYWYLPPECFVVGKtppKISSKV-DVWSVGVIFYQMLYGRKPFgHNQSQEAiLEENTilkaTEVEFPSKPVV 249

                        170       180       190
                 ....*....|....*....|....*....|
gi 568977678 243 SPKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd13990  250 SSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
 75-273 8.83e-09

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: 55.32  E-value: 8.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNI-NQITEILLGEtKAYVFFERSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEer 153
Cdd:cd06647   63 NPNIvNYLDSYLVGD-ELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMD-- 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 154 TRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILnTSGSYsGKAADVWSLGVMLYTMLVGRYPFHDIEP-SSLFSKIR 232
Cdd:cd06647  140 GSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVV-TRKAY-GPKVDIWSLGIMAIEMVEGEPPYLNENPlRALYLIAT 217

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 568977678 233 RG--QFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd06647  218 NGtpELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHPFL 260
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
 101-273 1.01e-08

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


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 54.92  E-value: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 101 DMHSFVRtckKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKL-----ESLEDAYILRGDddsls 175
Cdd:cd14019   90 DFRDFYR---KMSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNRETGKGVLVdfglaQREEDRPEQRAP----- 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 176 dKHGCPAYVSPEILNTSGSYSGkAADVWSLGVMLYTMLVGRYPF----HDIEPSSLFSKIrRGqfnipetlSPKAKCLIR 251
Cdd:cd14019  162 -RAGTRGFRAPEVLFKCPHQTT-AIDIWSAGVILLSILSGRFPFffssDDIDALAEIATI-FG--------SDEAYDLLD 230

                        170       180
                 ....*....|....*....|..
gi 568977678 252 SILRREPSERLTSQEILDHPWF 273
Cdd:cd14019  231 KLLELDPSKRITAEEALKHPFF 252
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
 101-274 1.04e-08

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


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 55.83  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 101 DMHSFVRtCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKlesleDAYILRGDDDSLSDKHGC 180
Cdd:cd07878  105 DLNNIVK-CQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRIL-----DFGLARQADDEMTGYVAT 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 181 PAYVSPEILNTSGSYSgKAADVWSLGVMLYTMLVGR--YPFHDI------------EPSS-LFSKI-----RRGQFNIPE 240
Cdd:cd07878  179 RWYRAPEIMLNWMHYN-QTVDIWSVGCIMAELLKGKalFPGNDYidqlkrimevvgTPSPeVLKKIssehaRKYIQSLPH 257

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 568977678 241 T-----------LSPKAKCLIRSILRREPSERLTSQEILDHPWFS 274
Cdd:cd07878  258 MpqqdlkkifrgANPLAIDLLEKMLVLDSDKRISASEALAHPYFS 302
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
 75-269 1.06e-08

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: 55.08  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKA---YVFFERSYG-DMHSFV-RTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFK 149
Cdd:cd13979   58 HENIVRVLAAETGTDFAslgLIIMEYCGNgTLQQLIyEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILIS 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 150 DEERTR-------VKLESLEDAyilrgdDDSLSDKHGCPAYVSPEILNtsGSYSGKAADVWSLGVMLYTMLVGRYPFHDI 222
Cdd:cd13979  138 EQGVCKlcdfgcsVKLGEGNEV------GTPRSHIGGTYTYRAPELLK--GERVTPKADIYSFGITLWQMLTRELPYAGL 209

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568977678 223 EPSSLFSKIRRG-----QFNIPETLSPKAKCLIRSILRREPSERLTSQEILD 269
Cdd:cd13979  210 RQHVLYAVVAKDlrpdlSGLEDSEFGQRLRSLISRCWSAQPAERPNADESLL 261
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
 100-273 1.16e-08

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: 54.86  E-value: 1.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRV----KLESLEDAYilrgDDDSLS 175
Cdd:cd05576   98 LDERLAAASRFYIPEECIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLtyfsRWSEVEDSC----DSDAIE 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 176 DkhgcpAYVSPEIlntsGSYS--GKAADVWSLGVMLYTMLVGRyPFHDIEPSSLFskiRRGQFNIPETLSPKAKCLIRSI 253
Cdd:cd05576  174 N-----MYCAPEV----GGISeeTEACDWWSLGALLFELLTGK-ALVECHPAGIN---THTTLNIPEWVSEEARSLLQQL 240

                        170       180
                 ....*....|....*....|....*
gi 568977678 254 LRREPSERLTS-----QEILDHPWF 273
Cdd:cd05576  241 LQFNPTERLGAgvagvEDIKSHPFF 265
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
 114-272 1.17e-08

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: 54.85  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 114 EEEAARLFY-QIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRV-------KLESLEDAYILRGDDDSLsdkHGCPAYVS 185
Cdd:cd06628  104 EESLVRNFVrQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKIsdfgiskKLEANSLSTKNNGARPSL---QGSVFWMA 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 186 PEILNTSgSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPSSLFSKI-RRGQFNIPETLSPKAKCLIRSILRREPSERLTS 264
Cdd:cd06628  181 PEVVKQT-SYTRKA-DIWSLGCLVVEMLTGTHPFPDCTQMQAIFKIgENASPTIPSNISSEARDFLEKTFEIDHNKRPTA 258


                 ....*...
gi 568977678 265 QEILDHPW 272
Cdd:cd06628  259 DELLKHPF 266
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
 179-273 1.21e-08

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: 55.63  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 179 GCPAYVSPEILNTSGSysGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIR--RGQFNIPE--TLSPKAKCLIRSIL 254
Cdd:cd05629  210 GTPDYIAPEIFLQQGY--GQECDWWSLGAIMFECLIGWPPFCSENSHETYRKIInwRETLYFPDdiHLSVEAEDLIRRLI 287

                         90       100
                 ....*....|....*....|..
gi 568977678 255 rREPSERL---TSQEILDHPWF 273
Cdd:cd05629  288 -TNAENRLgrgGAHEIKSHPFF 308
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
 172-274 1.48e-08

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


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 54.74  E-value: 1.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 172 DSLSD--KHGCPAYVSPEILNTSGSYSGK--AADVWSLGVMLYTMLVGRYP-------FHDI-----EPSSLFSKirrgq 235
Cdd:cd06617  156 DSVAKtiDAGCKPYMAPERINPELNQKGYdvKSDVWSLGITMIELATGRFPydswktpFQQLkqvveEPSPQLPA----- 230

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568977678 236 fnipETLSPKAKCLIRSILRREPSERLTSQEILDHPWFS 274
Cdd:cd06617  231 ----EKFSPEFQDFVNKCLKKNYKERPNYPELLQHPFFE 265
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
 179-273 1.55e-08

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: 54.54  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 179 GCPAYVSPEILNTSG-SYSgkaADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPE----TLSPKAKCLIRSI 253
Cdd:cd14190  165 GTPEFLSPEVVNYDQvSFP---TDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMGNWYFDEetfeHVSDEAKDFVSNL 241

                         90       100
                 ....*....|....*....|
gi 568977678 254 LRREPSERLTSQEILDHPWF 273
Cdd:cd14190  242 IIKERSARMSATQCLKHPWL 261
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
 86-270 1.96e-08

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: 54.31  E-value: 1.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  86 LGETKAYVFFERSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFkdEERTRVKLESLEDAY 165
Cdd:cd06641   72 LKDTKLWIIMEYLGGGSALDLLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLL--SEHGEVKLADFGVAG 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 166 ILRGDDDSLSDKHGCPAYVSPEILNTSgSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPE-TLSP 244
Cdd:cd06641  150 QLTDTQIKRN*FVGTPFWMAPEVIKQS-AYDSKA-DIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLEgNYSK 227

                        170       180
                 ....*....|....*....|....*.
gi 568977678 245 KAKCLIRSILRREPSERLTSQEILDH 270
Cdd:cd06641  228 PLKEFVEACLNKEPSFRPTAKELLKH 253
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
 75-273 1.98e-08

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 54.35  E-value: 1.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFERSYGDMHSFVRTCKKLREEEAARL---FYQIASAVAHCHDGGLVLRDLKLRKFIFkdE 151
Cdd:cd07861   58 HPNIVCLEDVLMQENRLYLVFEFLSMDLKKYLDSLPKGKYMDAELVksyLYQILQGILFCHSRRVLHRDLKPQNLLI--D 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 152 ERTRVKLEsledayilrgdDDSLSDKHGCPA-----------YVSPEILNTSGSYSgKAADVWSLGVMLYTMLVGRYPFH 220
Cdd:cd07861  136 NKGVIKLA-----------DFGLARAFGIPVrvythevvtlwYRAPEVLLGSPRYS-TPVDIWSIGTIFAEMATKKPLFH 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 221 -DIEPSSLFSKIR----------RGQFNIPETLS--PKAKC----------------LIRSILRREPSERLTSQEILDHP 271
Cdd:cd07861  204 gDSEIDQLFRIFRilgtptediwPGVTSLPDYKNtfPKWKKgslrtavknldedgldLLEKMLIYDPAKRISAKKALVHP 283


                 ..
gi 568977678 272 WF 273
Cdd:cd07861  284 YF 285
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
 112-272 2.00e-08

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: 54.48  E-value: 2.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 112 LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDAYILR-GDDDSLSdkHGCPAYVSPEILN 190
Cdd:cd14104   94 LNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRGSYIKIIEFGQSRQLKpGDKFRLQ--YTSAEFYAPEVHQ 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 191 TSgsYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPE----TLSPKAKCLIRSILRREPSERLTSQE 266
Cdd:cd14104  172 HE--SVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDDeafkNISIEALDFVDRLLVKERKSRMTAQE 249


                 ....*.
gi 568977678 267 ILDHPW 272
Cdd:cd14104  250 ALNHPW 255
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
 111-273 2.31e-08

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: 54.20  E-value: 2.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 111 KLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLES--LEDAYILRgddDSLSDKHGCPAYVSPEI 188
Cdd:cd14192   98 QLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNSTGNQIKIIDfgLARRYKPR---EKLKVNFGTPEFLAPEV 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 189 LNTSgsYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIP----ETLSPKAKCLIRSILRREPSERLTS 264
Cdd:cd14192  175 VNYD--FVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDaeafENLSEEAKDFISRLLVKEKSCRMSA 252


                 ....*....
gi 568977678 265 QEILDHPWF 273
Cdd:cd14192  253 TQCLKHEWL 261
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
 102-235 2.84e-08

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: 53.89  E-value: 2.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 102 MHSFVRTCK-KLREEEAARLFYQIASAVAHCHDGGLVLRDLKlRKFIFKDEER---TRVKLESLEDAYILRGDDDSLSDK 177
Cdd:cd14063   83 LYSLIHERKeKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLK-SKNIFLENGRvviTDFGLFSLSGLLQPGRREDTLVIP 161

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568977678 178 HGCPAYVSPEILNT---------SGSYSgKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQ 235
Cdd:cd14063  162 NGWLCYLAPEIIRAlspdldfeeSLPFT-KASDVYAFGTVWYELLAGRWPFKEQPAESIIWQVGCGK 227
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
 179-272 3.60e-08

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: 53.73  E-value: 3.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 179 GCPAYVSPEilNTSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIE-------PSSLFSKIRR--------GQFnipetlS 243
Cdd:cd06619  155 GTNAYMAPE--RISGEQYGIHSDVWSLGISFMELALGRFPYPQIQknqgslmPLQLLQCIVDedppvlpvGQF------S 226

                         90       100
                 ....*....|....*....|....*....
gi 568977678 244 PKAKCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd06619  227 EKFVHFITQCMRKQPKERPAPENLMDHPF 255
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
 100-272 3.61e-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: 53.47  E-value: 3.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCK--KLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKdeERTRVKLESLEDAYILrgdDDSLSDK 177
Cdd:cd06636  104 GSVTDLVKNTKgnALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT--ENAEVKLVDFGVSAQL---DRTVGRR 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 178 H---GCPAYVSPEIL----NTSGSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPsslfskiRRGQFNIPETLSPKAK--- 247
Cdd:cd06636  179 NtfiGTPYWMAPEVIacdeNPDATYDYRS-DIWSLGITAIEMAEGAPPLCDMHP-------MRALFLIPRNPPPKLKskk 250

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 568977678 248 -----------CLIRSILRREPSERLtsqeiLDHPW 272
Cdd:cd06636  251 wskkfidfiegCLVKNYLSRPSTEQL-----LKHPF 281
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
 179-274 3.87e-08

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: 53.37  E-value: 3.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 179 GCPAYVSPEILnTSGSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRG---QFNIPETLSPKAKCLIRSILR 255
Cdd:cd06614  159 GTPYWMAPEVI-KRKDYGPKV-DIWSLGIMCIEMAEGEPPYLEEPPLRALFLITTKgipPLKNPEKWSPEFKDFLNKCLV 236

                         90
                 ....*....|....*....
gi 568977678 256 REPSERLTSQEILDHPWFS 274
Cdd:cd06614  237 KDPEKRPSAEELLQHPFLK 255
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
 122-273 4.65e-08

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: 53.72  E-value: 4.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 122 YQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKL-ESLEDAYILRG-------------DDDSLSD----KHgcpaY 183
Cdd:cd14134  122 KQLLEAVAFLHDLKLTHTDLKPENILLVDSDYVKVYNpKKKRQIRVPKStdiklidfgsatfDDEYHSSivstRH----Y 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 184 VSPE-ILNTSGSYSgkaADVWSLGVMLYTMLVGR--YPFHD-------IE------PSSLFSKIR---------RGQFNI 238
Cdd:cd14134  198 RAPEvILGLGWSYP---CDVWSIGCILVELYTGEllFQTHDnlehlamMErilgplPKRMIRRAKkgakyfyfyHGRLDW 274

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568977678 239 PE-------------TLSPKAKC----------LIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd14134  275 PEgsssgrsikrvckPLKRLMLLvdpehrllfdLIRKMLEYDPSKRITAKEALKHPFF 332
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
 119-271 5.76e-08

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: 52.84  E-value: 5.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 119 RLFYQIASAVA--HCHDGGLVLRDLKLRKFIFKDEERTRVK---LESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSG 193
Cdd:cd13978   97 RIIHEIALGMNflHNMDPPLLHHDLKPENILLDNHFHVKISdfgLSKLGMKSISANRRRGTENLGGTPIYMAPEAFDDFN 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 194 SYSGKAADVWSLGVMLYTMLVGRYPFHD-IEPSSLFSKIRRGQFNIPETLS-----PKAKCLIRSILR---REPSERLTS 264
Cdd:cd13978  177 KKPTSKSDVYSFAIVIWAVLTRKEPFENaINPLLIMQIVSKGDRPSLDDIGrlkqiENVQELISLMIRcwdGNPDARPTF 256


                 ....*..
gi 568977678 265 QEILDHP 271
Cdd:cd13978  257 LECLDRL 263
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
 87-272 5.79e-08

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: 52.78  E-value: 5.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  87 GETKAYVFFE-RSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKfIFKDEErTRVKLESLEDAY 165
Cdd:cd06651   82 AEKTLTIFMEyMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGAN-ILRDSA-GNVKLGDFGASK 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 166 ILRG---DDDSLSDKHGCPAYVSPEILntSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFN--IPE 240
Cdd:cd06651  160 RLQTicmSGTGIRSVTGTPYWMSPEVI--SGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNpqLPS 237

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568977678 241 TLSPKAKCLIRSILrREPSERLTSQEILDHPW 272
Cdd:cd06651  238 HISEHARDFLGCIF-VEARHRPSAEELLRHPF 268
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
 88-272 7.89e-08

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: 52.33  E-value: 7.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  88 ETKAYVFFE-RSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKfIFKDEErTRVKLESLEDAYI 166
Cdd:cd06653   78 EKKLSIFVEyMPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGAN-ILRDSA-GNVKLGDFGASKR 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 167 LRG---DDDSLSDKHGCPAYVSPEILNTSGSysGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFN--IPET 241
Cdd:cd06653  156 IQTicmSGTGIKSVTGTPYWMSPEVISGEGY--GRKADVWSVACTVVEMLTEKPPWAEYEAMAAIFKIATQPTKpqLPDG 233

                        170       180       190
                 ....*....|....*....|....*....|.
gi 568977678 242 LSPKAKCLIRSILRREpSERLTSQEILDHPW 272
Cdd:cd06653  234 VSDACRDFLRQIFVEE-KRRPTAEFLLRHPF 263
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
 75-272 9.29e-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: 52.07  E-value: 9.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFERSYGDMHSFVRTCKK-LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEer 153
Cdd:cd06607   60 HPNTIEYKGCYLREHTAWLVMEYCLGSASDIVEVHKKpLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEP-- 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 154 TRVKLESLEDAYILrgddDSLSDKHGCPAYVSPEIL--NTSGSYSGKaADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKI 231
Cdd:cd06607  138 GTVKLADFGSASLV----CPANSFVGTPYWMAPEVIlaMDEGQYDGK-VDVWSLGITCIELAERKPPLFNMNAMSALYHI 212

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568977678 232 RRgqfNIPETLSPKA-----KCLIRSILRREPSERLTSQEILDHPW 272
Cdd:cd06607  213 AQ---NDSPTLSSGEwsddfRNFVDSCLQKIPQDRPSAEDLLKHPF 255
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
 112-270 1.10e-07

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: 51.98  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 112 LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFkdEERTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNT 191
Cdd:cd06642   98 LEETYIATILREILKGLDYLHSERKIHRDIKAANVLL--SEQGDVKLADFGVAGQLTDTQIKRNTFVGTPFWMAPEVIKQ 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 192 SgSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRgqfNIPETL----SPKAKCLIRSILRREPSERLTSQEI 267
Cdd:cd06642  176 S-AYDFKA-DIWSLGITAIELAKGEPPNSDLHPMRVLFLIPK---NSPPTLegqhSKPFKEFVEACLNKDPRFRPTAKEL 250


                 ...
gi 568977678 268 LDH 270
Cdd:cd06642  251 LKH 253
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
 179-278 1.13e-07

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: 52.71  E-value: 1.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 179 GCPAYVSPEILNTSGsYSgKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKI--RRGQFNIPE--TLSPKAKCLIRSiL 254
Cdd:cd05626  210 GTPNYIAPEVLLRKG-YT-QLCDWWSVGVILFEMLVGQPPFLAPTPTETQLKVinWENTLHIPPqvKLSPEAVDLITK-L 286

                         90       100
                 ....*....|....*....|....*...
gi 568977678 255 RREPSERL---TSQEILDHPWFST-DFS 278
Cdd:cd05626  287 CCSAEERLgrnGADDIKAHPFFSEvDFS 314
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
 101-282 1.19e-07

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: 52.37  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 101 DMHSFVRTCKKLREEEAARLFYQIASAVAHCHD--GGLVLRDLKLRKFIFKDEERT-RVKLESLEDAYILrgDDDSL--- 174
Cdd:cd14040   97 DLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLVDGTACgEIKITDFGLSKIM--DDDSYgvd 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 175 -----SDKHGCPAYVSPE--ILNTSGSYSGKAADVWSLGVMLYTMLVGRYPF------HDIEPSSLFSKIRRGQFNIPET 241
Cdd:cd14040  175 gmdltSQGAGTYWYLPPEcfVVGKEPPKISNKVDVWSVGVIFFQCLYGRKPFghnqsqQDILQENTILKATEVQFPVKPV 254

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 568977678 242 LSPKAKCLIRSILRREPSERLTSQEILDHPWFSTDFSVSNS 282
Cdd:cd14040  255 VSNEAKAFIRRCLAYRKEDRFDVHQLASDPYLLPHMRRSNS 295
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
 67-270 1.46e-07

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: 51.58  E-value: 1.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  67 APCFCLSAHSNINQITEILLGETKAYVFFERSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLV---LRDLKL 143
Cdd:cd14145   56 AKLFAMLKHPNIIALRGVCLKEPNLCLVMEFARGGPLNRVLSGKRIPPDILVNWAVQIARGMNYLHCEAIVpviHRDLKS 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 144 RKFIFKDeertRVKLESLEDAyILRGDDDSLSDK---------HGCPAYVSPEILNTSgSYSgKAADVWSLGVMLYTMLV 214
Cdd:cd14145  136 SNILILE----KVENGDLSNK-ILKITDFGLAREwhrttkmsaAGTYAWMAPEVIRSS-MFS-KGSDVWSYGVLLWELLT 208

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568977678 215 GRYPFHDIEPSSLFSKIRRGQFN--IPETLSPKAKCLIRSILRREPSERLTSQEILDH 270
Cdd:cd14145  209 GEVPFRGIDGLAVAYGVAMNKLSlpIPSTCPEPFARLMEDCWNPDPHSRPPFTNILDQ 266
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
 122-267 1.60e-07

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: 51.89  E-value: 1.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 122 YQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESL------EDAYILRGDDDslsdkhgCPA-YVSPEILnTSGS 194
Cdd:cd05045  134 WQISRGMQYLAEMKLVHRDLAARNVLVAEGRKMKISDFGLsrdvyeEDSYVKRSKGR-------IPVkWMAIESL-FDHI 205

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568977678 195 YSGKAaDVWSLGVMLYTML-VGRYPFHDIEPSSLFSKIRRG-QFNIPETLSPKAKCLIRSILRREPSERLTSQEI 267
Cdd:cd05045  206 YTTQS-DVWSFGVLLWEIVtLGGNPYPGIAPERLFNLLKTGyRMERPENCSEEMYNLMLTCWKQEPDKRPTFADI 279
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
 67-270 1.67e-07

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: 51.34  E-value: 1.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  67 APCFCLsahsninqITEILlgetkayvfferSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKF 146
Cdd:cd14059   53 APCYCI--------LMEYC------------PYGQLYEVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNV 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 147 IFKDEERtrVKLESLedayilrGDDDSLSDKH------GCPAYVSPEILNTSgSYSGKAaDVWSLGVMLYTMLVGRYPFH 220
Cdd:cd14059  113 LVTYNDV--LKISDF-------GTSKELSEKStkmsfaGTVAWMAPEVIRNE-PCSEKV-DIWSFGVVLWELLTGEIPYK 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568977678 221 DIEPSSLFSKIRRG--QFNIPETLSPKAKCLIRSILRREPSERLTSQEILDH 270
Cdd:cd14059  182 DVDSSAIIWGVGSNslQLPVPSTCPDGFKLLMKQCWNSKPRNRPSFRQILMH 233
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
 78-273 2.19e-07

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: 51.26  E-value: 2.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  78 INQITEILLGEtKAYVFFERSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEerTRVK 157
Cdd:cd06656   79 VNYLDSYLVGD-ELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMD--GSVK 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 158 LESLEDAYILRGDDDSLSDKHGCPAYVSPEILnTSGSYsGKAADVWSLGVMLYTMLVGRYPFHDIEP-SSLFSKIRRG-- 234
Cdd:cd06656  156 LTDFGFCAQITPEQSKRSTMVGTPYWMAPEVV-TRKAY-GPKVDIWSLGIMAIEMVEGEPPYLNENPlRALYLIATNGtp 233

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568977678 235 QFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd06656  234 ELQNPERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 272
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
 130-276 2.79e-07

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: 50.87  E-value: 2.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 130 HCHDGGLVLRDLKLRKfIFKDEERTRVKLESLEDAYILRgdDDSLSDKHGCPAYVSPEILNtsgSYSGKAADVWSLGVML 209
Cdd:cd14031  130 HTRTPPIIHRDLKCDN-IFITGPTGSVKIGDLGLATLMR--TSFAKSVIGTPEFMAPEMYE---EHYDESVDVYAFGMCM 203

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568977678 210 YTMLVGRYPFHDIEPSS-----LFSKIRRGQFNipETLSPKAKCLIRSILRREPSERLTSQEILDHPWFSTD 276
Cdd:cd14031  204 LEMATSEYPYSECQNAAqiyrkVTSGIKPASFN--KVTDPEVKEIIEGCIRQNKSERLSIKDLLNHAFFAED 273
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
 114-270 3.09e-07

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: 50.82  E-value: 3.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 114 EEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFkdEERTRVKLESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSg 193
Cdd:cd06640  100 EFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLL--SEQGDVKLADFGVAGQLTDTQIKRNTFVGTPFWMAPEVIQQS- 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 194 SYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRgqFNIPE---TLSPKAKCLIRSILRREPSERLTSQEILDH 270
Cdd:cd06640  177 AYDSKA-DIWSLGITAIELAKGEPPNSDMHPMRVLFLIPK--NNPPTlvgDFSKPFKEFIDACLNKDPSFRPTAKELLKH 253
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
 93-270 3.38e-07

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


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 50.43  E-value: 3.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  93 VFFERS-YGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKfIFKDEErTRVKLESLEDAYILRG-- 169
Cdd:cd06652   83 IFMEYMpGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGAN-ILRDSV-GNVKLGDFGASKRLQTic 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 170 -DDDSLSDKHGCPAYVSPEILntSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNiPEtLSPKAKC 248
Cdd:cd06652  161 lSGTGMKSVTGTPYWMSPEVI--SGEGYGRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIATQPTN-PQ-LPAHVSD 236

                        170       180
                 ....*....|....*....|....*
gi 568977678 249 LIRSILRR---EPSERLTSQEILDH 270
Cdd:cd06652  237 HCRDFLKRifvEAKLRPSADELLRH 261
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
 77-273 3.41e-07

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: 50.76  E-value: 3.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  77 NINQITEILLGETKAYVFFERSYGDMHSFVRTCKKLREEEAARLF-YQIASAVAHCHDGGLVLRDLKLRKFIFKDEERtr 155
Cdd:cd07848   61 NIVELKEAFRRRGKLYLVFEYVEKNMLELLEEMPNGVPPEKVRSYiYQLIKAIHWCHKNDIVHRDIKPENLLISHNDV-- 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 156 VKLESLEDAYIL-RGDDDSLSDKHGCPAYVSPEILntSGSYSGKAADVWSLGVML-------------------YTM--L 213
Cdd:cd07848  139 LKLCDFGFARNLsEGSNANYTEYVATRWYRSPELL--LGAPYGKAVDMWSVGCILgelsdgqplfpgeseidqlFTIqkV 216

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568977678 214 VGRYPFHDIE---PSSLFSKIRRGQFNIPETLSPKAKC--------LIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd07848  217 LGPLPAEQMKlfySNPRFHGLRFPAVNHPQSLERRYLGilsgvlldLMKNLLKLNPTDRYLTEQCLNHPAF 287
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
 179-275 3.60e-07

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: 50.83  E-value: 3.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 179 GCPAYVSPEILNTSGSysGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNI---PET-LSPKAKCLirsIL 254
Cdd:cd05627  199 GTPDYIAPEVFMQTGY--NKLCDWWSLGVIMYEMLIGYPPFCSETPQETYRKVMNWKETLvfpPEVpISEKAKDL---IL 273

                         90       100
                 ....*....|....*....|....*.
gi 568977678 255 R--REPSERLTS---QEILDHPWFST 275
Cdd:cd05627  274 RfcTDAENRIGSngvEEIKSHPFFEG 299
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
 100-261 3.87e-07

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: 50.51  E-value: 3.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTC--KKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEerTRVKLESLEDAYILRgDDDSLSDK 177
Cdd:cd05148   87 GSLLAFLRSPegQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGED--LVCKVADFGLARLIK-EDVYLSSD 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 178 HGCP-AYVSPEILNtSGSYSGKAaDVWSLGVMLYTMLV-GRYPFHDIEPSSLFSKIRRGqFNIPetlSPkAKC------L 249
Cdd:cd05148  164 KKIPyKWTAPEAAS-HGTFSTKS-DVWSFGILLYEMFTyGQVPYPGMNNHEVYDQITAG-YRMP---CP-AKCpqeiykI 236

                        170
                 ....*....|..
gi 568977678 250 IRSILRREPSER 261
Cdd:cd05148  237 MLECWAAEPEDR 248
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
 86-263 4.59e-07

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: 50.57  E-value: 4.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  86 LGETKA-YVFFERSYGDMHSFVRTCKkLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFI--FKDEERTRVKLESL- 161
Cdd:cd14018  109 LGHNRTlFLVMKNYPCTLRQYLWVNT-PSYRLARVMILQLLEGVDHLVRHGIAHRDLKSDNILleLDFDGCPWLVIADFg 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 162 ----EDAYILRGDDDSLS-DKHGCPAYVSPEILNTSG------SYSgkAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSK 230
Cdd:cd14018  188 cclaDDSIGLQLPFSSWYvDRGGNACLMAPEVSTAVPgpgvviNYS--KADAWAVGAIAYEIFGLSNPFYGLGDTMLESR 265

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568977678 231 -IRRGQF-NIPETLSPKAKCLIRSILRREPSERLT 263
Cdd:cd14018  266 sYQESQLpALPSAVPPDVRQVVKDLLQRDPNKRVS 300
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
 110-274 4.68e-07

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: 50.72  E-value: 4.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 110 KKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEertrVKLESLeDAYILRGDDDSLSDKHGCPAYVSPEIL 189
Cdd:cd07880  113 EKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNED----CELKIL-DFGLARQTDSEMTGYVVTRWYRAPEVI 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 190 NTSGSYSgKAADVWSLGVMLYTMLVGRYPF--HDI------------EPSSLFS----------------KIRRGQF-NI 238
Cdd:cd07880  188 LNWMHYT-QTVDIWSVGCIMAEMLTGKPLFkgHDHldqlmeimkvtgTPSKEFVqklqsedaknyvkklpRFRKKDFrSL 266

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 568977678 239 PETLSPKAKCLIRSILRREPSERLTSQEILDHPWFS 274
Cdd:cd07880  267 LPNANPLAVNVLEKMLVLDAESRITAAEALAHPYFE 302
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
 67-268 6.45e-07

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: 49.60  E-value: 6.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  67 APCFCLSAHSNINQITEILLGETKAYVFFERSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLV---LRDLKL 143
Cdd:cd14148   44 ARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGGALNRALAGKKVPPHVLVNWAVQIARGMNYLHNEAIVpiiHRDLKS 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 144 RKFIFKDeertRVKLESLEDAyILRGDDDSLSDK---------HGCPAYVSPEILNTSgsYSGKAADVWSLGVMLYTMLV 214
Cdd:cd14148  124 SNILILE----PIENDDLSGK-TLKITDFGLAREwhkttkmsaAGTYAWMAPEVIRLS--LFSKSSDVWSFGVLLWELLT 196

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568977678 215 GRYPFHDIEPSSLFSKIRRGQFN--IPETLSPKAKCLIRSILRREPSERLTSQEIL 268
Cdd:cd14148  197 GEVPYREIDALAVAYGVAMNKLTlpIPSTCPEPFARLLEECWDPDPHGRPDFGSIL 252
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
 100-233 1.06e-06

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: 49.19  E-value: 1.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSF---VRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERtRVKLESLEDAYILRGDDDSLSD 176
Cdd:cd14038   83 GDLRKYlnqFENCCGLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQ-RLIHKIIDLGYAKELDQGSLCT 161

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568977678 177 KH-GCPAYVSPEILNTSgSYSgKAADVWSLGVMLYTMLVGRYPF-HDIEPSSLFSKIRR 233
Cdd:cd14038  162 SFvGTLQYLAPELLEQQ-KYT-VTVDYWSFGTLAFECITGFRPFlPNWQPVQWHGKVRQ 218
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 100-220 1.11e-06

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: 49.26  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCKKLR----EEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKdeERTRVKLESLEDAYILRGDDDSLS 175
Cdd:cd08229  109 GDLSRMIKHFKKQKrlipEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFIT--ATGVVKLGDLGLGRFFSSKTTAAH 186

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 568977678 176 DKHGCPAYVSPEILNTSGsYSGKAaDVWSLGVMLYTMLVGRYPFH 220
Cdd:cd08229  187 SLVGTPYYMSPERIHENG-YNFKS-DIWSLGCLLYEMAALQSPFY 229
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
 75-284 1.13e-06

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: 49.49  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFERSYG-DMHSFVrTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKdeER 153
Cdd:cd07856   68 HENIISLSDIFISPLEDIYFVTELLGtDLHRLL-TSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVN--EN 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 154 TRVKlesLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSGSYSgKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRR 233
Cdd:cd07856  145 CDLK---ICDFGLARIQDPQMTGYVSTRYYRAPEIMLTWQKYD-VEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITE 220

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 234 GQFNIPE-------------------------------TLSPKAKCLIRSILRREPSERLTSQEILDHPWFS-----TDF 277
Cdd:cd07856  221 LLGTPPDdvinticsentlrfvqslpkrervpfsekfkNADPDAIDLLEKMLVFDPKKRISAAEALAHPYLApyhdpTDE 300


                 ....*..
gi 568977678 278 SVSNSGF 284
Cdd:cd07856  301 PVADEKF 307
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
 104-272 1.30e-06

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: 48.84  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 104 SFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEerTRVKLESLEDAYILRGDDDSLSDKHGCPAY 183
Cdd:cd06639  117 GLLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTE--GGVKLVDFGVSAQLTSARLRRNTSVGTPFW 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 184 VSPEILNTSGSYSGK---AADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRgqfNIPETL-SPKAKC-----LIRSIL 254
Cdd:cd06639  195 MAPEVIACEQQYDYSydaRCDVWSLGITAIELADGDPPLFDMHPVKALFKIPR---NPPPTLlNPEKWCrgfshFISQCL 271

                        170
                 ....*....|....*...
gi 568977678 255 RREPSERLTSQEILDHPW 272
Cdd:cd06639  272 IKDFEKRPSVTHLLEHPF 289
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
 183-272 1.34e-06

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: 48.96  E-value: 1.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 183 YVSPEILnTSGSYSGKAaDVWSLGVMLYTMLVGRYPF-----HDIEPSSLFSKIRRgqFNIPETL---------SPKAKC 248
Cdd:cd06621  169 YMAPERI-QGGPYSITS-DVWSLGLTLLEVAQNRFPFppegePPLGPIELLSYIVN--MPNPELKdepengikwSESFKD 244

                         90       100
                 ....*....|....*....|....
gi 568977678 249 LIRSILRREPSERLTSQEILDHPW 272
Cdd:cd06621  245 FIEKCLEKDGTRRPGPWQMLAHPW 268
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
 101-273 1.52e-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: 48.90  E-value: 1.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 101 DMHSFVRTCKKLREEEAARLFYQIASAVAHCHD--GGLVLRDLKLRKFIFKDEERT-RVKLESLEDAYILrgDDDSL--- 174
Cdd:cd14041   97 DLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEikPPIIHYDLKPGNILLVNGTACgEIKITDFGLSKIM--DDDSYnsv 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 175 ------SDKHGCPAYVSPE--ILNTSGSYSGKAADVWSLGVMLYTMLVGRYPF------HDIEPSSLFSKIRRGQFNIPE 240
Cdd:cd14041  175 dgmeltSQGAGTYWYLPPEcfVVGKEPPKISNKVDVWSVGVIFYQCLYGRKPFghnqsqQDILQENTILKATEVQFPPKP 254

                        170       180       190
                 ....*....|....*....|....*....|...
gi 568977678 241 TLSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd14041  255 VVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYL 287
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
 179-273 1.62e-06

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: 48.59  E-value: 1.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 179 GCPAYVSPEILNtSGSYSGKAaDVWSLGVMLYTMLVGRYPFHDIE--------PSSLFSKIRRGQFNIPETL------SP 244
Cdd:cd06620  165 GTSTYMSPERIQ-GGKYSVKS-DVWSLGLSIIELALGEFPFAGSNddddgyngPMGILDLLQRIVNEPPPRLpkdrifPK 242

                         90       100
                 ....*....|....*....|....*....
gi 568977678 245 KAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd06620  243 DLRDFVDRCLLKDPRERPSPQLLLDHDPF 271
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
 98-267 1.75e-06

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 48.57  E-value: 1.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  98 SYGDMHSFVRTCKKLREEEAARLF-YQIASAVAHCHDGGLVLRDLKLRKFIFKDEERtrVKL------ESLEDAYILRGD 170
Cdd:cd05056   89 PLGELRSYLQVNKYSLDLASLILYaYQLSTALAYLESKRFVHRDIAARNVLVSSPDC--VKLgdfglsRYMEDESYYKAS 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 171 DDSLSDKhgcpaYVSPEILN----TSgsysgkAADVWSLGV-MLYTMLVGRYPFHDIEPSSLFSKIRRGQ-FNIPETLSP 244
Cdd:cd05056  167 KGKLPIK-----WMAPESINfrrfTS------ASDVWMFGVcMWEILMLGVKPFQGVKNNDVIGRIENGErLPMPPNCPP 235

                        170       180
                 ....*....|....*....|...
gi 568977678 245 KAKCLIRSILRREPSERLTSQEI 267
Cdd:cd05056  236 TLYSLMTKCWAYDPSKRPRFTEL 258
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
 75-272 1.85e-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: 48.65  E-value: 1.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKA----------YVFFERSYGDMHSFVRT-CKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKL 143
Cdd:cd07864   65 HRSVVNLKEIVTDKQDAldfkkdkgafYLVFEYMDHDLMGLLESgLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKC 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 144 RKFIFKDeeRTRVKLESLEDAYILRGDDDSL-SDKHGCPAYVSPEILNTSGSYsGKAADVWSLGVMLYTMLVGR------ 216
Cdd:cd07864  145 SNILLNN--KGQIKLADFGLARLYNSEESRPyTNKVITLWYRPPELLLGEERY-GPAIDVWSCGCILGELFTKKpifqan 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 217 --------------------YP-------FHDIEPSSLFSKIRRGQFnipETLSPKAKCLIRSILRREPSERLTSQEILD 269
Cdd:cd07864  222 qelaqlelisrlcgspcpavWPdviklpyFNTMKPKKQYRRRLREEF---SFIPTPALDLLDHMLTLDPSKRCTAEQALN 298


                 ...
gi 568977678 270 HPW 272
Cdd:cd07864  299 SPW 301
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
 112-219 2.10e-06

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: 48.64  E-value: 2.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 112 LREEEAARLFYQIASAVAHCHDGGLVLRDLK---LRKFIfKDEERTRVKLESLEDAYILrGDDDSLSDKHGCPAYVSPEI 188
Cdd:cd13988   93 LPESEFLIVLRDVVAGMNHLRENGIVHRDIKpgnIMRVI-GEDGQSVYKLTDFGAAREL-EDDEQFVSLYGTEEYLHPDM 170

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 568977678 189 L------NTSGSYSGKAADVWSLGVMLYTMLVGRYPF 219
Cdd:cd13988  171 YeravlrKDHQKKYGATVDLWSIGVTFYHAATGSLPF 207
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
 78-273 2.18e-06

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: 48.18  E-value: 2.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  78 INQITEILLGEtKAYVFFERSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEerTRVK 157
Cdd:cd06654   80 VNYLDSYLVGD-ELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMD--GSVK 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 158 LESLEDAYILRGDDDSLSDKHGCPAYVSPEILnTSGSYsGKAADVWSLGVMLYTMLVGRYPFHDIEP-SSLFSKIRRG-- 234
Cdd:cd06654  157 LTDFGFCAQITPEQSKRSTMVGTPYWMAPEVV-TRKAY-GPKVDIWSLGIMAIEMIEGEPPYLNENPlRALYLIATNGtp 234

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568977678 235 QFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd06654  235 ELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFL 273
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
 100-250 2.28e-06

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: 48.50  E-value: 2.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFkdEERTRVKLES------LEDAY---ILRGD 170
Cdd:cd05628   86 GDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLL--DSKGHVKLSDfglctgLKKAHrteFYRNL 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 171 DDSLSDKH--------------------------GCPAYVSPEILNTSGSysGKAADVWSLGVMLYTMLVGRYPFHDIEP 224
Cdd:cd05628  164 NHSLPSDFtfqnmnskrkaetwkrnrrqlafstvGTPDYIAPEVFMQTGY--NKLCDWWSLGVIMYEMLIGYPPFCSETP 241

                        170       180       190
                 ....*....|....*....|....*....|
gi 568977678 225 SSLFSKIRRGQFNI---PET-LSPKAKCLI 250
Cdd:cd05628  242 QETYKKVMNWKETLifpPEVpISEKAKDLI 271
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
 172-273 2.74e-06

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: 48.20  E-value: 2.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 172 DSLSDKH-GCPAYVSPEILntSGSYSGKAADVWSLGVMLYTMLVGRYP-----------FHDIEPSSLFSKIRRGQFN-- 237
Cdd:cd06615  152 DSMANSFvGTRSYMSPERL--QGTHYTVQSDIWSLGLSLVEMAIGRYPipppdakeleaMFGRPVSEGEAKESHRPVSgh 229

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568977678 238 ---------IPETL----------------SPKAKCLIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd06615  230 ppdsprpmaIFELLdyivnepppklpsgafSDEFQDFVDKCLKKNPKERADLKELTKHPFI 290
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
 123-276 4.01e-06

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


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 47.34  E-value: 4.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 123 QIASAVAHCHDGGLVLRDLKLRKFIFkdEERTRVKLESLEDAYILrgDDDSLSDKHGCP---AYVSPEILNTsGSYSGKA 199
Cdd:cd05072  112 QIAEGMAYIERKNYIHRDLRAANVLV--SESLMCKIADFGLARVI--EDNEYTAREGAKfpiKWTAPEAINF-GSFTIKS 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 200 aDVWSLGVMLYTMLV-GRYPFHDIEPSSLFSKIRRG-QFNIPETLSPKAKCLIRSILRREPSERLTS---QEILDHPWFS 274
Cdd:cd05072  187 -DVWSFGILLYEIVTyGKIPYPGMSNSDVMSALQRGyRMPRMENCPDELYDIMKTCWKEKAEERPTFdylQSVLDDFYTA 265


                 ..
gi 568977678 275 TD 276
Cdd:cd05072  266 TE 267
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
 75-234 4.17e-06

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


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 47.31  E-value: 4.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFER-SYGDMHSFVRTCK-KLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEE 152
Cdd:cd05085   52 HPNIVKLIGVCTQRQPIYIVMELvPGGDFLSFLRKKKdELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENN 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 153 RTRVkleslEDAYILRGDDDSLSDKHGCP----AYVSPEILNTsGSYSGKAaDVWSLGVMLY-TMLVGRYPFHDIEPSSL 227
Cdd:cd05085  132 ALKI-----SDFGMSRQEDDGVYSSSGLKqipiKWTAPEALNY-GRYSSES-DVWSFGILLWeTFSLGVCPYPGMTNQQA 204


                 ....*..
gi 568977678 228 FSKIRRG 234
Cdd:cd05085  205 REQVEKG 211
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
 106-233 4.20e-06

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: 47.44  E-value: 4.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 106 VRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEE-RTRVKLESLEDAYILrgDDDSL-SDKHGCPAY 183
Cdd:cd13989   93 PENCCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGgRVIYKLIDLGYAKEL--DQGSLcTSFVGTLQY 170

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568977678 184 VSPEILNTSgSYSgKAADVWSLGVMLYTMLVGRYPF-HDIEPSSLFSKIRR 233
Cdd:cd13989  171 LAPELFESK-KYT-CTVDYWSFGTLAFECITGYRPFlPNWQPVQWHGKVKQ 219
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
 123-230 4.68e-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: 47.38  E-value: 4.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 123 QIASAVAHCHDGGLVLRDLKLRKfIFKDEERtRVK---------LESLEDAYILRGDDDSlsdkhgcPAY-VSPEILNTS 192
Cdd:cd05038  117 QICKGMEYLGSQRYIHRDLAARN-ILVESED-LVKisdfglakvLPEDKEYYYVKEPGES-------PIFwYAPECLRES 187

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568977678 193 GSYSgkAADVWSLGVMLYTMLVgrYPFHDIEPSSLFSK 230
Cdd:cd05038  188 RFSS--ASDVWSFGVTLYELFT--YGDPSQSPPALFLR 221
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
 179-293 4.87e-06

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: 47.36  E-value: 4.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 179 GCPAYVSPEILNTSGSYSGK--AADVWSLGVMLYTMLVGRYPFHdiEPSSLFSKIRRGQFNIPETLSPK-----AKCLIR 251
Cdd:cd06616  171 GCRPYMAPERIDPSASRDGYdvRSDVWSLGITLYEVATGKFPYP--KWNSVFDQLTQVVKGDPPILSNSeerefSPSFVN 248

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 568977678 252 SI---LRREPSERLTSQEILDHPwFSTDFSVSNsGFGAKEACDQL 293
Cdd:cd06616  249 FVnlcLIKDESKRPKYKELLKHP-FIKMYEERN-VDVAAYVQKIL 291
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
 75-267 5.22e-06

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 47.03  E-value: 5.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFE-RSYGDMHSFVRTCKKlREEEAARLFY---QIASAVAHCHDGGLVLRDLKLRKFIFkd 150
Cdd:cd05052   61 HPNLVQLLGVCTREPPFYIITEfMPYGNLLDYLRECNR-EELNAVVLLYmatQIASAMEYLEKKNFIHRDLAARNCLV-- 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 151 EERTRVKLESLEDAYILRGDDDSLSDKHGCP-AYVSPEIL--NTSGSYSgkaaDVWSLGVMLYTMLV-GRYPFHDIEPSS 226
Cdd:cd05052  138 GENHLVKVADFGLSRLMTGDTYTAHAGAKFPiKWTAPESLayNKFSIKS----DVWAFGVLLWEIATyGMSPYPGIDLSQ 213

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568977678 227 LFSKIRRG-QFNIPETLSPKAKCLIRSILRREPSERLTSQEI 267
Cdd:cd05052  214 VYELLEKGyRMERPEGCPPKVYELMRACWQWNPSDRPSFAEI 255
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
 75-273 6.09e-06

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 47.04  E-value: 6.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFERSYGDMHSFVRTCKKLREEEAARLF-YQIASAVAHCHDGGLVLRDLKLRKFIFKDeeR 153
Cdd:cd07839   58 HKNIVRLYDVLHSDKKLTLVFEYCDQDLKKYFDSCNGDIDPEIVKSFmFQLLKGLAFCHSHNVLHRDLKPQNLLINK--N 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 154 TRVKLEsledayilrgdDDSLSDKHGCPA-----------YVSPEILNTSGSYSgKAADVWSLGVMLYTML-VGR--YPF 219
Cdd:cd07839  136 GELKLA-----------DFGLARAFGIPVrcysaevvtlwYRPPDVLFGAKLYS-TSIDMWSAGCIFAELAnAGRplFPG 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 220 HDIE------------------PSslFSKIRRGQF-----------NIPETLSPKAKCLIRSILRREPSERLTSQEILDH 270
Cdd:cd07839  204 NDVDdqlkrifrllgtpteeswPG--VSKLPDYKPypmypattslvNVVPKLNSTGRDLLQNLLVCNPVQRISAEEALQH 281


                 ...
gi 568977678 271 PWF 273
Cdd:cd07839  282 PYF 284
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
 119-267 6.91e-06

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: 46.84  E-value: 6.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 119 RLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDAYILRGDDDS-LSDKHGCPAYVSPEILNTSGSYSG 197
Cdd:cd14000  116 RIALQVADGLRYLHSAMIIYRDLKSHNVLVWTLYPNSAIIIKIADYGISRQCCRMgAKGSEGTPGFRAPEIARGNVIYNE 195

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568977678 198 KAaDVWSLGVMLYTMLVGRYPF---HDIEPSSLFSKIRRGQFNIPETLS-PKAKCLIRSILRREPSERLTSQEI 267
Cdd:cd14000  196 KV-DVFSFGMLLYEILSGGAPMvghLKFPNEFDIHGGLRPPLKQYECAPwPEVEVLMKKCWKENPQQRPTAVTV 268
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
 75-273 7.38e-06

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 46.99  E-value: 7.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGET--KAYVFFERSYGDM------HSFVRTCKK---LREEEAARLFYQIASAVAHCHDGGLVLRDLKL 143
Cdd:cd07867   58 HPNVIALQKVFLSHSdrKVWLLFDYAEHDLwhiikfHRASKANKKpmqLPRSMVKSLLYQILDGIHYLHANWVLHRDLKP 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 144 RKFIFKDE--ERTRVKLESLEDAYILRGDDDSLSDKHGCPA---YVSPEILNTSGSYSgKAADVWSLGVMLYTMLVGRYP 218
Cdd:cd07867  138 ANILVMGEgpERGRVKIADMGFARLFNSPLKPLADLDPVVVtfwYRAPELLLGARHYT-KAIDIWAIGCIFAELLTSEPI 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 219 FH----DIEPSSLFSKIRRGQF----------------NIPE-------------------------TLSPKAKC--LIR 251
Cdd:cd07867  217 FHcrqeDIKTSNPFHHDQLDRIfsvmgfpadkdwedirKMPEyptlqkdfrrttyansslikymekhKVKPDSKVflLLQ 296

                        250       260
                 ....*....|....*....|..
gi 568977678 252 SILRREPSERLTSQEILDHPWF 273
Cdd:cd07867  297 KLLTMDPTKRITSEQALQDPYF 318
Kinase-like pfam14531
Kinase-like; This family includes the pseudokinases ROP2 and ROP8 from Toxoplasma gondii. ...
 101-261 1.18e-05

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: 45.95  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  101 DMHSFVRTCKKL-----REEEAARLFY--QIASAVAHCHDGGLVLRDLKLRKFIFKdeERTRVKLESLEDAYilrGDDDS 173
Cdd:pfam14531 123 DLQLLGEVLLSHssthkSLVHHARLQLtlQLIRLAANLQHYGLVHGQFTVDNFFLD--QRGGVFLGGFEHLV---RDGTK 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  174 LSDKHGCPAYVSPEILNTSGSYSGK-------AADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPEtlspKA 246
Cdd:pfam14531 198 VVASEVPRGFAPPELLGSRGGYTMKnttlmthAFDAWQLGLVIYWIWCLDLPNTLDAEEGGIEWKFRLCKNIPE----PV 273

                         170
                  ....*....|....*
gi 568977678  247 KCLIRSILRREPSER 261
Cdd:pfam14531 274 RALLKGFLNYSQEDR 288
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
 100-273 1.31e-05

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: 45.76  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCKKLREEEAARLFYQIASAVA--HCHDGGLVLRDLKLRKfIFKDEERTRVKLESLEDAYILRGDddSLSDK 177
Cdd:cd14033   89 GTLKTYLKRFREMKLKLLQRWSRQILKGLHflHSRCPPILHRDLKCDN-IFITGPTGSVKIGDLGLATLKRAS--FAKSV 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 178 HGCPAYVSPEILNTSgsYSgKAADVWSLGVMLYTMLVGRYPFHDIEPSS-LFSKIRRG-------QFNIPETlspkaKCL 249
Cdd:cd14033  166 IGTPEFMAPEMYEEK--YD-EAVDVYAFGMCILEMATSEYPYSECQNAAqIYRKVTSGikpdsfyKVKVPEL-----KEI 237

                        170       180
                 ....*....|....*....|....
gi 568977678 250 IRSILRREPSERLTSQEILDHPWF 273
Cdd:cd14033  238 IEGCIRTDKDERFTIQDLLEHRFF 261
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
 100-261 1.59e-05

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 45.34  E-value: 1.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESLEDAyiLRGDDDSLSDK-H 178
Cdd:cd05116   80 GPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKA--LRADENYYKAQtH 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 179 G-CPA-YVSPEILNTSgSYSGKaADVWSLGVMLYTML-VGRYPFHDIEPSSLFSKIRRGQ-FNIPETLSPKAKCLIRSIL 254
Cdd:cd05116  158 GkWPVkWYAPECMNYY-KFSSK-SDVWSFGVLMWEAFsYGQKPYKGMKGNEVTQMIEKGErMECPAGCPPEMYDLMKLCW 235


                 ....*..
gi 568977678 255 RREPSER 261
Cdd:cd05116  236 TYDVDER 242
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
 122-273 1.59e-05

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 46.18  E-value: 1.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 122 YQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTrVKLESLEDAYILRGDDDSLSdkHGCPA-YVSPEILNTSGSYSGKAa 200
Cdd:PTZ00036 177 YQLCRALAYIHSKFICHRDLKPQNLLIDPNTHT-LKLCDFGSAKNLLAGQRSVS--YICSRfYRAPELMLGATNYTTHI- 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 201 DVWSLGVMLYTMLVGrYP--------------------------------FHDIEPSSLFSKIRRGQFniPETLSPKAKC 248
Cdd:PTZ00036 253 DLWSLGCIIAEMILG-YPifsgqssvdqlvriiqvlgtptedqlkemnpnYADIKFPDVKPKDLKKVF--PKGTPDDAIN 329

                        170       180
                 ....*....|....*....|....*
gi 568977678 249 LIRSILRREPSERLTSQEILDHPWF 273
Cdd:PTZ00036 330 FISQFLKYEPLKRLNPIEALADPFF 354
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
 30-213 1.75e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 46.23  E-value: 1.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  30 TEREQARRARTHTRTH-SRARSEIPGHV---FEISCYQESLAPCFCLSAHSNINQITEILLGETKAYVFFERSYGDMHSF 105
Cdd:PHA03210 173 TEEAEARRGVNSTNQGkPKCERLIAKRVkagSRAAIQLENEILALGRLNHENILKIEEILRSEANTYMITQKYDFDLYSF 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 106 V-------RTCKKLREEEaaRLFYQIASAVAHCHDGGLVLRDLKLRKfIFKDEERTRVklesLED-AYILRGDDDSLSDK 177
Cdd:PHA03210 253 MydeafdwKDRPLLKQTR--AIMKQLLCAVEYIHDKKLIHRDIKLEN-IFLNCDGKIV----LGDfGTAMPFEKEREAFD 325

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568977678 178 HGCPAYV---SPEILntSGSYSGKAADVWSLGVMLYTML 213
Cdd:PHA03210 326 YGWVGTVatnSPEIL--AGDGYCEITDIWSCGLILLDML 362
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
 75-273 1.97e-05

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 45.43  E-value: 1.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILL--GETKAYVFFERSYGDM------HSFVRTCKK---LREEEAARLFYQIASAVAHCHDGGLVLRDLKL 143
Cdd:cd07868   73 HPNVISLQKVFLshADRKVWLLFDYAEHDLwhiikfHRASKANKKpvqLPRGMVKSLLYQILDGIHYLHANWVLHRDLKP 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 144 RKFIFKDE--ERTRVKLESLEDAYILRGDDDSLSDKHGCPA---YVSPEILNTSGSYSgKAADVWSLGVMLYTMLVGRYP 218
Cdd:cd07868  153 ANILVMGEgpERGRVKIADMGFARLFNSPLKPLADLDPVVVtfwYRAPELLLGARHYT-KAIDIWAIGCIFAELLTSEPI 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 219 FH----DI---------------------------------EPSSLFSKIRRGQFN--------IPETLSPKAKC--LIR 251
Cdd:cd07868  232 FHcrqeDIktsnpyhhdqldrifnvmgfpadkdwedikkmpEHSTLMKDFRRNTYTncslikymEKHKVKPDSKAfhLLQ 311

                        250       260
                 ....*....|....*....|..
gi 568977678 252 SILRREPSERLTSQEILDHPWF 273
Cdd:cd07868  312 KLLTMDPIKRITSEQAMQDPYF 333
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
 105-270 2.30e-05

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: 45.00  E-value: 2.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 105 FVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEerTRVKLESLEDAYILRGDDDSLSDKHGCPAYV 184
Cdd:cd06638  114 FLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTE--GGVKLVDFGVSAQLTSTRLRRNTSVGTPFWM 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 185 SPEIL----NTSGSYSGKAaDVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRG---QFNIPETLSPKAKCLIRSILRRE 257
Cdd:cd06638  192 APEVIaceqQLDSTYDARC-DVWSLGITAIELGDGDPPLADLHPMRALFKIPRNpppTLHQPELWSNEFNDFIRKCLTKD 270

                        170
                 ....*....|...
gi 568977678 258 PSERLTSQEILDH 270
Cdd:cd06638  271 YEKRPTVSDLLQH 283
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
 162-269 2.82e-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: 44.83  E-value: 2.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 162 EDAYILRGDDDSLSDKHGCPAYVSPEILNTSGSYSGKaADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKI--RRGQFNIP 239
Cdd:cd14064  141 ESRFLQSLDEDNMTKQPGNLRWMAPEVFTQCTRYSIK-ADVFSYALCLWELLTGEIPFAHLKPAAAAADMayHHIRPPIG 219

                         90       100       110
                 ....*....|....*....|....*....|....
gi 568977678 240 ETLsPKAkclIRSILRR----EPSERLTSQEILD 269
Cdd:cd14064  220 YSI-PKP---ISSLLMRgwnaEPESRPSFVEIVA 249
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
 111-273 3.12e-05

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: 44.62  E-value: 3.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 111 KLREEEAARLFYQIASAVAHCH-DGGLVLRDL-------------KLRKFIF--KDEERTRvkleslEDAYILRGDDDSL 174
Cdd:cd14011  110 KLYDVEIKYGLLQISEALSFLHnDVKLVHGNIcpesvvinsngewKLAGFDFciSSEQATD------QFPYFREYDPNLP 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 175 SDKHGCPAYVSPE-ILNTSgsySGKAADVWSLGVMLYTMLVGRYPFHD-----IEPSSLFSKIRRGQFNIPETLSPKAKC 248
Cdd:cd14011  184 PLAQPNLNYLAPEyILSKT---CDPASDMFSLGVLIYAIYNKGKPLFDcvnnlLSYKKNSNQLRQLSLSLLEKVPEELRD 260

                        170       180
                 ....*....|....*....|....*
gi 568977678 249 LIRSILRREPSERLTSQEILDHPWF 273
Cdd:cd14011  261 HVKTLLNVTPEVRPDAEQLSKIPFF 285
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
 72-268 4.42e-05

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


Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 44.17  E-value: 4.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  72 LSAHSNINQITEILLGETKAYVFfeRSY--GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKfifk 149
Cdd:cd13980   54 LLELPNVLPFQKVIETDKAAYLI--RQYvkYNLYDRISTRPFLNLIEKKWIAFQLLHALNQCHKRGVCHGDIKTEN---- 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 150 deertrVKLESLEDAYI----------LRGDDDSL-------SDKHGCpaYVSPEILNTSGSYSG----------KAADV 202
Cdd:cd13980  128 ------VLVTSWNWVYLtdfasfkptyLPEDNPADfsyffdtSRRRTC--YIAPERFVDALTLDAeserrdgeltPAMDI 199

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568977678 203 WSLG-VMLYTMLVGRYPFhdiEPSSLFSkIRRGQFNIPETLS----PKAKCLIRSILRREPSERLTSQEIL 268
Cdd:cd13980  200 FSLGcVIAELFTEGRPLF---DLSQLLA-YRKGEFSPEQVLEkiedPNIRELILHMIQRDPSKRLSAEDYL 266
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
 58-223 5.02e-05

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: 43.86  E-value: 5.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  58 EISCYQESL---APCFCLSAHSNINQITEILLGETKAYVFFERSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDG 134
Cdd:cd14147   41 DISVTAESVrqeARLFAMLAHPNIIALKAVCLEEPNLCLVMEYAAGGPLSRALAGRRVPPHVLVNWAVQIARGMHYLHCE 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 135 GLV---LRDLKLRKFIFKDEertrVKLESLEDAYILRGDDDSLSDKH--------GCPAYVSPEILNTSGSysGKAADVW 203
Cdd:cd14147  121 ALVpviHRDLKSNNILLLQP----IENDDMEHKTLKITDFGLAREWHkttqmsaaGTYAWMAPEVIKASTF--SKGSDVW 194

                        170       180
                 ....*....|....*....|
gi 568977678 204 SLGVMLYTMLVGRYPFHDIE 223
Cdd:cd14147  195 SFGVLLWELLTGEVPYRGID 214
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
115-219 5.93e-05

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 44.40  E-value: 5.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 115 EEAARLFYQIASAVAHCHDGGLVLRDLK----LrkfIFKDEertRVKL----------ESledayilrgdddSLSDKH-- 178
Cdd:NF033483 107 EEAVEIMIQILSALEHAHRNGIVHRDIKpqniL---ITKDG---RVKVtdfgiaralsST------------TMTQTNsv 168

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 568977678 179 -GCPAYVSPEIlnTSGSYSGKAADVWSLGVMLYTMLVGRYPF 219
Cdd:NF033483 169 lGTVHYLSPEQ--ARGGTVDARSDIYSLGIVLYEMLTGRPPF 208
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
 119-240 6.54e-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: 43.80  E-value: 6.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 119 RLFYQIASAVAHCHDGGLVLRDLKLRK-FIFKDEERTRVKLEsLEDAYILRGD-DDSLSDKHGCPAYVSPEIlnTSGSYS 196
Cdd:cd14067  118 KIAYQIAAGLAYLHKKNIIFCDLKSDNiLVWSLDVQEHINIK-LSDYGISRQSfHEGALGVEGTPGYQAPEI--RPRIVY 194

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568977678 197 GKAADVWSLGVMLYTMLVGRYP---FHDIEPSSLFSKIRRGQFNIPE 240
Cdd:cd14067  195 DEKVDMFSYGMVLYELLSGQRPslgHHQLQIAKKLSKGIRPVLGQPE 241
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
 74-246 7.40e-05

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: 43.40  E-value: 7.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  74 AHSNINQITEILLGETKAYVFFE-RSYGDMHSFVRTCK-KLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKde 151
Cdd:cd05112   57 SHPKLVQLYGVCLEQAPICLVFEfMEHGCLSDYLRTQRgLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVG-- 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 152 ERTRVKLESLEDAYILRgdDDSLSDKHGCP---AYVSPEILnTSGSYSGKAaDVWSLGVMLYTMLV-GRYPFHDIEPSSL 227
Cdd:cd05112  135 ENQVVKVSDFGMTRFVL--DDQYTSSTGTKfpvKWSSPEVF-SFSRYSSKS-DVWSFGVLMWEVFSeGKIPYENRSNSEV 210

                        170
                 ....*....|....*....
gi 568977678 228 FSKIRRGQFNIPETLSPKA 246
Cdd:cd05112  211 VEDINAGFRLYKPRLASTH 229
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
 181-261 7.40e-05

Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. ILK contains N-terminal ankyrin repeats, a Pleckstrin Homology (PH) domain, and a C-terminal pseudokinase domain. It is a component of the IPP (ILK/PINCH/Parvin) complex that couples beta integrins to the actin cytoskeleton, and plays important roles in cell adhesion, spreading, invasion, and migration. ILK was initially thought to be an active kinase despite the lack of key conserved residues because of in vitro studies showing that it can phosphorylate certain protein substrates. However, in vivo experiments in Caenorhabditis elegans, Drosophila melanogaster, and mice (ILK-null and knock-in) proved that ILK is not an active kinase. In addition to actin cytoskeleton regulation, ILK also influences the microtubule network and mitotic spindle orientation. The pseudokinase domain of ILK binds several adaptor proteins including the parvins and paxillin. The ILK 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: 270959 [Multi-domain]  Cd Length: 251  Bit Score: 43.25  E-value: 7.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 181 PAYVSPEILNTS-GSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIR-RG-QFNIPETLSPKAKCLIRSILRRE 257
Cdd:cd14057  155 PAWMAPEALQKKpEDINRRSADMWSFAILLWELVTREVPFADLSNMEIGMKIAlEGlRVTIPPGISPHMCKLMKICMNED 234


                 ....
gi 568977678 258 PSER 261
Cdd:cd14057  235 PGKR 238
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
 123-270 8.97e-05

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


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 43.10  E-value: 8.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 123 QIASAVAHCHDGGLV---LRDLKLRKFIFkdeertrvkLESLEDAYI----LRGDDDSLSDK---------HGCPAYVSP 186
Cdd:cd14146  110 QIARGMLYLHEEAVVpilHRDLKSSNILL---------LEKIEHDDIcnktLKITDFGLAREwhrttkmsaAGTYAWMAP 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 187 EILNTSgsYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFN--IPETL-SPKAKcLIRSILRREPSERLT 263
Cdd:cd14146  181 EVIKSS--LFSKGSDIWSYGVLLWELLTGEVPYRGIDGLAVAYGVAVNKLTlpIPSTCpEPFAK-LMKECWEQDPHIRPS 257


                 ....*..
gi 568977678 264 SQEILDH 270
Cdd:cd14146  258 FALILEQ 264
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
 137-268 1.04e-04

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: 42.99  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 137 VLRDLKLRKFIFKDEERTRV-------KLESLEDAYILRGDDDSlsdkhgcPAY-VSPEILNTSGSYsgKAADVWSLGVM 208
Cdd:cd05079  131 VHRDLAARNVLVESEHQVKIgdfgltkAIETDKEYYTVKDDLDS-------PVFwYAPECLIQSKFY--IASDVWSFGVT 201

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568977678 209 LYTMLVgrYPFHDIEPSSLFSKI---RRGQFNI---------------PETLSPKAKCLIRSILRREPSERLTSQEIL 268
Cdd:cd05079  202 LYELLT--YCDSESSPMTLFLKMigpTHGQMTVtrlvrvleegkrlprPPNCPEEVYQLMRKCWEFQPSKRTTFQNLI 277
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
 100-267 1.07e-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: 43.31  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVRTCKKLREEEAArLFYQIASAVAHCHDGGLVLRDLKLRKFIF---KDEERTRVK---LESLEDAYILRGDDDS 173
Cdd:cd13977  120 GDMNEYLLSRRPDRQTNTS-FMLQLSSALAFLHRNQIVHRDLKPDNILIshkRGEPILKVAdfgLSKVCSGSGLNPEEPA 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 174 LSDKH------GCPAYVSPEILntSGSYSGKAaDVWSLGVMLYTMlVGRYPFHDIEPSS--LFSKIRRG----------- 234
Cdd:cd13977  199 NVNKHflssacGSDFYMAPEVW--EGHYTAKA-DIFALGIIIWAM-VERITFRDGETKKelLGTYIQQGkeivplgeall 274

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568977678 235 -----QFNIP----ETLSPKAKCLIRSILRREPSERLTSQEI 267
Cdd:cd13977  275 enpklELQIPlkkkKSMNDDMKQLLRDMLAANPQERPDAFQL 316
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
 122-274 1.13e-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: 43.07  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 122 YQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESL-EDAY----ILRGDDDSLSDKHGCPAYVSPEILNTSgsys 196
Cdd:cd14207  187 FQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLaRDIYknpdYVRKGDARLPLKWMAPESIFDKIYSTK---- 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 197 gkaADVWSLGVMLYTML-VGRYPFHDIE-PSSLFSKIRRG-QFNIPETLSPKAKCLIRSILRREPSERltsqeildhPWF 273
Cdd:cd14207  263 ---SDVWSYGVLLWEIFsLGASPYPGVQiDEDFCSKLKEGiRMRAPEFATSEIYQIMLDCWQGDPNER---------PRF 330


                 .
gi 568977678 274 S 274
Cdd:cd14207  331 S 331
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
 100-268 1.95e-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: 42.36  E-value: 1.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 100 GDMHSFVR-TCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRV-------KLESLEDAYILRGDD 171
Cdd:cd05033   90 GSLDKFLReNDGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVsdfglsrRLEDSEATYTTKGGK 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 172 DSLSdkhgcpaYVSPEILnTSGSYSgKAADVWSLGVMLY-TMLVGRYPFHDIEPSSLFSKIRRGqFNIPetlsPKAKC-- 248
Cdd:cd05033  170 IPIR-------WTAPEAI-AYRKFT-SASDVWSFGIVMWeVMSYGERPYWDMSNQDVIKAVEDG-YRLP----PPMDCps 235

                        170       180
                 ....*....|....*....|....
gi 568977678 249 ----LIRSILRREPSERLTSQEIL 268
Cdd:cd05033  236 alyqLMLDCWQKDRNERPTFSQIV 259
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
 123-221 2.59e-04

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: 41.87  E-value: 2.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 123 QIASAVAHCHDGG---LVLRDLKLRKfIFKDEERTrVKLESLEDAYILRGDDD--SLSDKHGCPAYVSPEILnTSGSYSG 197
Cdd:cd14066  101 GIARGLEYLHEECpppIIHGDIKSSN-ILLDEDFE-PKLTDFGLARLIPPSESvsKTSAVKGTIGYLAPEYI-RTGRVST 177

                         90       100
                 ....*....|....*....|....
gi 568977678 198 KAaDVWSLGVMLYTMLVGRYPFHD 221
Cdd:cd14066  178 KS-DVYSFGVVLLELLTGKPAVDE 200
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
 123-235 3.07e-04

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: 41.63  E-value: 3.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 123 QIASAVAHCHDGGLVLRDLKLRKFIFKdeERTRVKLESLEDAYILRGDDDSLSDKHG-CP-AYVSPEILnTSGSYSGKaA 200
Cdd:cd05057  117 QIAKGMSYLEEKRLVHRDLAARNVLVK--TPNHVKITDFGLAKLLDVDEKEYHAEGGkVPiKWMALESI-QYRIYTHK-S 192

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568977678 201 DVWSLGVMLYTMLV-GRYPFHDIEPSSLFSKIRRGQ 235
Cdd:cd05057  193 DVWSYGVTVWELMTfGAKPYEGIPAVEIPDLLEKGE 228
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
 200-267 3.35e-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: 41.49  E-value: 3.35e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 200 ADVWSLGVMLYTMLV-GRYPFHDIEPSSLFSKIRRG-QFNIPETLSPKAKCLIRSILRREPSERLTSQEI 267
Cdd:cd05092  205 SDIWSFGVVLWEIFTyGKQPWYQLSNTEAIECITQGrELERPRTCPPEVYAIMQGCWQREPQQRHSIKDI 274
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
 172-218 3.45e-04

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: 41.58  E-value: 3.45e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 568977678 172 DSLSDKH-GCPAYVSPEILNtsGSYSGKAADVWSLGVMLYTMLVGRYP 218
Cdd:cd06650  156 DSMANSFvGTRSYMSPERLQ--GTHYSVQSDIWSMGLSLVEMAVGRYP 201
pknD PRK13184
serine/threonine-protein kinase PknD;
110-264 3.57e-04

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 42.06  E-value: 3.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 110 KKLREEEAA----RLFYQIASAVAHCHDGGLVLRDLK-----LRKF-----------IFKdeertrvKLESLEDAYILRG 169
Cdd:PRK13184 104 KELAEKTSVgaflSIFHKICATIEYVHSKGVLHRDLKpdnilLGLFgevvildwgaaIFK-------KLEEEDLLDIDVD 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 170 DDDSLSDKH-------GCPAYVSPEILntSGSYSGKAADVWSLGVMLYTMLVGRYPF-----------HDIEPSSLFSKI 231
Cdd:PRK13184 177 ERNICYSSMtipgkivGTPDYMAPERL--LGVPASESTDIYALGVILYQMLTLSFPYrrkkgrkisyrDVILSPIEVAPY 254

                        170       180       190
                 ....*....|....*....|....*....|...
gi 568977678 232 RrgqfNIPETLSPKAkcliRSILRREPSERLTS 264
Cdd:PRK13184 255 R----EIPPFLSQIA----MKALAVDPAERYSS 279
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
 112-271 4.05e-04

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: 40.46  E-value: 4.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678   112 LREEEAARLFYQIASAVAHCHDGGlvlrdlKLRkFIFkDEERTRVKLESledAYILRGDDDSLSDkhgcPAYVSPEILnt 191
Cdd:smart00750  14 LNEEEIWAVCLQCLGALRELHRQA------KSG-NIL-LTWDGLLKLDG---SVAFKTPEQSRPD----PYFMAPEVI-- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678   192 SGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRrgqFNIPETLSPKAKCLIRSILR-------------REP 258
Cdd:smart00750  77 QGQSYTEKADIYSLGITLYEALDYELPYNEERELSAILEIL---LNGMPADDPRDRSNLEGVSAarsfedfmrlcasRLP 153

                          170
                   ....*....|...
gi 568977678   259 SERLTSQEILDHP 271
Cdd:smart00750 154 QRREAANHYLAHC 166
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
 86-235 4.33e-04

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk3, also called lemur tyrosine kinase 3 (Lmtk3) is a receptor kinase containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. The function of Aatyk3 is still unknown. The Aatyk3 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: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 41.09  E-value: 4.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  86 LGETKAYVFFERSYGDMHSFVRTCKKLREEeaaRLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESL---- 161
Cdd:cd14206   81 LGDLKRYLRAQRKADGMTPDLPTRDLRTLQ---RMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYGLshnn 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 162 --EDAYIlrgdddsLSDKHGCP-AYVSPEILntsGSYSG--------KAADVWSLGVMLYTML-VGRYPFHDIEPSSLFS 229
Cdd:cd14206  158 ykEDYYL-------TPDRLWIPlRWVAPELL---DELHGnlivvdqsKESNVWSLGVTIWELFeFGAQPYRHLSDEEVLT 227


                 ....*.
gi 568977678 230 KIRRGQ 235
Cdd:cd14206  228 FVVREQ 233
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
 75-261 4.38e-04

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 41.07  E-value: 4.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFERSYG-DMHSFVRT-CKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEE 152
Cdd:cd05084   53 HPNIVRLIGVCTQKQPIYIVMELVQGgDFLTFLRTeGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKN 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 153 RTRVkleslEDAYILRGDDDSLSDKHG----CPA-YVSPEILNTsGSYSGKAaDVWSLGVMLY-TMLVGRYPFHDIEPSS 226
Cdd:cd05084  133 VLKI-----SDFGMSREEEDGVYAATGgmkqIPVkWTAPEALNY-GRYSSES-DVWSFGILLWeTFSLGAVPYANLSNQQ 205

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 568977678 227 LFSKIRRG-QFNIPETLSPKAKCLIRSILRREPSER 261
Cdd:cd05084  206 TREAVEQGvRLPCPENCPDEVYRLMEQCWEYDPRKR 241
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
 119-273 4.45e-04

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: 41.38  E-value: 4.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 119 RLF-YQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLesledayIlrgDDDSlsdkhGCPA------------YVS 185
Cdd:cd14210  119 RKFaKQILQALQFLHKLNIIHCDLKPENILLKQPSKSSIKV-------I---DFGS-----SCFEgekvytyiqsrfYRA 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 186 PE-ILNTSgsYsGKAADVWSLGVMLYTMLVGRYPF-----HD-----IE-----PSSLFSKIRRGQ--FNI-----PETL 242
Cdd:cd14210  184 PEvILGLP--Y-DTAIDMWSLGCILAELYTGYPLFpgeneEEqlaciMEvlgvpPKSLIDKASRRKkfFDSngkprPTTN 260

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568977678 243 S------PKAKCL--------------IRSILRREPSERLTSQEILDHPWF 273
Cdd:cd14210  261 SkgkkrrPGSKSLaqvlkcddpsfldfLKKCLRWDPSERMTPEEALQHPWI 311
YegI COG4248
Uncharacterized conserved protein YegI with protein kinase and helix-hairpin-helix DNA-binding ...
 124-251 4.47e-04

Uncharacterized conserved protein YegI with protein kinase and helix-hairpin-helix DNA-binding domains [General function prediction only];


Pssm-ID: 443390 [Multi-domain]  Cd Length: 476  Bit Score: 41.61  E-value: 4.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 124 IASAVAHCHDGGLVLRDLKLRKFIFKDeeRTRVKLesledayIlrgDDDSLSDKH---------GCPAYVSPEILNTSGS 194
Cdd:COG4248  130 LAAAVAALHAAGYVHGDVNPSNILVSD--TALVTL-------I---DTDSFQVRDpgkvyrcvvGTPEFTPPELQGKSFA 197

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568977678 195 YSGKAA--DVWSLGVMLYTML-VGRYPF-----HDIEPSSLFSKIRRGQFnipeTLSPKAKCLIR 251
Cdd:COG4248  198 RVDRTEehDRFGLAVLIFQLLmEGRHPFsgvyqGDGDDPTLEERIAMGHF----VYHPNRRVLIR 258
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
 75-261 5.08e-04

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: 41.01  E-value: 5.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFERSYGDMHSFVRTCKKLREEEAARLFY--QIASAVAHCHDGGLVLRDLKLRKFIFKDEE 152
Cdd:cd05083   58 HKNLVRLLGVILHNGLYIVMELMSKGNLVNFLRSRGRALVPVIQLLQFslDVAEGMEYLESKKLVHRDLAARNILVSEDG 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 153 RTRVKLESLEDAYiLRGDDDSLsdkhgCPA-YVSPEILNtSGSYSGKAaDVWSLGVMLYTML-VGRYPFHDIEPSSLFSK 230
Cdd:cd05083  138 VAKISDFGLAKVG-SMGVDNSR-----LPVkWTAPEALK-NKKFSSKS-DVWSYGVLLWEVFsYGRAPYPKMSVKEVKEA 209

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568977678 231 IRRG-QFNIPETLSPKAKCLIRSILRREPSER 261
Cdd:cd05083  210 VEKGyRMEPPEGCPPDVYSIMTSCWEAEPGKR 241
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
 72-261 5.56e-04

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 41.14  E-value: 5.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  72 LSAHSNInqITEILLGETKAYVFFE---RSYGDMHSFVRTCKKLREEEA------------ARLFYQIASAVA----HCH 132
Cdd:cd05089   59 LGHHPNI--INLLGACENRGYLYIAieyAPYGNLLDFLRKSRVLETDPAfakehgtastltSQQLLQFASDVAkgmqYLS 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 133 DGGLVLRDLKLRKFIFKDEERTRVKlesleDAYILRGDDDSLSDKHG-CPA-YVSPEILNTSgSYSGKAaDVWSLGVMLY 210
Cdd:cd05089  137 EKQFIHRDLAARNVLVGENLVSKIA-----DFGLSRGEEVYVKKTMGrLPVrWMAIESLNYS-VYTTKS-DVWSFGVLLW 209

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568977678 211 TML-VGRYPFHDIEPSSLFSKIRRG-QFNIPETLSPKAKCLIRSILRREPSER 261
Cdd:cd05089  210 EIVsLGGTPYCGMTCAELYEKLPQGyRMEKPRNCDDEVYELMRQCWRDRPYER 262
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
 72-268 8.68e-04

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 40.41  E-value: 8.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  72 LSAHSNInqITEILLGETKAYVFFERSY---GDMHSFVR----------------TCKKLREEEAARLFYQIASAVAHCH 132
Cdd:cd05047   52 LGHHPNI--INLLGACEHRGYLYLAIEYaphGNLLDFLRksrvletdpafaiansTASTLSSQQLLHFAADVARGMDYLS 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 133 DGGLVLRDLKLRKFIFKDEERTRVKlesleDAYILRGDDDSLSDKHG-CPA-YVSPEILNTSgSYSGKAaDVWSLGVMLY 210
Cdd:cd05047  130 QKQFIHRDLAARNILVGENYVAKIA-----DFGLSRGQEVYVKKTMGrLPVrWMAIESLNYS-VYTTNS-DVWSYGVLLW 202

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 211 TML-VGRYPFHDIEPSSLFSKIRRG-QFNIPETLSPKAKCLIRSILRREPSERLTSQEIL 268
Cdd:cd05047  203 EIVsLGGTPYCGMTCAELYEKLPQGyRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 262
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
 102-235 8.91e-04

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 40.34  E-value: 8.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 102 MHSFVRTCKKLREEEAARLFYQ-IASAVAHCHDGGLVLRDLKlRKFIFKDEER---TRVKLESLEDAYILRGDDDSLSDK 177
Cdd:cd14152   83 LYSFVRDPKTSLDINKTRQIAQeIIKGMGYLHAKGIVHKDLK-SKNVFYDNGKvviTDFGLFGISGVVQEGRRENELKLP 161

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568977678 178 HGCPAYVSPEILNTSGSYSG-------KAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQ 235
Cdd:cd14152  162 HDWLCYLAPEIVREMTPGKDedclpfsKAADVYAFGTIWYELQARDWPLKNQPAEALIWQIGSGE 226
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
 119-269 8.93e-04

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: 39.94  E-value: 8.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 119 RLFYQIASAVAHCHDGGLVLRDLKLRK---FIFKDEERTRVKLESLEDA-YILRGdddSLSDKHGCPAYVSPEILNTSGS 194
Cdd:cd14068   90 RIALHVADGLRYLHSAMIIYRDLKPHNvllFTLYPNCAIIAKIADYGIAqYCCRM---GIKTSEGTPGFRAPEVARGNVI 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 195 YSgKAADVWSLGVMLYTMLVGRYPFHD-IEPSSLFSKIRRgQFNIPETLS-------PKAKCLIRSILRREPSERLTSQE 266
Cdd:cd14068  167 YN-QQADVYSFGLLLYDILTCGERIVEgLKFPNEFDELAI-QGKLPDPVKeygcapwPGVEALIKDCLKENPQCRPTSAQ 244


                 ...
gi 568977678 267 ILD 269
Cdd:cd14068  245 VFD 247
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
 96-215 9.89e-04

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: 40.17  E-value: 9.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  96 ERSYGDMHSFVRTCKKLREeeaaRLfyQIA----SAVAHCHDGGLVLRDLKLRKFIFKDEERTRV------KLESLEDAY 165
Cdd:cd13975   85 ERLHRDLYTGIKAGLSLEE----RL--QIAldvvEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKItdlgfcKPEAMMSGS 158

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 568977678 166 ILrgdddslsdkhGCPAYVSPEILntSGSYSgKAADVWSLGVMLYTMLVG 215
Cdd:cd13975  159 IV-----------GTPIHMAPELF--SGKYD-NSVDVYAFGILFWYLCAG 194
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
 98-273 1.93e-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: 39.18  E-value: 1.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  98 SYGDMHSFVRTCKKLRE----------EEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRV-----KLESLE 162
Cdd:cd05061   92 AHGDLKSYLRSLRPEAEnnpgrppptlQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIgdfgmTRDIYE 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 163 DAYILRGDDDSLSDKhgcpaYVSPEILNtSGSYSgKAADVWSLGVMLYTM-LVGRYPFHDIEPSSLFSKIRRGQF-NIPE 240
Cdd:cd05061  172 TDYYRKGGKGLLPVR-----WMAPESLK-DGVFT-TSSDMWSFGVVLWEItSLAEQPYQGLSNEQVLKFVMDGGYlDQPD 244

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568977678 241 TLSPKAKCLIRSILRREPSERLTSQEILD------HPWF 273
Cdd:cd05061  245 NCPERVTDLMRMCWQFNPKMRPTFLEIVNllkddlHPSF 283
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
 75-263 2.30e-03

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


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 38.90  E-value: 2.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILlGETKAYVFFE-RSYGDMHSFVR--TCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDE 151
Cdd:cd05071   63 HEKLVQLYAVV-SEEPIYIVTEyMSKGSLLDFLKgeMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGEN 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 152 ERTRVKLESLedAYILrgDDDSLSDKHGCP---AYVSPEILnTSGSYSGKaADVWSLGVMLYTMLV-GRYPFHDIEPSSL 227
Cdd:cd05071  142 LVCKVADFGL--ARLI--EDNEYTARQGAKfpiKWTAPEAA-LYGRFTIK-SDVWSFGILLTELTTkGRVPYPGMVNREV 215

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 568977678 228 FSKIRRG-QFNIPETLSPKAKCLIRSILRREPSERLT 263
Cdd:cd05071  216 LDQVERGyRMPCPPECPESLHDLMCQCWRKEPEERPT 252
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
 127-232 2.46e-03

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 39.06  E-value: 2.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 127 AVAHCHDGGLVLRDLKLRKfIFKDEERTRVkLESLEDAYILRGDDDSLSDkHGCPAYV---SPEILNTSgSYSGKAaDVW 203
Cdd:PHA03207 197 ALAYLHGRGIIHRDVKTEN-IFLDEPENAV-LGDFGAACKLDAHPDTPQC-YGWSGTLetnSPELLALD-PYCAKT-DIW 271

                         90       100
                 ....*....|....*....|....*....
gi 568977678 204 SLGVMLYTMLVGRYPFHDIEPSSLFSKIR 232
Cdd:PHA03207 272 SAGLVLFEMSVKNVTLFGKQVKSSSSQLR 300
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
 92-268 2.69e-03

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: 38.60  E-value: 2.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  92 YVFFERS-YGDMHSFVRTCKKLREEEAAR---------LFYQIASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKLESL 161
Cdd:cd05046   84 YMILEYTdLGDLKQFLRATKSKDEKLKPPplstkqkvaLCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSL 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 162 -EDAYilrGDDDSLSDKHGCPA-YVSPEILNtSGSYSGKaADVWSLGVMLYTMLV-GRYPFHDIEPSSLFSKIRRG--QF 236
Cdd:cd05046  164 sKDVY---NSEYYKLRNALIPLrWLAPEAVQ-EDDFSTK-SDVWSFGVLMWEVFTqGELPFYGLSDEEVLNRLQAGklEL 238

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568977678 237 NIPETLSPKAKCLIRSILRREPSERLTSQEIL 268
Cdd:cd05046  239 PVPEGCPSRLYKLMTRCWAVNPKDRPSFSELV 270
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
 172-247 2.73e-03

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: 38.88  E-value: 2.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 172 DSLSDKH-GCPAYVSPEILNtsGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRR----GQFNIPETLSPKA 246
Cdd:cd06649  156 DSMANSFvGTRSYMSPERLQ--GTHYSVQSDIWSMGLSLVELAIGRYPIPPPDAKELEAIFGRpvvdGEEGEPHSISPRP 233


                 .
gi 568977678 247 K 247
Cdd:cd06649  234 R 234
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
 124-218 3.66e-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: 3.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 124 IASAVAHCHDGGLVLRDLKLRKFIFKDEERTRVKL-------ESLEDAYILRGDDDSLSDKHGCPAYVSPEILNTSgSYS 196
Cdd:cd14065   98 IASGMAYLHSKNIIHRDLNSKNCLVREANRGRNAVvadfglaREMPDEKTKKPDRKKRLTVVGSPYWMAPEMLRGE-SYD 176

                         90       100
                 ....*....|....*....|..
gi 568977678 197 GKaADVWSLGVMLyTMLVGRYP 218
Cdd:cd14065  177 EK-VDVFSFGIVL-CEIIGRVP 196
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
 74-268 5.78e-03

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


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 37.55  E-value: 5.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  74 AHSNINQITEILLGETKAYVFFER-SYGDMHSFVR-TCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKDE 151
Cdd:cd05113   57 SHEKLVQLYGVCTKQRPIFIITEYmANGCLLNYLReMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQ 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 152 ERTRVKLESLEdAYILrgdDDSLSDKHGCPAYV---SPEILNTSgSYSGKAaDVWSLGVMLYTML-VGRYPFHDIEPSSL 227
Cdd:cd05113  137 GVVKVSDFGLS-RYVL---DDEYTSSVGSKFPVrwsPPEVLMYS-KFSSKS-DVWAFGVLMWEVYsLGKMPYERFTNSET 210

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568977678 228 FSKIRRG-QFNIPETLSPKAKCLIRSILRREPSERLTSQEIL 268
Cdd:cd05113  211 VEHVSQGlRLYRPHLASEKVYTIMYSCWHEKADERPTFKILL 252
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
 75-269 7.83e-03

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


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 37.43  E-value: 7.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678  75 HSNINQITEILLGETKAYVFFE-RSYGDMHSFVRTCK-KLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFIFKdeE 152
Cdd:cd05059   58 HPKLVQLYGVCTKQRPIFIVTEyMANGCLLNYLRERRgKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVG--E 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 153 RTRVKLESLEDA-YILrgdDDSLSDKHGCP---AYVSPEILNTSgSYSGKAaDVWSLGVMLYTMLV-GRYPFHDIEPSSL 227
Cdd:cd05059  136 QNVVKVSDFGLArYVL---DDEYTSSVGTKfpvKWSPPEVFMYS-KFSSKS-DVWSFGVLMWEVFSeGKMPYERFSNSEV 210

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 568977678 228 FSKIRRG-QFNIPETLSPKAKCLIRSILRREPSERLTSQEILD 269
Cdd:cd05059  211 VEHISQGyRLYRPHLAPTEVYTIMYSCWHEKPEERPTFKILLS 253
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
 183-267 7.88e-03

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: 37.37  E-value: 7.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 183 YVSPEILNTS-GSYSG-KAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFN--IPETLSPKAKC------LIRS 252
Cdd:cd13992  167 WTAPELLRGSlLEVRGtQKGDVYSFAIILYEILFRSDPFALEREVAIVEKVISGGNKpfRPELAVLLDEFpprlvlLVKQ 246

                         90
                 ....*....|....*
gi 568977678 253 ILRREPSERLTSQEI 267
Cdd:cd13992  247 CWAENPEKRPSFKQI 261
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
 183-268 8.00e-03

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: 37.32  E-value: 8.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 183 YVSPEILNtSGSYSGKAaDVWSLGVMLYTML-VGRYPFHDIEPSSLFSKI-RRGQFNIPETLSPKAKCLIRSILRREPSE 260
Cdd:cd05032  187 WMAPESLK-DGVFTTKS-DVWSFGVVLWEMAtLAEQPYQGLSNEEVLKFViDGGHLDLPENCPDKLLELMRMCWQYNPKM 264


                 ....*...
gi 568977678 261 RLTSQEIL 268
Cdd:cd05032  265 RPTFLEIV 272
PHA02988 PHA02988
hypothetical protein; Provisional
 182-269 8.42e-03

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 37.41  E-value: 8.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 182 AYVSPEILNTSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKI--RRGQFNIPETLSPKAKCLIRSILRREPS 259
Cdd:PHA02988 185 VYFSYKMLNDIFSEYTIKDDIYSLGVVLWEIFTGKIPFENLTTKEIYDLIinKNNSLKLPLDCPLEIKCIVEACTSHDSI 264

                         90
                 ....*....|
gi 568977678 260 ERLTSQEILD 269
Cdd:PHA02988 265 KRPNIKEILY 274
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
 179-276 8.80e-03

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: 37.34  E-value: 8.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568977678 179 GCPAYVSPEILNTSgsySGKAADVWSLGVMLYTMLVGRYPFHDIE-PSSLFSKIRRG--QFNIPETLSPKAKCLIRSILR 255
Cdd:cd14030  191 GTPEFMAPEMYEEK---YDESVDVYAFGMCMLEMATSEYPYSECQnAAQIYRRVTSGvkPASFDKVAIPEVKEIIEGCIR 267

                         90       100
                 ....*....|....*....|.
gi 568977678 256 REPSERLTSQEILDHPWFSTD 276
Cdd:cd14030  268 QNKDERYAIKDLLNHAFFQEE 288
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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