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Conserved domains on  [gi|1704602876|ref|NP_001358412|]
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MAP kinase-activated protein kinase 5 isoform 7 [Homo sapiens]

Protein Classification

protein kinase family protein( domain architecture ID 229378)

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

CATH:  1.10.510.10
PubMed:  16244704
SCOP:  4003661

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
15-274 1.42e-179

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 cd14171:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 289  Bit Score: 502.76  E-value: 1.42e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  15 SILEEYSINWTQKLGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLHMMCATHPNIVQIIEVFANSVQFPHESSP 94
Cdd:cd14171     1 SILEEYEVNWTQKLGTGISGPVRVCVKKSTGERFALKILLDRPKARTEVRLHMMCSGHPNIVQIYDVYANSVQFPGESSP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  95 RARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ------------------------------DAPVKLCDFGFAK 144
Cdd:cd14171    81 RARLLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQialavqhchslniahrdlkpenlllkdnseDAPIKLCDFGFAK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 145 IDQGDLMTPQFTPYYVAPQVLEAQRRHQKEKSGIIPTsPTPYTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDM 224
Cdd:cd14171   161 VDQGDLMTPQFTPYYVAPQVLEAQRRHRKERSGIPTS-PTPYTYDKSCDMWSLGVIIYIMLCGYPPFYSEHPSRTITKDM 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1704602876 225 RRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14171   240 KRKIMTGSYEFPEEEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
 
Name Accession Description Interval E-value
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
15-274 1.42e-179

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: 502.76  E-value: 1.42e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  15 SILEEYSINWTQKLGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLHMMCATHPNIVQIIEVFANSVQFPHESSP 94
Cdd:cd14171     1 SILEEYEVNWTQKLGTGISGPVRVCVKKSTGERFALKILLDRPKARTEVRLHMMCSGHPNIVQIYDVYANSVQFPGESSP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  95 RARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ------------------------------DAPVKLCDFGFAK 144
Cdd:cd14171    81 RARLLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQialavqhchslniahrdlkpenlllkdnseDAPIKLCDFGFAK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 145 IDQGDLMTPQFTPYYVAPQVLEAQRRHQKEKSGIIPTsPTPYTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDM 224
Cdd:cd14171   161 VDQGDLMTPQFTPYYVAPQVLEAQRRHRKERSGIPTS-PTPYTYDKSCDMWSLGVIIYIMLCGYPPFYSEHPSRTITKDM 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1704602876 225 RRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14171   240 KRKIMTGSYEFPEEEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
26-274 4.63e-63

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 204.30  E-value: 4.63e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876   26 QKLGAGISGPVRVCVKKSTQERFALKIL------LDRPKARNEVRLHMMCaTHPNIVQIIEVFansvQFPHEssprarLL 99
Cdd:smart00220   5 EKLGEGSFGKVYLARDKKTGKLVAIKVIkkkkikKDRERILREIKILKKL-KHPNIVRLYDVF----EDEDK------LY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  100 IVMEMMEGGELFHRISQHRHFTEKQASQVTKQ---------------------------DAPVKLCDFGFAK-IDQGDLM 151
Cdd:smart00220  74 LVMEYCEGGDLFDLLKKRGRLSEDEARFYLRQilsaleylhskgivhrdlkpenilldeDGHVKLADFGLARqLDPGEKL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  152 TPQF-TPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHsrtiPKDMRRKIMT 230
Cdd:smart00220 154 TTFVgTPEYMAPEVLLGKG------------------YGKAVDIWSLGVILYELLTGKPPFPGDDQ----LLELFKKIGK 211
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1704602876  231 GSFEFPEEEWSqISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:smart00220 212 PKPPFPPPEWD-ISPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
26-274 2.37e-50

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 169.73  E-value: 2.37e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKIL-LDRPK------ARNEVRLHMMCAtHPNIVQIIEVFANSvqfphessprARL 98
Cdd:pfam00069   5 RKLGSGSFGTVYKAKHRDTGKIVAIKKIkKEKIKkkkdknILREIKILKKLN-HPNIVRLYDAFEDK----------DNL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  99 LIVMEMMEGGELFHRISQHRHFTEKQASQVTKQdapvkLCDfGFAKidQGDLMTPQFTPYYVAPQVLEAQrrhqkeksgi 178
Cdd:pfam00069  74 YLVLEYVEGGSLFDLLSEKGAFSEREAKFIMKQ-----ILE-GLES--GSSLTTFVGTPWYMAPEVLGGN---------- 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 179 iptsptPYTynKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDMRRKIMtgsfefPEEEWSQISEMAKDVVRKLLKVK 258
Cdd:pfam00069 136 ------PYG--PKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYA------FPELPSNLSEEAKDLLKKLLKKD 201
                         250
                  ....*....|....*.
gi 1704602876 259 PEERLTIEGVLDHPWL 274
Cdd:pfam00069 202 PSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
13-262 3.13e-24

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 104.71  E-value: 3.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  13 ETSILEEYSInwTQKLGAGISGPVRVCVKKSTQERFALKILL----DRPKAR----NEVRLhMMCATHPNIVQIIEVFan 84
Cdd:COG0515     2 SALLLGRYRI--LRLLGRGGMGVVYLARDLRLGRPVALKVLRpelaADPEARerfrREARA-LARLNHPNIVRVYDVG-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  85 svqfphesSPRARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ---------------------------DAPVKL 137
Cdd:COG0515    77 --------EEDGRPYLVMEYVEGESLADLLRRRGPLPPAEALRILAQlaealaaahaagivhrdikpanilltpDGRVKL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 138 CDFGFAKIDQGDLMTPQ----FTPYYVAPQVLEAQRrhqkeksgiiptsPTPYTynkscDLWSLGVIIYVMLCGYPPFys 213
Cdd:COG0515   149 IDFGIARALGGATLTQTgtvvGTPGYMAPEQARGEP-------------VDPRS-----DVYSLGVTLYELLTGRPPF-- 208
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1704602876 214 khhSRTIPKDMRRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEER 262
Cdd:COG0515   209 ---DGDSPAELLRAHLREPPPPPSELRPDLPPALDAIVLRALAKDPEER 254
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
28-273 7.22e-24

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 101.43  E-value: 7.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLH-------MMCATHPNIVQIIEVFANsvqfphesspRARLLI 100
Cdd:PTZ00263   26 LGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHvaqeksiLMELSHPFIVNMMCSFQD----------ENRVYF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 101 VMEMMEGGELFHRISQHRHFTE---------------------------KQASQVTKQDAPVKLCDFGFAKIDQGDLMTP 153
Cdd:PTZ00263   96 LLEFVVGGELFTHLRKAGRFPNdvakfyhaelvlafeylhskdiiyrdlKPENLLLDNKGHVKVTDFGFAKKVPDRTFTL 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 154 QFTPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIpkdmrRKIMTGSF 233
Cdd:PTZ00263  176 CGTPEYLAPEVIQSK------------------GHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIY-----EKILAGRL 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1704602876 234 EFPeeEWsqISEMAKDVVRKLLKVKPEERL-----TIEGVLDHPW 273
Cdd:PTZ00263  233 KFP--NW--FDGRARDLVKGLLQTDHTKRLgtlkgGVADVKNHPY 273
 
Name Accession Description Interval E-value
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
15-274 1.42e-179

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: 502.76  E-value: 1.42e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  15 SILEEYSINWTQKLGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLHMMCATHPNIVQIIEVFANSVQFPHESSP 94
Cdd:cd14171     1 SILEEYEVNWTQKLGTGISGPVRVCVKKSTGERFALKILLDRPKARTEVRLHMMCSGHPNIVQIYDVYANSVQFPGESSP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  95 RARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ------------------------------DAPVKLCDFGFAK 144
Cdd:cd14171    81 RARLLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQialavqhchslniahrdlkpenlllkdnseDAPIKLCDFGFAK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 145 IDQGDLMTPQFTPYYVAPQVLEAQRRHQKEKSGIIPTsPTPYTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDM 224
Cdd:cd14171   161 VDQGDLMTPQFTPYYVAPQVLEAQRRHRKERSGIPTS-PTPYTYDKSCDMWSLGVIIYIMLCGYPPFYSEHPSRTITKDM 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1704602876 225 RRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14171   240 KRKIMTGSYEFPEEEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
19-273 3.57e-133

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: 383.95  E-value: 3.57e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  19 EYSINWtQKLGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLHMMCATHPNIVQIIEVFANSVQfphessPRARL 98
Cdd:cd14089     1 DYTISK-QVLGLGINGKVLECFHKKTGEKFALKVLRDNPKARREVELHWRASGCPHIVRIIDVYENTYQ------GRKCL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  99 LIVMEMMEGGELFHRISQH--RHFTEKQASQVTKQ------------------------------DAPVKLCDFGFAKID 146
Cdd:cd14089    74 LVVMECMEGGELFSRIQERadSAFTEREAAEIMRQigsavahlhsmniahrdlkpenllysskgpNAILKLTDFGFAKET 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 147 QGD--LMTPQFTPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRtIPKDM 224
Cdd:cd14089   154 TTKksLQTPCYTPYYVAPEVLGPEK------------------YDKSCDMWSLGVIMYILLCGYPPFYSNHGLA-ISPGM 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1704602876 225 RRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPW 273
Cdd:cd14089   215 KKRIRNGQYEFPNPEWSNVSEEAKDLIRGLLKTDPSERLTIEEVMNHPW 263
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
20-273 1.69e-82

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: 254.32  E-value: 1.69e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  20 YSInwTQKLGAGISGPVRVCVKKSTQERFALKIL-------LDRPKARNEVRLHMMCAtHPNIVQIIEVFANsvqfphes 92
Cdd:cd05117     2 YEL--GKVLGRGSFGVVRLAVHKKTGEEYAVKIIdkkklksEDEEMLRREIEILKRLD-HPNIVKLYEVFED-------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  93 spRARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ------------------------------DAPVKLCDFGF 142
Cdd:cd05117    71 --DKNLYLVMELCTGGELFDRIVKKGSFSEREAAKIMKQilsavaylhsqgivhrdlkpenillaskdpDSPIKIIDFGL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 143 AKI--DQGDLMTPQFTPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHsrti 220
Cdd:cd05117   149 AKIfeEGEKLKTVCGTPYYVAPEVLKGKG------------------YGKKCDIWSLGVILYILLCGYPPFYGETE---- 206
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1704602876 221 pKDMRRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPW 273
Cdd:cd05117   207 -QELFEKILKGKYSFDSPEWKNVSEEAKDLIKRLLVVDPKKRLTAAEALNHPW 258
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
28-303 8.44e-73

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: 231.42  E-value: 8.44e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLHMMCATHPNIVQIIEVFANSVQFphessprarlLIVMEMMEG 107
Cdd:cd14092    14 LGDGSFSVCRKCVHKKTGQEFAVKIVSRRLDTSREVQLLRLCQGHPNIVKLHEVFQDELHT----------YLVMELLRG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 108 GELFHRISQHRHFTEKQASQVTKQ------------------------------DAPVKLCDFGFAKIDQGD--LMTPQF 155
Cdd:cd14092    84 GELLERIRKKKRFTESEASRIMRQlvsavsfmhskgvvhrdlkpenllftdeddDAEIKIVDFGFARLKPENqpLKTPCF 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 156 TPYYVAPQVLEaqrrhqkeksgiipTSPTPYTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDMRRkIMTGSFEF 235
Cdd:cd14092   164 TLPYAAPEVLK--------------QALSTQGYDESCDLWSLGVILYTMLSGQVPFQSPSRNESAAEIMKR-IKSGDFSF 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1704602876 236 PEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEALDN-------VLPSAQLMMDKAVVAGIQQAH 303
Cdd:cd14092   229 DGEEWKNVSSEAKSLIQGLLTVDPSKRLTMSELRNHPWLQGSSSPSStplmtpgVLSSSAAAVSTALRATFDAFH 303
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
16-274 2.90e-72

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: 228.34  E-value: 2.90e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  16 ILEEYSINwTQKLGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLHMMCATHPNIVQIIEVFANSvqfpHESspR 95
Cdd:cd14172     1 VTDDYKLS-KQVLGLGVNGKVLECFHRRTGQKCALKLLYDSPKARREVEHHWRASGGPHIVHILDVYENM----HHG--K 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  96 ARLLIVMEMMEGGELFHRISQH--RHFTEKQASQVTK------------------------------QDAPVKLCDFGFA 143
Cdd:cd14172    74 RCLLIIMECMEGGELFSRIQERgdQAFTEREASEIMRdigtaiqylhsmniahrdvkpenllytskeKDAVLKLTDFGFA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 144 K--IDQGDLMTPQFTPYYVAPQVLeaqrrhqkeksgiiptspTPYTYNKSCDLWSLGVIIYVMLCGYPPFYSkHHSRTIP 221
Cdd:cd14172   154 KetTVQNALQTPCYTPYYVAPEVL------------------GPEKYDKSCDMWSLGVIMYILLCGFPPFYS-NTGQAIS 214
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1704602876 222 KDMRRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14172   215 PGMKRRIRMGQYGFPNPEWAEVSEEAKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
18-277 1.70e-67

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: 217.59  E-value: 1.70e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  18 EEYSINwTQKLGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLHMMCATHPNIVQIIEVFANSVQfphessPRAR 97
Cdd:cd14170     1 DDYKVT-SQVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDVYENLYA------GRKC 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  98 LLIVMEMMEGGELFHRISQH--RHFTEKQASQVTKQ------------------------------DAPVKLCDFGFAK- 144
Cdd:cd14170    74 LLIVMECLDGGELFSRIQDRgdQAFTEREASEIMKSigeaiqylhsiniahrdvkpenllytskrpNAILKLTDFGFAKe 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 145 -IDQGDLMTPQFTPYYVAPQVLeaqrrhqkeksgiiptspTPYTYNKSCDLWSLGVIIYVMLCGYPPFYSkHHSRTIPKD 223
Cdd:cd14170   154 tTSHNSLTTPCYTPYYVAPEVL------------------GPEKYDKSCDMWSLGVIMYILLCGYPPFYS-NHGLAISPG 214
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1704602876 224 MRRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNST 277
Cdd:cd14170   215 MKTRIRMGQYEFPNPEWSEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQS 268
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
26-274 4.63e-63

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 204.30  E-value: 4.63e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876   26 QKLGAGISGPVRVCVKKSTQERFALKIL------LDRPKARNEVRLHMMCaTHPNIVQIIEVFansvQFPHEssprarLL 99
Cdd:smart00220   5 EKLGEGSFGKVYLARDKKTGKLVAIKVIkkkkikKDRERILREIKILKKL-KHPNIVRLYDVF----EDEDK------LY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  100 IVMEMMEGGELFHRISQHRHFTEKQASQVTKQ---------------------------DAPVKLCDFGFAK-IDQGDLM 151
Cdd:smart00220  74 LVMEYCEGGDLFDLLKKRGRLSEDEARFYLRQilsaleylhskgivhrdlkpenilldeDGHVKLADFGLARqLDPGEKL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  152 TPQF-TPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHsrtiPKDMRRKIMT 230
Cdd:smart00220 154 TTFVgTPEYMAPEVLLGKG------------------YGKAVDIWSLGVILYELLTGKPPFPGDDQ----LLELFKKIGK 211
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1704602876  231 GSFEFPEEEWSqISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:smart00220 212 PKPPFPPPEWD-ISPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
28-273 1.11e-61

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: 201.87  E-value: 1.11e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKIL-----LDRPKARNEVRLHMMCATHPNIVQIIEVFANsvqfphesspRARLLIVM 102
Cdd:cd14090    10 LGEGAYASVQTCINLYTGKEYAVKIIekhpgHSRSRVFREVETLHQCQGHPNILQLIEYFED----------DERFYLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 103 EMMEGGELFHRISQHRHFTEKQASQVTKQDA------------------------------PVKLCDFGFAK--IDQGDL 150
Cdd:cd14090    80 EKMRGGPLLSHIEKRVHFTEQEASLVVRDIAsaldflhdkgiahrdlkpenilcesmdkvsPVKICDFDLGSgiKLSSTS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 151 MTPQFTP---------YYVAPQVLEAqrrhqkeksgiipTSPTPYTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHS---- 217
Cdd:cd14090   160 MTPVTTPelltpvgsaEYMAPEVVDA-------------FVGEALSYDKRCDLWSLGVILYIMLCGYPPFYGRCGEdcgw 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1704602876 218 ------RTIPKDMRRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPW 273
Cdd:cd14090   227 drgeacQDCQELLFHSIQEGEYEFPEKEWSHISAEAKDLISHLLVRDASQRYTAEQVLQHPW 288
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
19-302 5.88e-55

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: 184.37  E-value: 5.88e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  19 EYSInwTQKLGAGISGPVRVCVKKSTQERFALKILlDRPK--ARNEVRLHMMCATHPNIVQIIEVFANSvqfphessprA 96
Cdd:cd14091     1 EYEI--KEEIGKGSYSVCKRCIHKATGKEYAVKII-DKSKrdPSEEIEILLRYGQHPNIITLRDVYDDG----------N 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  97 RLLIVMEMMEGGELFHRISQHRHFTEKQASQVTK------------------------------QDAP-VKLCDFGFAK- 144
Cdd:cd14091    68 SVYLVTELLRGGELLDRILRQKFFSEREASAVMKtltktveylhsqgvvhrdlkpsnilyadesGDPEsLRICDFGFAKq 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 145 --IDQGDLMTPQFTPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRtiPK 222
Cdd:cd14091   148 lrAENGLLMTPCYTANFVAPEVLKKQ------------------GYDAACDIWSLGVLLYTMLAGYTPFASGPNDT--PE 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 223 DMRRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEAL-DNVLPSAQLMMD-KAVVAGIQ 300
Cdd:cd14091   208 VILARIGSGKIDLSGGNWDHVSDSAKDLVRKMLHVDPSQRPTAAQVLQHPWIRNRDSLpQRQLTDPQDAALvKGAVAATF 287

                  ..
gi 1704602876 301 QA 302
Cdd:cd14091   288 RA 289
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
28-274 3.03e-52

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: 176.78  E-value: 3.03e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKIL-------------LDRPKARNEVRLHMMCATHPNIVQIIEVFansvqfphESSp 94
Cdd:cd14093    11 LGRGVSSTVRRCIEKETGQEFAVKIIditgeksseneaeELREATRREIEILRQVSGHPNIIELHDVF--------ESP- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  95 rARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ---------------------------DAPVKLCDFGFAK-ID 146
Cdd:cd14093    82 -TFIFLVFELCRKGELFDYLTEVVTLSEKKTRRIMRQlfeaveflhslnivhrdlkpenillddNLNVKISDFGFATrLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 147 QGDLMTPQF-TPYYVAPQVLeaqrrhqkeKSGIIPTSPTpytYNKSCDLWSLGVIIYVMLCGYPPFYskhHSRTIPkdMR 225
Cdd:cd14093   161 EGEKLRELCgTPGYLAPEVL---------KCSMYDNAPG---YGKEVDMWACGVIMYTLLAGCPPFW---HRKQMV--ML 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1704602876 226 RKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14093   224 RNIMEGKYEFGSPEWDDISDTAKDLISKLLVVDPKKRLTAEEALEHPFF 272
Pkinase pfam00069
Protein kinase domain;
26-274 2.37e-50

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 169.73  E-value: 2.37e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKIL-LDRPK------ARNEVRLHMMCAtHPNIVQIIEVFANSvqfphessprARL 98
Cdd:pfam00069   5 RKLGSGSFGTVYKAKHRDTGKIVAIKKIkKEKIKkkkdknILREIKILKKLN-HPNIVRLYDAFEDK----------DNL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  99 LIVMEMMEGGELFHRISQHRHFTEKQASQVTKQdapvkLCDfGFAKidQGDLMTPQFTPYYVAPQVLEAQrrhqkeksgi 178
Cdd:pfam00069  74 YLVLEYVEGGSLFDLLSEKGAFSEREAKFIMKQ-----ILE-GLES--GSSLTTFVGTPWYMAPEVLGGN---------- 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 179 iptsptPYTynKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDMRRKIMtgsfefPEEEWSQISEMAKDVVRKLLKVK 258
Cdd:pfam00069 136 ------PYG--PKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYA------FPELPSNLSEEAKDLLKKLLKKD 201
                         250
                  ....*....|....*.
gi 1704602876 259 PEERLTIEGVLDHPWL 274
Cdd:pfam00069 202 PSKRLTATQALQHPWF 217
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
28-273 3.54e-50

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: 170.63  E-value: 3.54e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILlDRPKAR-------NEVRLHMMCaTHPNIVQIIEVFANsvqfphesspRARLLI 100
Cdd:cd14083    11 LGTGAFSEVVLAEDKATGKLVAIKCI-DKKALKgkedsleNEIAVLRKI-KHPNIVQLLDIYES----------KSHLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 101 VMEMMEGGELFHRISQHRHFTEKQASQVTKQ------------------------------DAPVKLCDFGFAKI-DQGD 149
Cdd:cd14083    79 VMELVTGGELFDRIVEKGSYTEKDASHLIRQvleavdylhslgivhrdlkpenllyyspdeDSKIMISDFGLSKMeDSGV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 150 LMTPQFTPYYVAPQVLEaqrrhQKeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRtipkdMRRKIM 229
Cdd:cd14083   159 MSTACGTPGYVAPEVLA-----QK-------------PYGKAVDCWSIGVISYILLCGYPPFYDENDSK-----LFAQIL 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1704602876 230 TGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPW 273
Cdd:cd14083   216 KAEYEFDSPYWDDISDSAKDFIRHLMEKDPNKRYTCEQALEHPW 259
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
26-273 8.05e-50

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 169.62  E-value: 8.05e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKIL-LDRPKARNEVRL-----HMMCATHPNIVQIIEVFANSvqfphessprARLL 99
Cdd:cd14003     6 KTLGEGSFGKVKLARHKLTGEKVAIKIIdKSKLKEEIEEKIkreieIMKLLNHPNIIKLYEVIETE----------NKIY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMEGGELFHRISQHRHFTEKQASQVTKQ---------------------------DAPVKLCDFGFAKIDQGD--L 150
Cdd:cd14003    76 LVMEYASGGELFDYIVNNGRLSEDEARRFFQQlisavdychsngivhrdlklenilldkNGNLKIIDFGLSNEFRGGslL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 151 MTPQFTPYYVAPQVLEAQrrhqkeksgiiptsptPYtYNKSCDLWSLGVIIYVMLCGYPPFyskhHSRTIPKdMRRKIMT 230
Cdd:cd14003   156 KTFCGTPAYAAPEVLLGR----------------KY-DGPKADVWSLGVILYAMLTGYLPF----DDDNDSK-LFRKILK 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1704602876 231 GSFEFPeeewSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPW 273
Cdd:cd14003   214 GKYPIP----SHLSPDARDLIRRMLVVDPSKRITIEEILNHPW 252
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
11-293 3.07e-48

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: 166.71  E-value: 3.07e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  11 IKETSILEEYsinwtqkLGAGISGPVRVCVKKSTQERFALKILLDRPKAR-----NEVRLhMMCATHPNIVQIIEVFANS 85
Cdd:cd14166     1 IRETFIFMEV-------LGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRdssleNEIAV-LKRIKHENIVTLEDIYEST 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  86 VQFphessprarlLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ------------------------------DAPV 135
Cdd:cd14166    73 THY----------YLVMQLVSGGELFDRILERGVYTEKDASRVINQvlsavkylhengivhrdlkpenllyltpdeNSKI 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 136 KLCDFGFAKIDQGDLM-TPQFTPYYVAPQVLeAQRrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSK 214
Cdd:cd14166   143 MITDFGLSKMEQNGIMsTACGTPGYVAPEVL-AQK-----------------PYSKAVDCWSIGVITYILLCGYPPFYEE 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 215 HHSRtipkdMRRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEAL-DNVLPSAQLMMDK 293
Cdd:cd14166   205 TESR-----LFEKIKEGYYEFESPFWDDISESAKDFIRHLLEKNPSKRYTCEKALSHPWIIGNTALhRDIYPSVSEQIQK 279
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
26-273 1.02e-47

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: 164.42  E-value: 1.02e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKILlDRPKAR-------NEVRLhMMCATHPNIVQIIEVFANSVQfphessprarL 98
Cdd:cd14095     6 RVIGDGNFAVVKECRDKATDKEYALKII-DKAKCKgkehmieNEVAI-LRRVKHPNIVQLIEEYDTDTE----------L 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  99 LIVMEMMEGGELFHRISQHRHFTEKQASQ-----------------------------VTKQDAP--VKLCDFGFAKIDQ 147
Cdd:cd14095    74 YLVMELVKGGDLFDAITSSTKFTERDASRmvtdlaqalkylhslsivhrdikpenllvVEHEDGSksLKLADFGLATEVK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 148 GDLMTPQFTPYYVAPQVLEaqrrhqkeKSGiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTipkDMRRK 227
Cdd:cd14095   154 EPLFTVCGTPTYVAPEILA--------ETG----------YGLKVDIWAAGVITYILLCGFPPFRSPDRDQE---ELFDL 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1704602876 228 IMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPW 273
Cdd:cd14095   213 ILAGEFEFLSPYWDNISDSAKDLISRMLVVDPEKRYSAGQVLDHPW 258
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
18-290 2.54e-46

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: 162.13  E-value: 2.54e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  18 EEYSINWTQK-LGAGISGPVRVCVKKSTQERFALKILLDRPKA--RNEVRLHMMCATHPNIVQIIEVFANSVQfphessp 94
Cdd:cd14179     4 QHYELDLKDKpLGEGSFSICRKCLHKKTNQEYAVKIVSKRMEAntQREIAALKLCEGHPNIVKLHEVYHDQLH------- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  95 rarLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ------------------------------DAPVKLCDFGFAK 144
Cdd:cd14179    77 ---TFLVMELLKGGELLERIKKKQHFSETEASHIMRKlvsavshmhdvgvvhrdlkpenllftdesdNSEIKIIDFGFAR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 145 I---DQGDLMTPQFTPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSR--T 219
Cdd:cd14179   154 LkppDNQPLKTPCFTLHYAAPELLNYN------------------GYDESCDLWSLGVILYTMLSGQVPFQCHDKSLtcT 215
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1704602876 220 IPKDMRRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNStealDNVLPSAQLM 290
Cdd:cd14179   216 SAEEIMKKIKQGDFSFEGEAWKNVSQEAKDLIQGLLTVDPNKRIKMSGLRYNEWLQD----GSQLSSNPLM 282
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
26-302 1.52e-45

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: 159.81  E-value: 1.52e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKILlDRPK--ARNEVRLHMMCATHPNIVQIIEVFANSVQfphessprarLLIVME 103
Cdd:cd14175     7 ETIGVGSYSVCKRCVHKATNMEYAVKVI-DKSKrdPSEEIEILLRYGQHPNIITLKDVYDDGKH----------VYLVTE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 104 MMEGGELFHRISQHRHFTEKQASQV-------------------------------TKQDAPVKLCDFGFAK---IDQGD 149
Cdd:cd14175    76 LMRGGELLDKILRQKFFSEREASSVlhticktveylhsqgvvhrdlkpsnilyvdeSGNPESLRICDFGFAKqlrAENGL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 150 LMTPQFTPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFysKHHSRTIPKDMRRKIM 229
Cdd:cd14175   156 LMTPCYTANFVAPEVLKRQ------------------GYDEGCDIWSLGILLYTMLAGYTPF--ANGPSDTPEEILTRIG 215
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1704602876 230 TGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEAldnvLPSAQL-MMDKAVVAGIQQA 302
Cdd:cd14175   216 SGKFTLSGGNWNTVSDAAKDLVSKMLHVDPHQRLTAKQVLQHPWITQKDK----LPQSQLnHQDVQLVKGAMAA 285
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
16-274 3.45e-45

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: 158.32  E-value: 3.45e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  16 ILEEYSInwTQKLGAGISGPVRVCVKKSTQERFALKILLDR-------------PKARNEVRLhMMCATHPNIVQIIEVF 82
Cdd:cd14084     4 LRKKYIM--SRTLGSGACGEVKLAYDKSTCKKVAIKIINKRkftigsrreinkpRNIETEIEI-LKKLSHPCIIKIEDFF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  83 ansvqfphesSPRARLLIVMEMMEGGELFHRISQHRHFTEKQAS------------------------------QVTKQD 132
Cdd:cd14084    81 ----------DAEDDYYIVLELMEGGELFDRVVSNKRLKEAICKlyfyqmllavkylhsngiihrdlkpenvllSSQEEE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 133 APVKLCDFGFAKIDQGD-LM-TPQFTPYYVAPQVLEAQRRHqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPP 210
Cdd:cd14084   151 CLIKITDFGLSKILGETsLMkTLCGTPTYLAPEVLRSFGTE---------------GYTRAVDCWSLGVILFICLSGYPP 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1704602876 211 FysKHHSRTIPkdMRRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14084   216 F--SEEYTQMS--LKEQILSGKYTFIPKAWKNVSEEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
26-302 8.03e-45

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: 157.87  E-value: 8.03e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKILlDRPK--ARNEVRLHMMCATHPNIVQIIEVFANSvQFphessprarLLIVME 103
Cdd:cd14178     9 EDIGIGSYSVCKRCVHKATSTEYAVKII-DKSKrdPSEEIEILLRYGQHPNIITLKDVYDDG-KF---------VYLVME 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 104 MMEGGELFHRISQHRHFTEKQASQV-------------------------------TKQDAPVKLCDFGFAK---IDQGD 149
Cdd:cd14178    78 LMRGGELLDRILRQKCFSEREASAVlctitktveylhsqgvvhrdlkpsnilymdeSGNPESIRICDFGFAKqlrAENGL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 150 LMTPQFTPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFysKHHSRTIPKDMRRKIM 229
Cdd:cd14178   158 LMTPCYTANFVAPEVLKRQ------------------GYDAACDIWSLGILLYTMLAGFTPF--ANGPDDTPEEILARIG 217
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1704602876 230 TGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEALDnvlPSAQLMMDKAVVAGIQQA 302
Cdd:cd14178   218 SGKYALSGGNWDSISDAAKDIVSKMLHVDPHQRLTAPQVLRHPWIVNREYLS---QNQLSRQDVHLVKGAMAA 287
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
26-281 2.15e-44

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: 156.20  E-value: 2.15e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLHMMCA-----THPNIVQIIEVFansvqfpheSSPrARLLI 100
Cdd:cd14169     9 EKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEAMVENEIAvlrriNHENIVSLEDIY---------ESP-THLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 101 VMEMMEGGELFHRISQHRHFTEKQASQVTKQ------------------------------DAPVKLCDFGFAKI-DQGD 149
Cdd:cd14169    79 AMELVTGGELFDRIIERGSYTEKDASQLIGQvlqavkylhqlgivhrdlkpenllyatpfeDSKIMISDFGLSKIeAQGM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 150 LMTPQFTPYYVAPQVLEaqrrhQKeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSrtipkDMRRKIM 229
Cdd:cd14169   159 LSTACGTPGYVAPELLE-----QK-------------PYGKAVDVWAIGVISYILLCGYPPFYDENDS-----ELFNQIL 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1704602876 230 TGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEALD 281
Cdd:cd14169   216 KAEYEFDSPYWDDISESAKDFIRHLLERDPEKRFTCEQALQHPWISGDTALD 267
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
28-274 2.37e-43

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: 153.64  E-value: 2.37e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILLDRP---KAR--NEVRLHMMCATHPNIVQIIEVFANSVQFphessprarlLIVM 102
Cdd:cd14173    10 LGEGAYARVQTCINLITNKEYAVKIIEKRPghsRSRvfREVEMLYQCQGHRNVLELIEFFEEEDKF----------YLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 103 EMMEGGELFHRISQHRHFTEKQASQVTK------------------------------QDAPVKLCDFGF---------- 142
Cdd:cd14173    80 EKMRGGSILSHIHRRRHFNELEASVVVQdiasaldflhnkgiahrdlkpenilcehpnQVSPVKICDFDLgsgiklnsdc 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 143 AKIDQGDLMTPQFTPYYVAPQVLEAQrrhqKEKSGIiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHS----- 217
Cdd:cd14173   160 SPISTPELLTPCGSAEYMAPEVVEAF----NEEASI---------YDKRCDLWSLGVILYIMLSGYPPFVGRCGSdcgwd 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1704602876 218 -----RTIPKDMRRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14173   227 rgeacPACQNMLFESIQEGKYEFPEKDWAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
28-280 5.82e-43

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: 153.49  E-value: 5.82e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILLDRPKA--RNEVRLHMMCATHPNIVQIIEVFANSVQfphessprarLLIVMEMM 105
Cdd:cd14180    14 LGEGSFSVCRKCRHRQSGQEYAVKIISRRMEAntQREVAALRLCQSHPNIVALHEVLHDQYH----------TYLVMELL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 106 EGGELFHRISQHRHFTEKQASQVTK------------------------------QDAPVKLCDFGFAKI-DQGD--LMT 152
Cdd:cd14180    84 RGGELLDRIKKKARFSESEASQLMRslvsavsfmheagvvhrdlkpenilyadesDGAVLKVIDFGFARLrPQGSrpLQT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 153 PQFTPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKH----HSRTipKDMRRKI 228
Cdd:cd14180   164 PCFTLQYAAPELFSNQ------------------GYDESCDLWSLGVILYTMLSGQVPFQSKRgkmfHNHA--ADIMHKI 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1704602876 229 MTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEAL 280
Cdd:cd14180   224 KEGDFSLEGEAWKGVSEEAKDLVRGLLTVDPAKRLKLSELRESDWLQGGSAL 275
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
18-273 8.85e-42

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: 148.64  E-value: 8.85e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  18 EEYSINwtQKLGAGISGPVRVCVKKSTQERFALKILlDRPKAR-------NEVRLhMMCATHPNIVQIIEvfansvqfph 90
Cdd:cd14184     1 EKYKIG--KVIGDGNFAVVKECVERSTGKEFALKII-DKAKCCgkehlieNEVSI-LRRVKHPNIIMLIE---------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  91 ESSPRARLLIVMEMMEGGELFHRISQHRHFTEKQASQ-----------------VTKQDAP--------------VKLCD 139
Cdd:cd14184    67 EMDTPAELYLVMELVKGGDLFDAITSSTKYTERDASAmvynlasalkylhglciVHRDIKPenllvceypdgtksLKLGD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 140 FGFAKIDQGDLMTPQFTPYYVAPQVLEaqrrhqkeKSGiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHsrt 219
Cdd:cd14184   147 FGLATVVEGPLYTVCGTPTYVAPEIIA--------ETG----------YGLKVDIWAAGVITYILLCGFPPFRSENN--- 205
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1704602876 220 IPKDMRRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPW 273
Cdd:cd14184   206 LQEDLFDQILLGKLEFPSPYWDNITDSAKELISHMLQVNVEARYTAEQILSHPW 259
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
28-274 1.56e-41

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: 148.25  E-value: 1.56e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILLDRP------KARNEVR-LHMMcaTHPNIVQIIEVFansvqfphESspRARLLI 100
Cdd:cd14167    11 LGTGAFSEVVLAEEKRTQKLVAIKCIAKKAlegketSIENEIAvLHKI--KHPNIVALDDIY--------ES--GGHLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 101 VMEMMEGGELFHRISQHRHFTEKQASQVTKQ------------------------------DAPVKLCDFGFAKI-DQGD 149
Cdd:cd14167    79 IMQLVSGGELFDRIVEKGFYTERDASKLIFQildavkylhdmgivhrdlkpenllyysldeDSKIMISDFGLSKIeGSGS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 150 LM-TPQFTPYYVAPQVLeAQRrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRtipkdMRRKI 228
Cdd:cd14167   159 VMsTACGTPGYVAPEVL-AQK-----------------PYSKAVDCWSIGVIAYILLCGYPPFYDENDAK-----LFEQI 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1704602876 229 MTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14167   216 LKAEYEFDSPYWDDISDSAKDFIQHLMEKDPEKRFTCEQALQHPWI 261
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
28-274 4.87e-41

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: 147.48  E-value: 4.87e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKIL-----LDRPKARNEVRLHMMCATHPNIVQIIEVFANSvqfphessprARLLIVM 102
Cdd:cd14174    10 LGEGAYAKVQGCVSLQNGKEYAVKIIeknagHSRSRVFREVETLYQCQGNKNILELIEFFEDD----------TRFYLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 103 EMMEGGELFHRISQHRHFTEKQASQVTKQDA------------------------------PVKLCDFGFAK-------- 144
Cdd:cd14174    80 EKLRGGSILAHIQKRKHFNEREASRVVRDIAsaldflhtkgiahrdlkpenilcespdkvsPVKICDFDLGSgvklnsac 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 145 --IDQGDLMTPQFTPYYVAPQVLEaqrrhqkeksgiIPTSPTPYtYNKSCDLWSLGVIIYVMLCGYPPFYSK-------- 214
Cdd:cd14174   160 tpITTPELTTPCGSAEYMAPEVVE------------VFTDEATF-YDKRCDLWSLGVILYIMLSGYPPFVGHcgtdcgwd 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1704602876 215 --HHSRTIPKDMRRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14174   227 rgEVCRVCQNKLFESIQEGKYEFPDKDWSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWV 288
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
26-289 8.97e-41

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: 148.24  E-value: 8.97e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKIL-LDRPKARNEVRLHMMCATHPNIVQIIEVFANSvqfphessprARLLIVMEM 104
Cdd:cd14176    25 EDIGVGSYSVCKRCIHKATNMEFAVKIIdKSKRDPTEEIEILLRYGQHPNIITLKDVYDDG----------KYVYVVTEL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 105 MEGGELFHRISQHRHFTEKQASQV-------------------------------TKQDAPVKLCDFGFAK---IDQGDL 150
Cdd:cd14176    95 MKGGELLDKILRQKFFSEREASAVlftitktveylhaqgvvhrdlkpsnilyvdeSGNPESIRICDFGFAKqlrAENGLL 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 151 MTPQFTPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFysKHHSRTIPKDMRRKIMT 230
Cdd:cd14176   175 MTPCYTANFVAPEVLERQ------------------GYDAACDIWSLGVLLYTMLTGYTPF--ANGPDDTPEEILARIGS 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1704602876 231 GSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEAldnvLPSAQL 289
Cdd:cd14176   235 GKFSLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQ----LPQYQL 289
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
26-274 3.70e-40

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: 145.26  E-value: 3.70e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKIL-------LDRPKARNEVRLhmmCAT--HPNIVQIIEVFANSVQFphesspra 96
Cdd:cd14086     7 EELGKGAFSVVRRCVQKSTGQEFAAKIIntkklsaRDHQKLEREARI---CRLlkHPNIVRLHDSISEEGFH-------- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  97 rlLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ------------------------------DAPVKLCDFGFAKID 146
Cdd:cd14086    76 --YLVFDLVTGGELFEDIVAREFYSEADASHCIQQilesvnhchqngivhrdlkpenlllaskskGAAVKLADFGLAIEV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 147 QGDlmTPQF-----TPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRtip 221
Cdd:cd14086   154 QGD--QQAWfgfagTPGYLSPEVLRKD------------------PYGKPVDIWACGVILYILLVGYPPFWDEDQHR--- 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1704602876 222 kdMRRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14086   211 --LYAQIKAGAYDYPSPEWDTVTPEAKDLINQMLTVNPAKRITAAEALKHPWI 261
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
28-273 3.84e-40

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: 143.81  E-value: 3.84e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKIL-LDRPKARNEV------RLHMMCATHPNIVQIieVFAnsvqFPHESSprarLLI 100
Cdd:cd05123     1 LGKGSFGKVLLVRKKDTGKLYAMKVLrKKEIIKRKEVehtlneRNILERVNHPFIVKL--HYA----FQTEEK----LYL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 101 VMEMMEGGELFHRISQHRHFTEKQ----ASQVT-----------------------KQDAPVKLCDFGFAK-IDQGDLMT 152
Cdd:cd05123    71 VLDYVPGGELFSHLSKEGRFPEERarfyAAEIVlaleylhslgiiyrdlkpenillDSDGHIKLTDFGLAKeLSSDGDRT 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 153 PQF--TPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHsrtipKDMRRKIMT 230
Cdd:cd05123   151 YTFcgTPEYLAPEVLLGK------------------GYGKAVDWWSLGVLLYEMLTGKPPFYAENR-----KEIYEKILK 207
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1704602876 231 GSFEFPEEewsqISEMAKDVVRKLLKVKPEERLT---IEGVLDHPW 273
Cdd:cd05123   208 SPLKFPEY----VSPEAKSLISGLLQKDPTKRLGsggAEEIKAHPF 249
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
26-288 4.25e-40

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: 145.35  E-value: 4.25e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKIL---LDRPKARNEVRLhMMCATHPNIVQIIEVFANSvqfphessprARLLIVM 102
Cdd:cd14085     9 SELGRGATSVVYRCRQKGTQKPYAVKKLkktVDKKIVRTEIGV-LLRLSHPNIIKLKEIFETP----------TEISLVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 103 EMMEGGELFHRISQHRHFTEKQASQVTKQ------------------------------DAPVKLCDFGFAKIDQGDLMT 152
Cdd:cd14085    78 ELVTGGELFDRIVEKGYYSERDAADAVKQileavaylhengivhrdlkpenllyatpapDAPLKIADFGLSKIVDQQVTM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 153 PQF--TPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTipkdMRRKIMT 230
Cdd:cd14085   158 KTVcgTPGYCAPEILRGC------------------AYGPEVDMWSVGVITYILLCGFEPFYDERGDQY----MFKRILN 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1704602876 231 GSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEALDNVLPSAQ 288
Cdd:cd14085   216 CDYDFVSPWWDDVSLNAKDLVKKLIVLDPKKRLTTQQALQHPWVTGKAANFAHMDTAQ 273
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
26-288 1.58e-39

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: 143.62  E-value: 1.58e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKILlDRPK--ARNEVRLHMMCATHPNIVQIIEVFANSvqfphessprARLLIVME 103
Cdd:cd14177    10 EDIGVGSYSVCKRCIHRATNMEFAVKII-DKSKrdPSEEIEILMRYGQHPNIITLKDVYDDG----------RYVYLVTE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 104 MMEGGELFHRISQHRHFTEKQASQV-------------------------------TKQDAPVKLCDFGFAKIDQGD--- 149
Cdd:cd14177    79 LMKGGELLDRILRQKFFSEREASAVlytitktvdylhcqgvvhrdlkpsnilymddSANADSIRICDFGFAKQLRGEngl 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 150 LMTPQFTPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFysKHHSRTIPKDMRRKIM 229
Cdd:cd14177   159 LLTPCYTANFVAPEVLMRQ------------------GYDAACDIWSLGVLLYTMLAGYTPF--ANGPNDTPEEILLRIG 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1704602876 230 TGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEALDNVLPSAQ 288
Cdd:cd14177   219 SGKFSLSGGNWDTVSDAAKDLLSHMLHVDPHQRYTAEQVLKHSWIACRDQLPHYQLNRQ 277
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
16-274 5.53e-39

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: 141.33  E-value: 5.53e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  16 ILEEYSINWTQkLGAGISGPVRVCVKKSTQERFALKILLDRPKA---RNEVrLH-----MMCATHPNIVQIIEVFANsvq 87
Cdd:cd14106     5 INEVYTVESTP-LGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGqdcRNEI-LHeiavlELCKDCPRVVNLHEVYET--- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  88 fphesspRARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ------------------------------DAPVKL 137
Cdd:cd14106    80 -------RSELILILELAAGGELQTLLDEEECLTEADVRRLMRQilegvqylhernivhldlkpqnilltsefpLGDIKL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 138 CDFGFAK-IDQG-DLMTPQFTPYYVAPQVLeaqrrhqkeksgiiptSPTPYTYnkSCDLWSLGVIIYVMLCGYPPFYSKH 215
Cdd:cd14106   153 CDFGISRvIGEGeEIREILGTPDYVAPEIL----------------SYEPISL--ATDMWSIGVLTYVLLTGHSPFGGDD 214
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1704602876 216 HSRTIpkdmrRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14106   215 KQETF-----LNISQCNLDFPEELFKDVSPLAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
26-274 8.39e-39

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: 140.69  E-value: 8.39e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKILldrPKA-----------RNEVRLHMMCAtHPNIVQIIEVFansvqfpHESSp 94
Cdd:cd14007     6 KPLGKGKFGNVYLAREKKSGFIVALKVI---SKSqlqksglehqlRREIEIQSHLR-HPNILRLYGYF-------EDKK- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  95 raRLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ--DA---------------P----------VKLCDFGF-AKID 146
Cdd:cd14007    74 --RIYLILEYAPNGELYKELKKQKRFDEKEAAKYIYQlaLAldylhskniihrdikPenillgsngeLKLADFGWsVHAP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 147 QGDLMTPQFTPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIpkdmrR 226
Cdd:cd14007   152 SNRRKTFCGTLDYLPPEMVEGKE------------------YDYKVDIWSLGVLCYELLVGKPPFESKSHQETY-----K 208
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1704602876 227 KIMTGSFEFPeeewSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14007   209 RIQNVDIKFP----SSVSPEAKDLISKLLQKDPSKRLSLEQVLNHPWI 252
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
18-274 1.53e-38

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: 141.03  E-value: 1.53e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  18 EEYSInwTQKLGAG-ISGPVRVCVKKSTQERFALKIL------------LDRPKARNEVRLHMMcATHPNIVQIIEVFAN 84
Cdd:cd14096     1 ENYRL--INKIGEGaFSNVYKAVPLRNTGKPVAIKVVrkadlssdnlkgSSRANILKEVQIMKR-LSHPNIVKLLDFQES 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  85 SVQFphessprarlLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQDA-----------------P------------- 134
Cdd:cd14096    78 DEYY----------YIVLELADGGEIFHQIVRLTYFSEDLSRHVITQVAsavkylheigvvhrdikPenllfepipfips 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 135 ------------------------------VKLCDFGFAKI-DQGDLMTPQFTPYYVAPQVLEAQRrhqkeksgiiptsp 183
Cdd:cd14096   148 ivklrkadddetkvdegefipgvggggigiVKLADFGLSKQvWDSNTKTPCGTVGYTAPEVVKDER-------------- 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 184 tpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHsrtipKDMRRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERL 263
Cdd:cd14096   214 ----YSKKVDMWALGCVLYTLLCGFPPFYDESI-----ETLTEKISRGDYTFLSPWWDEISKSAKDLISHLLTVDPAKRY 284
                         330
                  ....*....|.
gi 1704602876 264 TIEGVLDHPWL 274
Cdd:cd14096   285 DIDEFLAHPWI 295
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
28-274 5.99e-36

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: 132.73  E-value: 5.99e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKIL-----LDRPKARNEVRLhMMCATHPNIVQIIEVFANsvqfPHEssprarLLIVM 102
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAKFIkcrkaKDREDVRNEIEI-MNQLRHPRLLQLYDAFET----PRE------MVLVM 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 103 EMMEGGELFHR-ISQHRHFTEK-------QASQ----------------------VTKQDAPVKLCDFGFA-KIDQGDLM 151
Cdd:cd14103    70 EYVAGGELFERvVDDDFELTERdcilfmrQICEgvqymhkqgilhldlkpenilcVSRTGNQIKIIDFGLArKYDPDKKL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 152 TPQF-TPYYVAPQVLeaqrrhqkeksgiiptSPTPYTYnkSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIpkdmrRKIMT 230
Cdd:cd14103   150 KVLFgTPEFVAPEVV----------------NYEPISY--ATDMWSVGVICYVLLSGLSPFMGDNDAETL-----ANVTR 206
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1704602876 231 GSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14103   207 AKWDFDDEAFDDISDEAKDFISKLLVKDPRKRMSAAQCLQHPWL 250
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
28-273 1.56e-35

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: 131.99  E-value: 1.56e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILlDRPKAR-------NEVRLhMMCATHPNIVQIIEVFANSvqfphessprARLLI 100
Cdd:cd14185     8 IGDGNFAVVKECRHWNENQEYAMKII-DKSKLKgkedmieSEILI-IKSLSHPNIVKLFEVYETE----------KEIYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 101 VMEMMEGGELFHRISQHRHFTEKQAS----------------QVTKQD---------------APVKLCDFGFAKIDQGD 149
Cdd:cd14185    76 ILEYVRGGDLFDAIIESVKFTEHDAAlmiidlcealvyihskHIVHRDlkpenllvqhnpdksTTLKLADFGLAKYVTGP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 150 LMTPQFTPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRtipKDMRRKIM 229
Cdd:cd14185   156 IFTVCGTPTYVAPEILSEK------------------GYGLEVDMWAAGVILYILLCGFPPFRSPERDQ---EELFQIIQ 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1704602876 230 TGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPW 273
Cdd:cd14185   215 LGHYEFLPPYWDNISEAAKDLISRLLVVDPEKRYTAKQVLQHPW 258
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
28-273 6.21e-35

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: 130.08  E-value: 6.21e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLH--MMC-ATHPNIVQIIEVFansvqfpheSSPRArLLIVMEM 104
Cdd:cd14006     1 LGRGRFGVVKRCIEKATGREFAAKFIPKRDKKKEAVLREisILNqLQHPRIIQLHEAY---------ESPTE-LVLILEL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 105 MEGGELFHRISQHRHFTEKQASQVTKQ--------------------------DAP---VKLCDFGFA-KIDQGDLMTPQ 154
Cdd:cd14006    71 CSGGELLDRLAERGSLSEEEVRTYMRQlleglqylhnhhilhldlkpenillaDRPspqIKIIDFGLArKLNPGEELKEI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 155 F-TPYYVAPQVLEAQrrhqkeksgiiPTSPTpytynksCDLWSLGVIIYVMLCGYPPFYSKHHSRTIpkdmrRKIMTGSF 233
Cdd:cd14006   151 FgTPEFVAPEIVNGE-----------PVSLA-------TDMWSIGVLTYVLLSGLSPFLGEDDQETL-----ANISACRV 207
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1704602876 234 EFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPW 273
Cdd:cd14006   208 DFSEEYFSSVSQEAKDFIRKLLVKEPRKRPTAQEALQHPW 247
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
33-274 7.19e-35

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: 130.53  E-value: 7.19e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  33 SGPVRVCvkKSTQERFALKIlldRPKARNEVRLHMMcATHPNIVQIIEVFANsvqfphesspRARLLIVMEMMEGGELFH 112
Cdd:cd14088    25 TGKLYTC--KKFLKRDGRKV---RKAAKNEINILKM-VKHPNILQLVDVFET----------RKEYFIFLELATGREVFD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 113 RISQHRHFTEKQASQVTKQ------------------------------DAPVKLCDFGFAKIDQGDLMTPQFTPYYVAP 162
Cdd:cd14088    89 WILDQGYYSERDTSNVIRQvleavaylhslkivhrnlklenlvyynrlkNSKIVISDFHLAKLENGLIKEPCGTPEYLAP 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 163 QVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHS---RTIPKDMRRKIMTGSFEFPEEE 239
Cdd:cd14088   169 EVVGRQR------------------YGRPVDCWAIGVIMYILLSGNPPFYDEAEEddyENHDKNLFRKILAGDYEFDSPY 230
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1704602876 240 WSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14088   231 WDDISQAAKDLVTRLMEVEQDQRITAEEAISHEWI 265
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
27-274 3.70e-34

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: 128.14  E-value: 3.70e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  27 KLGAGISGPVRVCVKKSTQERFALKI----LLDRPKARNEVR---LHMMCATHPNIVQIIEVFANSVQfphessprarLL 99
Cdd:cd14081     8 TLGKGQTGLVKLAKHCVTGQKVAIKIvnkeKLSKESVLMKVEreiAIMKLIEHPNVLKLYDVYENKKY----------LY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMEGGELFHRISQHRHFTEKQASQVTKQ---------------------------DAPVKLCDFGFAKIDQGDLM- 151
Cdd:cd14081    78 LVLEYVSGGELFDYLVKKGRLTEKEARKFFRQiisaldychshsichrdlkpenllldeKNNIKIADFGMASLQPEGSLl 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 152 -TPQFTPYYVAPQVLeaqrRHQKeksgiiptsptpYTYNKScDLWSLGVIIYVMLCGYPPFYSKHHSRTIpkdmrRKIMT 230
Cdd:cd14081   158 eTSCGSPHYACPEVI----KGEK------------YDGRKA-DIWSCGVILYALLVGALPFDDDNLRQLL-----EKVKR 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1704602876 231 GSFEFPEEewsqISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14081   216 GVFHIPHF----ISPDAQDLLRRMLEVNPEKRITIEEIKKHPWF 255
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
34-278 1.25e-33

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: 128.04  E-value: 1.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  34 GP---VRVCVKKSTQERFALKIL----------LDRPKARNEVRL-HMMcaTHPNIVQIIEVFaNSVQFPHessprarll 99
Cdd:cd14094    14 GPfsvVRRCIHRETGQQFAVKIVdvakftsspgLSTEDLKREASIcHML--KHPHIVELLETY-SSDGMLY--------- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMEGG----ELFHRISQHRHFTEKQASQVTKQ------------------------------DAPVKLCDFGFAK- 144
Cdd:cd14094    82 MVFEFMDGAdlcfEIVKRADAGFVYSEAVASHYMRQilealrychdnniihrdvkphcvllaskenSAPVKLGGFGVAIq 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 145 IDQGDLMTPQF--TPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHhsrtipK 222
Cdd:cd14094   162 LGESGLVAGGRvgTPHFMAPEVVKREP------------------YGKPVDVWGCGVILFILLSGCLPFYGTK------E 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1704602876 223 DMRRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTE 278
Cdd:cd14094   218 RLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWIKERD 273
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
36-274 1.56e-33

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: 126.49  E-value: 1.56e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  36 VRVcVKKSTQERFALKILLDRPKAR----NEVRLhMMCATHPNIVQIIEVFANSvqfphessprARLLIVMEMMEGGELF 111
Cdd:cd14087    18 VRV-EHRVTRQPYAIKMIETKCRGRevceSELNV-LRRVRHTNIIQLIEVFETK----------ERVYMVMELATGGELF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 112 HRISQHRHFTEKQASQVTKQ------------------------------DAPVKLCDFGFA----KIDQGDLMTPQFTP 157
Cdd:cd14087    86 DRIIAKGSFTERDATRVLQMvldgvkylhglgithrdlkpenllyyhpgpDSKIMITDFGLAstrkKGPNCLMKTTCGTP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 158 YYVAPQVLEAQrrhqkeksgiiptsptPYTynKSCDLWSLGVIIYVMLCGYPPFYSKHHSRtipkdMRRKIMTGSFEFPE 237
Cdd:cd14087   166 EYIAPEILLRK----------------PYT--QSVDMWAVGVIAYILLSGTMPFDDDNRTR-----LYRQILRAKYSYSG 222
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1704602876 238 EEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14087   223 EPWPSVSNLAKDFIDRLLTVNPGERLSATQALKHPWI 259
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
14-276 1.58e-33

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: 127.03  E-value: 1.58e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  14 TSILEEYSINWTqkLGAGISGPVRVCVKKSTQERFALKILlDRPKAR-------NEVRLhMMCATHPNIVQIIEvfansv 86
Cdd:cd14183     2 ASISERYKVGRT--IGDGNFAVVKECVERSTGREYALKII-NKSKCRgkehmiqNEVSI-LRRVKHPNIVLLIE------ 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  87 qfphESSPRARLLIVMEMMEGGELFHRISQHRHFTEKQASQV-----------------------------TKQDAP--V 135
Cdd:cd14183    72 ----EMDMPTELYLVMELVKGGDLFDAITSTNKYTERDASGMlynlasaikylhslnivhrdikpenllvyEHQDGSksL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 136 KLCDFGFAKIDQGDLMTPQFTPYYVAPQVLEaqrrhqkeKSGiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKH 215
Cdd:cd14183   148 KLGDFGLATVVDGPLYTVCGTPTYVAPEIIA--------ETG----------YGLKVDIWAAGVITYILLCGFPPFRGSG 209
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1704602876 216 HSRTIPKDmrrKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNS 276
Cdd:cd14183   210 DDQEVLFD---QILMGQVDFPSPYWDNVSDSAKELITMMLQVDVDQRYSALQVLEHPWVND 267
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
28-274 1.64e-33

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: 127.01  E-value: 1.64e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILLDRPK-------------ARNEVRLHMMCATHPNIVQIIEVFansvqfphESSp 94
Cdd:cd14181    18 IGRGVSSVVRRCVHRHTGQEFAVKIIEVTAErlspeqleevrssTLKEIHILRQVSGHPSIITLIDSY--------ESS- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  95 rARLLIVMEMMEGGELFHRISQHRHFTEKQ----------------ASQVTKQDAP-----------VKLCDFGFAKIDQ 147
Cdd:cd14181    89 -TFIFLVFDLMRRGELFDYLTEKVTLSEKEtrsimrslleavsylhANNIVHRDLKpenillddqlhIKLSDFGFSCHLE 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 148 GDLMTPQF--TPYYVAPQVLeaqrrhqkeKSGIIPTSPTpytYNKSCDLWSLGVIIYVMLCGYPPFYskhHSRTIPkdMR 225
Cdd:cd14181   168 PGEKLRELcgTPGYLAPEIL---------KCSMDETHPG---YGKEVDLWACGVILFTLLAGSPPFW---HRRQML--ML 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1704602876 226 RKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14181   231 RMIMEGRYQFSSPEWDDRSSTVKDLISRLLVVDPEIRLTAEQALQHPFF 279
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
26-274 1.94e-33

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: 126.53  E-value: 1.94e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVC--VKKSTQERFALKILlDRPKARNE-------------VRLHmmcatHPNIVQIIEVFansvqfph 90
Cdd:cd14080     6 KTIGEGSYSKVKLAeyTKSGLKEKVACKII-DKKKAPKDflekflpreleilRKLR-----HPNIIQVYSIF-------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  91 ESSPRarLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ-------------------------DAP--VKLCDFGFA 143
Cdd:cd14080    72 ERGSK--VFIFMEYAEHGDLLEYIQKRGALSESQARIWFRQlalavqylhsldiahrdlkcenillDSNnnVKLSDFGFA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 144 KI---DQGDLMTPQF--TPYYVAPQVLEAqrrhqkeksgiIPTSPTPYtynkscDLWSLGVIIYVMLCGYPPFYSKHHSR 218
Cdd:cd14080   150 RLcpdDDGDVLSKTFcgSAAYAAPEILQG-----------IPYDPKKY------DIWSLGVILYIMLCGSMPFDDSNIKK 212
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1704602876 219 TIPKDMRRKImtgsfEFPEEEWsQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14080   213 MLKDQQNRKV-----RFPSSVK-KLSPECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
28-273 3.05e-33

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: 126.05  E-value: 3.05e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLHMM--------CATHPNIVQIIEVFANSvqfphessprARLL 99
Cdd:cd14098     8 LGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNDKNLQLFqreinilkSLEHPGIVRLIDWYEDD----------QHIY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMEGGELFHRISQHRHFTEKQASQVTKQ---------------------------DAP--VKLCDFGFAKIDQGDL 150
Cdd:cd14098    78 LVMEYVEGGDLMDFIMAWGAIPEQHARELTKQileamaythsmgithrdlkpenilitqDDPviVKISDFGLAKVIHTGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 151 MTPQF--TPYYVAPQVLEAqrRHQKEKSGiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIpkdmrRKI 228
Cdd:cd14098   158 FLVTFcgTMAYLAPEILMS--KEQNLQGG----------YSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVE-----KRI 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1704602876 229 MTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPW 273
Cdd:cd14098   221 RKGRYTQPPLVDFNISEEAIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
21-273 8.09e-33

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: 125.38  E-value: 8.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  21 SINWTQKLGAGISGPVRVCVKKSTQERFALKILLDRPKAR--------NEVRLhMMCATHPNIVQIIEVFANSvqfphes 92
Cdd:cd05580     2 DFEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIIKlkqvehvlNEKRI-LSEVRHPFIVNLLGSFQDD------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  93 sprARLLIVMEMMEGGELFHRISQHRHFTEKQ----ASQVT-----------------------KQDAPVKLCDFGFAKI 145
Cdd:cd05580    74 ---RNLYMVMEYVPGGELFSLLRRSGRFPNDVakfyAAEVVlaleylhsldivyrdlkpenlllDSDGHIKITDFGFAKR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 146 DQGDLMTPQFTPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHhsrtiPKDMR 225
Cdd:cd05580   151 VKDRTYTLCGTPEYLAPEIILSK------------------GHGKAVDWWALGILIYEMLAGYPPFFDEN-----PMKIY 207
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1704602876 226 RKIMTGSFEFPEEewsqISEMAKDVVRKLLKVKPEERL-----TIEGVLDHPW 273
Cdd:cd05580   208 EKILEGKIRFPSF----FDPDAKDLIKRLLVVDLTKRLgnlknGVEDIKNHPW 256
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
25-274 8.95e-33

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: 124.91  E-value: 8.95e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  25 TQKLGAGISGPVRVCVKKSTQERFALKIL-----------LDRPKARNEVRLhMMCATHPNIVQIIEVFANsvqfphess 93
Cdd:cd14105    10 GEELGSGQFAVVKKCREKSTGLEYAAKFIkkrrskasrrgVSREDIEREVSI-LRQVLHPNIITLHDVFEN--------- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  94 pRARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ----------------------------DAP---VKLCDFGF 142
Cdd:cd14105    80 -KTDVVLILELVAGGELFDFLAEKESLSEEEATEFLKQildgvnylhtkniahfdlkpenimlldkNVPiprIKLIDFGL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 143 A-KIDQGDLMTPQF-TPYYVAPQVLEAQrrhqkeksgiiPTSPtpytynkSCDLWSLGVIIYVMLCGYPPFYSKHHSRTI 220
Cdd:cd14105   159 AhKIEDGNEFKNIFgTPEFVAPEIVNYE-----------PLGL-------EADMWSIGVITYILLSGASPFLGDTKQETL 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1704602876 221 pkdmrRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14105   221 -----ANITAVNYDFDDEYFSNTSELAKDFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
26-272 1.36e-32

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 124.11  E-value: 1.36e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALK-ILL------DRPKARNEVRLhMMCATHPNIVQIIEVFANsvqfphesspRARL 98
Cdd:cd08215     6 RVIGKGSFGSAYLVRRKSDGKLYVLKeIDLsnmsekEREEALNEVKL-LSKLKHPNIVKYYESFEE----------NGKL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  99 LIVMEMMEGGELFHRISQHR----HFTEKQA-------------------------SQ---VTKQDApVKLCDFGFAKID 146
Cdd:cd08215    75 CIVMEYADGGDLAQKIKKQKkkgqPFPEEQIldwfvqiclalkylhsrkilhrdlkTQnifLTKDGV-VKLGDFGISKVL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 147 QGDLmtpQF------TPYYVAPQVLEAQrrhqkeksgiiptsptPYTYnKScDLWSLGVIIYVMLCGYPPFYSKHhsrti 220
Cdd:cd08215   154 ESTT---DLaktvvgTPYYLSPELCENK----------------PYNY-KS-DIWALGCVLYELCTLKHPFEANN----- 207
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1704602876 221 PKDMRRKIMTGSFEFPEEEWSQisEMaKDVVRKLLKVKPEERLTIEGVLDHP 272
Cdd:cd08215   208 LPALVYKIVKGQYPPIPSQYSS--EL-RDLVNSMLQKDPEKRPSANEILSSP 256
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
28-274 1.52e-32

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: 124.26  E-value: 1.52e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKIL------LDRPKARNEVR---------LHMMCAtHPNIVQIIEVFANSVQFphes 92
Cdd:cd14182    11 LGRGVSSVVRRCIHKPTRQEYAVKIIditgggSFSPEEVQELReatlkeidiLRKVSG-HPNIIQLKDTYETNTFF---- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  93 sprarlLIVMEMMEGGELFHRISQHRHFTEKQASQVTK---------------------------QDAPVKLCDFGFA-K 144
Cdd:cd14182    86 ------FLVFDLMKKGELFDYLTEKVTLSEKETRKIMRallevicalhklnivhrdlkpenilldDDMNIKLTDFGFScQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 145 IDQGD-LMTPQFTPYYVAPQVLEAQRRHQKEKsgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYskHHSRTIpkd 223
Cdd:cd14182   160 LDPGEkLREVCGTPGYLAPEIIECSMDDNHPG------------YGKEVDMWSTGVIMYTLLAGSPPFW--HRKQML--- 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1704602876 224 MRRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14182   223 MLRMIMSGNYQFGSPEWDDRSDTVKDLISRFLVVQPQKRYTAEEALAHPFF 273
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
28-274 2.86e-31

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


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 120.74  E-value: 2.86e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILlDRPKARNEVRLHMMCAT-------------------HPNIVQIIEVFANsvqf 88
Cdd:cd14008     1 LGRGSFGKVKLALDTETGQLYAIKIF-NKSRLRKRREGKNDRGKiknalddvrreiaimkkldHPNIVRLYEVIDD---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  89 PHESSprarLLIVMEMMEGGELFHRISQHRH--FTEKQASQVTKQ---------------------------DAPVKLCD 139
Cdd:cd14008    76 PESDK----LYLVLEYCEGGPVMELDSGDRVppLPEETARKYFRDlvlgleylhengivhrdikpenllltaDGTVKISD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 140 FGFAKIDQGDLMTPQF---TPYYVAPqvlEAQRRHQKEKSGiiptsptpytynKSCDLWSLGVIIYVMLCGYPPFYSKhh 216
Cdd:cd14008   152 FGVSEMFEDGNDTLQKtagTPAFLAP---ELCDGDSKTYSG------------KAADIWALGVTLYCLVFGRLPFNGD-- 214
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1704602876 217 srTIPkDMRRKIMTGSFEFPEEEwsQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14008   215 --NIL-ELYEAIQNQNDEFPIPP--ELSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
28-278 3.09e-31

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: 121.36  E-value: 3.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILlDRPKArneVRLHMMCATH--PNIVQIIEvFANSVQFPHESSPRARLLIVMEMM 105
Cdd:cd14209     9 LGTGSFGRVMLVRHKETGNYYAMKIL-DKQKV---VKLKQVEHTLneKRILQAIN-FPFLVKLEYSFKDNSNLYMVMEYV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 106 EGGELFHRISQHRHFTEKQ----ASQVT-----------------------KQDAPVKLCDFGFAKIDQGDLMTPQFTPY 158
Cdd:cd14209    84 PGGEMFSHLRRIGRFSEPHarfyAAQIVlafeylhsldliyrdlkpenlliDQQGYIKVTDFGFAKRVKGRTWTLCGTPE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 159 YVAPQvleaqrrhqkeksgIIPTSPtpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHhsrtiPKDMRRKIMTGSFEFPee 238
Cdd:cd14209   164 YLAPE--------------IILSKG----YNKAVDWWALGVLIYEMAAGYPPFFADQ-----PIQIYEKIVSGKVRFP-- 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1704602876 239 ewSQISEMAKDVVRKLLKVKPEERL--TIEGVLD---HPWLNSTE 278
Cdd:cd14209   219 --SHFSSDLKDLLRNLLQVDLTKRFgnLKNGVNDiknHKWFATTD 261
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
24-293 3.39e-31

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: 121.31  E-value: 3.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  24 WTQKLGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLHMMCAT-----HPNIVQIIEVFANSvqfphessprARL 98
Cdd:cd14168    14 FKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKESSIENEIAVlrkikHENIVALEDIYESP----------NHL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  99 LIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ------------------------------DAPVKLCDFGFAKID-Q 147
Cdd:cd14168    84 YLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQvldavyylhrmgivhrdlkpenllyfsqdeESKIMISDFGLSKMEgK 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 148 GDLM-TPQFTPYYVAPQVLeAQRrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRtipkdMRR 226
Cdd:cd14168   164 GDVMsTACGTPGYVAPEVL-AQK-----------------PYSKAVDCWSIGVIAYILLCGYPPFYDENDSK-----LFE 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1704602876 227 KIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEALD-NVLPSAQLMMDK 293
Cdd:cd14168   221 QILKADYEFDSPYWDDISDSAKDFIRNLMEKDPNKRYTCEQALRHPWIAGDTALCkNIHESVSAQIRK 288
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
26-274 5.74e-31

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: 120.12  E-value: 5.74e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKIL-----------LDRPKARNEVRLhMMCATHPNIVQIIEVFANsvqfphessp 94
Cdd:cd14194    11 EELGSGQFAVVKKCREKSTGLQYAAKFIkkrrtkssrrgVSREDIEREVSI-LKEIQHPNVITLHEVYEN---------- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  95 RARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ----------------------------DAP---VKLCDFGFA 143
Cdd:cd14194    80 KTDVILILELVAGGELFDFLAEKESLTEEEATEFLKQilngvyylhslqiahfdlkpenimlldrNVPkprIKIIDFGLA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 144 -KIDQGDLMTPQF-TPYYVAPQVLeaqrrhQKEKSGIiptsptpytynkSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIP 221
Cdd:cd14194   160 hKIDFGNEFKNIFgTPEFVAPEIV------NYEPLGL------------EADMWSIGVITYILLSGASPFLGDTKQETLA 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1704602876 222 KdmrrkIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14194   222 N-----VSAVNYEFEDEYFSNTSALAKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
42-274 5.86e-31

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 119.58  E-value: 5.86e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  42 KSTQERFALKI----LLDRPKAR----NEVRLHMMcATHPNIVQIIEVFANSvqfphessprARLLIVMEMMEGGELFHR 113
Cdd:cd14099    23 MSTGKVYAGKVvpksSLTKPKQReklkSEIKIHRS-LKHPNIVKFHDCFEDE----------ENVYILLELCSNGSLMEL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 114 ISQHRHFTEKQASQVTKQ---------------------------DAPVKLCDFGFA-KIDQGDL--MTPQFTPYYVAPQ 163
Cdd:cd14099    92 LKRRKALTEPEVRYFMRQilsgvkylhsnriihrdlklgnlfldeNMNVKIGDFGLAaRLEYDGErkKTLCGTPNYIAPE 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 164 VLEAQRRHQKEksgiiptsptpytynksCDLWSLGVIIYVMLCGYPPFYSKhhsrTIpKDMRRKIMTGSFEFPEEewSQI 243
Cdd:cd14099   172 VLEKKKGHSFE-----------------VDIWSLGVILYTLLVGKPPFETS----DV-KETYKRIKKNEYSFPSH--LSI 227
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1704602876 244 SEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14099   228 SDEAKDLIRSMLQPDPTKRPSLDEILSHPFF 258
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
28-273 2.25e-30

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: 117.89  E-value: 2.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILlDRPKA---------RNEVRLhMMCATHPNIVQIIEVFANsvqfphesspRARL 98
Cdd:cd14663     8 LGEGTFAKVKFARNTKTGESVAIKII-DKEQVaregmveqiKREIAI-MKLLRHPNIVELHEVMAT----------KTKI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  99 LIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ---------------------------DAPVKLCDFGFAKI-----D 146
Cdd:cd14663    76 FFVMELVTGGELFSKIAKNGRLKEDKARKYFQQlidavdychsrgvfhrdlkpenllldeDGNLKISDFGLSALseqfrQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 147 QGDLMTPQFTPYYVAPQVLeAQRRHQKEKSgiiptsptpytynkscDLWSLGVIIYVMLCGYPPFyskhHSRTIPKdMRR 226
Cdd:cd14663   156 DGLLHTTCGTPNYVAPEVL-ARRGYDGAKA----------------DIWSCGVILFVLLAGYLPF----DDENLMA-LYR 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1704602876 227 KIMTGSFEFPeeewSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPW 273
Cdd:cd14663   214 KIMKGEFEYP----RWFSPGAKSLIKRILDPNPSTRITVEQIMASPW 256
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
28-274 1.25e-29

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: 115.83  E-value: 1.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILlDRPKARN---------EVRLhMMCATHPNIVQIIEVfansVQFPHEssprarL 98
Cdd:cd14079    10 LGVGSFGKVKLAEHELTGHKVAVKIL-NRQKIKSldmeekirrEIQI-LKLFRHPHIIRLYEV----IETPTD------I 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  99 LIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ---------------------------DAPVKLCDFGFAKIDQ-GD- 149
Cdd:cd14079    78 FMVMEYVSGGELFDYIVQKGRLSEDEARRFFQQiisgveychrhmvvhrdlkpenllldsNMNVKIADFGLSNIMRdGEf 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 150 LMTPQFTPYYVAPQVLeaqrrhqkekSGIIPTSPtpytynkSCDLWSLGVIIYVMLCGYPPFYSKHhsrtIPkDMRRKIM 229
Cdd:cd14079   158 LKTSCGSPNYAAPEVI----------SGKLYAGP-------EVDVWSCGVILYALLCGSLPFDDEH----IP-NLFKKIK 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1704602876 230 TGSFEFPeeewSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14079   216 SGIYTIP----SHLSPGARDLIKRMLVVDPLKRITIPEIRQHPWF 256
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
25-274 5.33e-29

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: 114.02  E-value: 5.33e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  25 TQKLGAGISGPVRVCVKKSTQERFALKIL--------LDRPKARNEVRLhMMCATHPNIVQIIEVFANsvqfphesspRA 96
Cdd:cd14073     6 LETLGKGTYGKVKLAIERATGREVAIKSIkkdkiedeQDMVRIRREIEI-MSSLNHPHIIRIYEVFEN----------KD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  97 RLLIVMEMMEGGELFHRISQHRHFTEKQAS----QVTK-----------------------QDAPVKLCDFGFA-KIDQG 148
Cdd:cd14073    75 KIVIVMEYASGGELYDYISERRRLPEREARrifrQIVSavhychkngvvhrdlklenilldQNGNAKIADFGLSnLYSKD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 149 DLMTpQF--TPYYVAPQVLEAqrrhqkeksgiiptspTPYtYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRtipkdMRR 226
Cdd:cd14073   155 KLLQ-TFcgSPLYASPEIVNG----------------TPY-QGPEVDCWSLGVLLYTLVYGTMPFDGSDFKR-----LVK 211
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1704602876 227 KIMTGSFEFPeeewSQISEmAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14073   212 QISSGDYREP----TQPSD-ASGLIRWMLTVNPKRRATIEDIANHWWV 254
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
27-274 8.38e-29

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: 113.45  E-value: 8.38e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  27 KLGAGISGPVRVCVKKSTQERFALKILLDRPKAR-----NEVRLHMMCaTHPNIVQIIevfaNSVQFPHEssprarLLIV 101
Cdd:cd05122     7 KIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKkesilNEIAILKKC-KHPNIVKYY----GSYLKKDE------LWIV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 102 MEMMEGGELFHRISQHRH-FTEKQASQVTKQ---------------------------DAPVKLCDFGFAKI--DQGDLM 151
Cdd:cd05122    76 MEFCSGGSLKDLLKNTNKtLTEQQIAYVCKEvlkgleylhshgiihrdikaanilltsDGEVKLIDFGLSAQlsDGKTRN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 152 TPQFTPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPfYSKHHSrtipkdMRRKIMTG 231
Cdd:cd05122   156 TFVGTPYWMAPEVIQGKP------------------YGFKADIWSLGITAIEMAEGKPP-YSELPP------MKALFLIA 210
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1704602876 232 SFEFPEEEW-SQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd05122   211 TNGPPGLRNpKKWSKEFKDFLKKCLQKDPEKRPTAEQLLKHPFI 254
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
27-274 8.54e-29

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: 113.80  E-value: 8.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  27 KLGAGISGPVRVCVKKSTQERFALKILlDRPKA--------RNEVRLhMMCATHPNIVQIIEVFANSvqfphessprARL 98
Cdd:cd14097     8 KLGQGSFGVVIEATHKETQTKWAIKKI-NREKAgssavkllEREVDI-LKHVNHAHIIHLEEVFETP----------KRM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  99 LIVMEMMEGGELFHRISQHRHFTEKQASQVTKQDAP----------------------------------VKLCDFGFAK 144
Cdd:cd14097    76 YLVMELCEDGELKELLLRKGFFSENETRHIIQSLASavaylhkndivhrdlklenilvkssiidnndklnIKVTDFGLSV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 145 IDQG---DLMTPQF-TPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRti 220
Cdd:cd14097   156 QKYGlgeDMLQETCgTPIYMAPEVISAH------------------GYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEK-- 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1704602876 221 pkdMRRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14097   216 ---LFEEIRKGDLTFTQSVWQSVSDAAKNVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
26-274 1.56e-28

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: 113.13  E-value: 1.56e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKILLDRPK-------ARNEVRLH---MMCATHPNIVQIIEVFANsvqfphesspR 95
Cdd:cd14196    11 EELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrasrrgvSREEIEREvsiLRQVLHPNIITLHDVYEN----------R 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  96 ARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ----------------------------DAP---VKLCDFGFA- 143
Cdd:cd14196    81 TDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQildgvnylhtkkiahfdlkpenimlldkNIPiphIKLIDFGLAh 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 144 KIDQGDLMTPQF-TPYYVAPQVLeaqrrhQKEKSGIiptsptpytynkSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPK 222
Cdd:cd14196   161 EIEDGVEFKNIFgTPEFVAPEIV------NYEPLGL------------EADMWSIGVITYILLSGASPFLGDTKQETLAN 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1704602876 223 dmrrkIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14196   223 -----ITAVSYDFDEEFFSHTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
72-273 8.26e-28

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: 110.77  E-value: 8.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  72 HPNIVQIIEVFANSvqfphessprARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ-------------------- 131
Cdd:cd14009    51 HPNIVRLYDVQKTE----------DFIYLVLEYCAGGDLSQYIRKRGRLPEAVARHFMQQlasglkflrskniihrdlkp 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 132 ----------DAPVKLCDFGFAKIDQGDLMTPQF--TPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGV 199
Cdd:cd14009   121 qnlllstsgdDPVLKIADFGFARSLQPASMAETLcgSPLYMAPEILQFQK------------------YDAKADLWSVGA 182
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1704602876 200 IIYVMLCGYPPFYSKHHSrtipkDMRRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPW 273
Cdd:cd14009   183 ILFEMLVGKPPFRGSNHV-----QLLRNIERSDAVIPFPIAAQLSPDCKDLLRRLLRRDPAERISFEEFFAHPF 251
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
26-276 1.35e-27

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: 110.86  E-value: 1.35e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKIL-----------LDRPKARNEVRLhMMCATHPNIVQIIEVFANsvqfphessp 94
Cdd:cd14195    11 EELGSGQFAIVRKCREKGTGKEYAAKFIkkrrlsssrrgVSREEIEREVNI-LREIQHPNIITLHDIFEN---------- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  95 RARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ----------------------------DAP---VKLCDFGFA 143
Cdd:cd14195    80 KTDVVLILELVSGGELFDFLAEKESLTEEEATQFLKQildgvhylhskriahfdlkpenimlldkNVPnprIKLIDFGIA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 144 -KIDQGDLMTPQF-TPYYVAPQVLeaqrrhQKEKSGIiptsptpytynkSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIP 221
Cdd:cd14195   160 hKIEAGNEFKNIFgTPEFVAPEIV------NYEPLGL------------EADMWSIGVITYILLSGASPFLGETKQETLT 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1704602876 222 KdmrrkIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNS 276
Cdd:cd14195   222 N-----ISAVNYDFDEEYFSNTSELAKDFIRRLLVKDPKKRMTIAQSLEHSWIKA 271
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
28-275 3.14e-27

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: 109.24  E-value: 3.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILldRPKARNEVRL--H-------MMCATHPNIVQIIEVFANsvqfphesspRARL 98
Cdd:cd05572     1 LGVGGFGRVELVQLKSKGRTFALKCV--KKRHIVQTRQqeHifsekeiLEECNSPFIVKLYRTFKD----------KKYL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  99 LIVMEMMEGGELFHRISQHRHFTEKQA----SQVTKQ---------------------DAP--VKLCDFGFAKIDQGDLM 151
Cdd:cd05572    69 YMLMEYCLGGELWTILRDRGLFDEYTArfytACVVLAfeylhsrgiiyrdlkpenlllDSNgyVKLVDFGFAKKLGSGRK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 152 TPQF--TPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFyskhhsrTIPKDMRRKIM 229
Cdd:cd05572   149 TWTFcgTPEYVAPEIILNK------------------GYDFSVDYWSLGILLYELLTGRPPF-------GGDDEDPMKIY 203
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1704602876 230 ------TGSFEFPeeewSQISEMAKDVVRKLLKVKPEERL-----TIEGVLDHPWLN 275
Cdd:cd05572   204 niilkgIDKIEFP----KYIDKNAKNLIKQLLRRNPEERLgylkgGIRDIKKHKWFE 256
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
28-276 6.71e-27

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: 110.14  E-value: 6.71e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILL-DRPKARNEVRlHMMCAT-------HPNIVQIievfANSVQFPHesspraRLL 99
Cdd:cd05571     3 LGKGTFGKVILCREKATGELYAIKILKkEVIIAKDEVA-HTLTENrvlqntrHPFLTSL----KYSFQTND------RLC 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMEGGELFHRISQHRHFTEKQA----SQVT-----------------------KQDAPVKLCDFGFAK--IDQGDl 150
Cdd:cd05571    72 FVMEYVNGGELFFHLSRERVFSEDRTrfygAEIVlalgylhsqgivyrdlklenlllDKDGHIKITDFGLCKeeISYGA- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 151 MTPQF--TPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRtipkdMRRKI 228
Cdd:cd05571   151 TTKTFcgTPEYLAPEVLEDN------------------DYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEV-----LFELI 207
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1704602876 229 MTGSFEFPeeewSQISEMAKDVVRKLLKVKPEERL-----TIEGVLDHPWLNS 276
Cdd:cd05571   208 LMEEVRFP----STLSPEAKSLLAGLLKKDPKKRLgggprDAKEIMEHPFFAS 256
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
23-274 7.43e-27

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: 108.55  E-value: 7.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  23 NWTQKLGAGISGPVRVCVKKSTQERFALKILL-----DRPKARNEVRLhMMCATHPNIVQIIEVFANsvqfphesspRAR 97
Cdd:cd14191     5 DIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKaysakEKENIRQEISI-MNCLHHPKLVQCVDAFEE----------KAN 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  98 LLIVMEMMEGGELFHRI-SQHRHFTEKQASQ-----------------------------VTKQDAPVKLCDFGFAKI-- 145
Cdd:cd14191    74 IVMVLEMVSGGELFERIiDEDFELTERECIKymrqisegveyihkqgivhldlkpenimcVNKTGTKIKLIDFGLARRle 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 146 DQGDLMTPQFTPYYVAPQVLEAQrrhqkeksgiiptsptPYTYnkSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKdmr 225
Cdd:cd14191   154 NAGSLKVLFGTPEFVAPEVINYE----------------PIGY--ATDMWSIGVICYILVSGLSPFMGDNDNETLAN--- 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1704602876 226 rkIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14191   213 --VTSATWDFDDEAFDEISDDAKDFISNLLKKDMKARLTCTQCLQHPWL 259
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
18-274 1.73e-26

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: 107.21  E-value: 1.73e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  18 EEYSINwTQKLGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLHMMCaTHPNIVQIIEVFansvqfphESSPRAr 97
Cdd:cd14109     3 ELYEIG-EEDEKRAAQGAPFHVTERSTGRNFLAQLRYGDPFLMREVDIHNSL-DHPNIVQMHDAY--------DDEKLA- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  98 LLIVMEMMEGGELF--HRISQHRHFTEKQASQVTKQ--------------------------DAPVKLCDFGFA-KIDQG 148
Cdd:cd14109    72 VTVIDNLASTIELVrdNLLPGKDYYTERQVAVFVRQlllalkhmhdlgiahldlrpedillqDDKLKLADFGQSrRLLRG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 149 DLMTPQF-TPYYVAPQVLEAqrrhqkeksgiiptsptpYTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIpkdmrRK 227
Cdd:cd14109   152 KLTTLIYgSPEFVSPEIVNS------------------YPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETL-----TN 208
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1704602876 228 IMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14109   209 VRSGKWSFDSSPLGNISDDARDFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
26-277 1.79e-26

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: 109.30  E-value: 1.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKIL-----LDRPKARN--EVRLHMMCATHPNIVQIIEVFansvQFPHesspraRL 98
Cdd:cd05573     7 KVIGRGAFGEVWLVRDKDTGQVYAMKILrksdmLKREQIAHvrAERDILADADSPWIVRLHYAF----QDED------HL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  99 LIVMEMMEGGELFHRISQHRHFTEKQA-----------SQVTKQ----------------DAPVKLCDFGFAK--IDQGD 149
Cdd:cd05573    77 YLVMEYMPGGDLMNLLIKYDVFPEETArfyiaelvlalDSLHKLgfihrdikpdnilldaDGHIKLADFGLCTkmNKSGD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 150 LMTPQFTPYYVAPQVLEAQRRHQKEKSGIIPTSP--TP-YT---------YNKSCDLWSLGVIIYVMLCGYPPFYSKHHS 217
Cdd:cd05573   157 RESYLNDSVNTLFQDNVLARRRPHKQRRVRAYSAvgTPdYIapevlrgtgYGPECDWWSLGVILYEMLYGFPPFYSDSLV 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1704602876 218 RTipkdmRRKIMTG--SFEFPEEEwsQISEMAKDVVRKLLKvKPEERLT-IEGVLDHPWLNST 277
Cdd:cd05573   237 ET-----YSKIMNWkeSLVFPDDP--DVSPEAIDLIRRLLC-DPEDRLGsAEEIKAHPFFKGI 291
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
27-274 1.99e-26

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: 107.04  E-value: 1.99e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  27 KLGAGISGPVRVCVKKSTQERFALKILlDRPKARNEV-RL------HMMCATHPNIVQIIEVfansVQFPhessprARLL 99
Cdd:cd14075     9 ELGSGNFSQVKLGIHQLTKEKVAIKIL-DKTKLDQKTqRLlsreisSMEKLHHPNIIRLYEV----VETL------SKLH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMEGGELFHRISQHRHFTEKQASQVTKQ---------------------------DAPVKLCDFGFAKIDQGDLMT 152
Cdd:cd14075    78 LVMEYASGGELYTKISTEGKLSESEAKPLFAQivsavkhmhenniihrdlkaenvfyasNNCVKVGDFGFSTHAKRGETL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 153 PQF--TPYYVAPQVLEAQrrhqkeksgiiptsptpYTYNKSCDLWSLGVIIYVMLCGYPPFyskhHSRTIPKdMRRKIMT 230
Cdd:cd14075   158 NTFcgSPPYAAPELFKDE-----------------HYIGIYVDIWALGVLLYFMVTGVMPF----RAETVAK-LKKCILE 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1704602876 231 GSFEFPeeewSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14075   216 GTYTIP----SYVSEPCQELIRGILQPVPSDRYSIDEIKNSEWL 255
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
20-273 2.10e-26

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: 107.11  E-value: 2.10e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  20 YSINWTQKLGAGISGPVRVCVKKSTQERFALKIL--LDRPKA-----RNEVR-LHMMCatHPNIVQIIEVFANsvqfphe 91
Cdd:cd14082     3 YQIFPDEVLGSGQFGIVYGGKHRKTGRDVAIKVIdkLRFPTKqesqlRNEVAiLQQLS--HPGVVNLECMFET------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  92 sspRARLLIVMEMMEG-----------GELFHRISQ-----------HRHFTE------KQASQVTKQDAP---VKLCDF 140
Cdd:cd14082    74 ---PERVFVVMEKLHGdmlemilssekGRLPERITKflvtqilvalrYLHSKNivhcdlKPENVLLASAEPfpqVKLCDF 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 141 GFAKIdqgdLMTPQF------TPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSK 214
Cdd:cd14082   151 GFARI----IGEKSFrrsvvgTPAYLAPEVLRNKG------------------YNRSLDMWSVGVIIYVSLSGTFPFNED 208
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1704602876 215 hhsrtipKDMRRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPW 273
Cdd:cd14082   209 -------EDINDQIQNAAFMYPPNPWKEISPDAIDLINNLLQVKMRKRYSVDKSLSHPW 260
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
18-274 4.23e-26

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: 106.56  E-value: 4.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  18 EEYSINWTQKLGAGISGPVRVCVKKSTQERFALKILLDRPKARN-------EVRLHMMCATHPNIVQIIEVFANSVQfph 90
Cdd:cd14197     7 ERYSLSPGRELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDcrmeiihEIAVLELAQANPWVINLHEVYETASE--- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  91 essprarLLIVMEMMEGGELFHRISQHRH--FTEKQASQVTKQ---------------------------DAP---VKLC 138
Cdd:cd14197    84 -------MILVLEYAAGGEIFNQCVADREeaFKEKDVKRLMKQilegvsflhnnnvvhldlkpqnilltsESPlgdIKIV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 139 DFGFAKI--DQGDLMTPQFTPYYVAPQVLEAQrrhqkeksgiiPTSptpytynKSCDLWSLGVIIYVMLCGYPPFYSKHH 216
Cdd:cd14197   157 DFGLSRIlkNSEELREIMGTPEYVAPEILSYE-----------PIS-------TATDMWSIGVLAYVMLTGISPFLGDDK 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1704602876 217 SRTIpkdmrRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14197   219 QETF-----LNISQMNVSYSEEEFEHLSESAIDFIKTLLIKKPENRATAEDCLKHPWL 271
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
34-275 4.61e-26

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: 106.53  E-value: 4.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  34 GPVRVCVKKSTQERFALKIL----------LDRPKARNEVrlhMMCATHPNIVQIIEVFANsvqfphesspRARLLIVME 103
Cdd:cd05579     7 GRVYLAKKKSTGDLYAIKVIkkrdmirknqVDSVLAERNI---LSQAQNPFVVKLYYSFQG----------KKNLYLVME 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 104 MMEGGELFHRISQHRHFTEKQASQVTKQ---------------------------DAPVKLCDFGFAKI----DQGDLMT 152
Cdd:cd05579    74 YLPGGDLYSLLENVGALDEDVARIYIAEivlaleylhshgiihrdlkpdnilidaNGHLKLTDFGLSKVglvrRQIKLSI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 153 PQF--------------TPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFyskhHSR 218
Cdd:cd05579   154 QKKsngapekedrrivgTPDYLAPEILLGQ------------------GHGKTVDWWSLGVILYEFLVGIPPF----HAE 211
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 219 TiPKDMRRKIMTGSFEFPEEEwsQISEMAKDVVRKLLKVKPEERL---TIEGVLDHPWLN 275
Cdd:cd05579   212 T-PEEIFQNILNGKIEWPEDP--EVSDEAKDLISKLLTPDPEKRLgakGIEEIKNHPFFK 268
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
20-264 1.20e-25

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: 104.98  E-value: 1.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  20 YSInwTQKLGAGISGPVRVCVKKSTQERFALKILL----DRPKAR----NEVRLHMMCAtHPNIVQIIEVFAnsvqfpHE 91
Cdd:cd14014     2 YRL--VRLLGRGGMGEVYRARDTLLGRPVAIKVLRpelaEDEEFRerflREARALARLS-HPNIVRVYDVGE------DD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  92 SSPrarlLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ---------------------------DAPVKLCDFGFAK 144
Cdd:cd14014    73 GRP----YIVMEYVEGGSLADLLRERGPLPPREALRILAQiadalaaahragivhrdikpanillteDGRVKLTDFGIAR 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 145 IDQGDLMTP----QFTPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFyskhhSRTI 220
Cdd:cd14014   149 ALGDSGLTQtgsvLGTPAYMAPEQARGGP------------------VDPRSDIYSLGVVLYELLTGRPPF-----DGDS 205
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1704602876 221 PKDMRRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLT 264
Cdd:cd14014   206 PAAVLAKHLQEAPPPPSPLNPDVPPALDAIILRALAKDPEERPQ 249
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
17-274 1.58e-25

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: 104.59  E-value: 1.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  17 LEEYSINwtQKLGAGISGPVRVCVKKSTQERFALKIL-----LDRPKARNEVRLhMMCATHPNIVQIIEVFANSVQfphe 91
Cdd:cd14114     1 YDHYDIL--EELGTGAFGVVHRCTERATGNNFAAKFImtpheSDKETVRKEIQI-MNQLHHPKLINLHDAFEDDNE---- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  92 ssprarLLIVMEMMEGGELFHRIS-QHRHFTEKQA----SQV-------------------------TKQDAPVKLCDFG 141
Cdd:cd14114    74 ------MVLILEFLSGGELFERIAaEHYKMSEAEVinymRQVceglchmhennivhldikpenimctTKRSNEVKLIDFG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 142 FA-KIDQGDLM-TPQFTPYYVAPQVLEaqrrhqKEKSGIiptsptpYTynkscDLWSLGVIIYVMLCGYPPFYSKHHSRT 219
Cdd:cd14114   148 LAtHLDPKESVkVTTGTAEFAAPEIVE------REPVGF-------YT-----DMWAVGVLSYVLLSGLSPFAGENDDET 209
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1704602876 220 IpkdmrRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14114   210 L-----RNVKSCDWNFDDSAFSGISEEAKDFIRKLLLADPNKRMTIHQALEHPWL 259
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
23-274 1.61e-25

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: 104.52  E-value: 1.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  23 NWT--QKLGAGISGPVRVCVKKSTQERFALK-ILLDRPKA------RNEVRLhmMCA-THPNIVQIievfansvqFPHES 92
Cdd:cd06606     1 RWKkgELLGKGSFGSVYLALNLDTGELMAVKeVELSGDSEeelealEREIRI--LSSlKHPNIVRY---------LGTER 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  93 SPRArLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ---------------------------DAPVKLCDFGFAK- 144
Cdd:cd06606    70 TENT-LNIFLEYVPGGSLASLLKKFGKLPEPVVRKYTRQilegleylhsngivhrdikganilvdsDGVVKLADFGCAKr 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 145 ----IDQGDLMTPQFTPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTI 220
Cdd:cd06606   149 laeiATGEGTKSLRGTPYWMAPEVIRGEG------------------YGRAADIWSLGCTVIEMATGKPPWSELGNPVAA 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1704602876 221 pkdMRRKIMTGSF-EFPEeewsQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd06606   211 ---LFKIGSSGEPpPIPE----HLSEEAKDFLRKCLQRDPKKRPTADELLQHPFL 258
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
27-272 1.94e-25

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: 104.40  E-value: 1.94e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  27 KLGAGISGPVRVCVKKSTQERFALKIL-------LDRPKARNEVRLhMMCATHPNIVQIIEVFANSvqfphessprARLL 99
Cdd:cd08530     7 KLGKGSYGSVYKVKRLSDNQVYALKEVnlgslsqKEREDSVNEIRL-LASVNHPNIIRYKEAFLDG----------NRLC 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMEGGELFHRISQH----RHFTE---------------------------KQASQVTKQDAPVKLCDFGFAKIDQG 148
Cdd:cd08530    76 IVMEYAPFGDLSKLISKRkkkrRLFPEddiwrifiqmlrglkalhdqkilhrdlKSANILLSAGDLVKIGDLGISKVLKK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 149 DLMTPQF-TPYYVAPQVLeaQRRhqkeksgiiptsptPYTYNksCDLWSLGVIIYVMLCGYPPFyskhHSRTIpKDMRRK 227
Cdd:cd08530   156 NLAKTQIgTPLYAAPEVW--KGR--------------PYDYK--SDIWSLGCLLYEMATFRPPF----EARTM-QELRYK 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1704602876 228 IMTGSFEFPEEEWSQisEMAKdVVRKLLKVKPEERLTIEGVLDHP 272
Cdd:cd08530   213 VCRGKFPPIPPVYSQ--DLQQ-IIRSLLQVNPKKRPSCDKLLQSP 254
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
28-273 2.31e-25

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: 104.08  E-value: 2.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLHMM---CATHPNIVQIIEVFANSVQfphessprarLLIVMEM 104
Cdd:cd14662     8 IGSGNFGVARLMRNKETKELVAVKYIERGLKIDENVQREIInhrSLRHPNIIRFKEVVLTPTH----------LAIVMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 105 MEGGELFHRISQHRHFTEKQAS----------------QVTKQD------------AP-VKLCDFGFAK--IDQGDLMTP 153
Cdd:cd14662    78 AAGGELFERICNAGRFSEDEARyffqqlisgvsychsmQICHRDlklentlldgspAPrLKICDFGYSKssVLHSQPKST 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 154 QFTPYYVAPQVLEaqrrhQKEKSGiiptsptpytynKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDMRRkIMTGSF 233
Cdd:cd14662   158 VGTPAYIAPEVLS-----RKEYDG------------KVADVWSCGVTLYVMLVGAYPFEDPDDPKNFRKTIQR-IMSVQY 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1704602876 234 EFPeeEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPW 273
Cdd:cd14662   220 KIP--DYVRVSQDCRHLLSRIFVANPAKRITIPEIKNHPW 257
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
16-274 4.79e-25

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: 103.23  E-value: 4.79e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  16 ILEEYSINWTqkLGAGISGPVRVCVKKSTQERFALKIL------LDRPKARNEVRLhMMCATHPNIVQIIEVFANSvqfp 89
Cdd:cd14078     1 LLKYYELHET--IGSGGFAKVKLATHILTGEKVAIKIMdkkalgDDLPRVKTEIEA-LKNLSHQHICRLYHVIETD---- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  90 hessprARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ---------------------------DAPVKLCDFGF 142
Cdd:cd14078    74 ------NKIFMVLEYCPGGELFDYIVAKDRLSEDEARVFFRQivsavayvhsqgyahrdlkpenllldeDQNLKLIDFGL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 143 -AKIDQG---DLMTPQFTPYYVAPQVLEAQrrhqkeksgiiptsptPYTYNKScDLWSLGVIIYVMLCGYPPFyskhHSR 218
Cdd:cd14078   148 cAKPKGGmdhHLETCCGSPAYAAPELIQGK----------------PYIGSEA-DVWSMGVLLYALLCGFLPF----DDD 206
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1704602876 219 TIPKdMRRKIMTGSFEFPeeEWsqISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14078   207 NVMA-LYRKIQSGKYEEP--EW--LSPSSKLLLDQMLQVDPKKRITVKELLNHPWV 257
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
20-274 6.10e-25

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: 103.12  E-value: 6.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  20 YSINWTQKLGAGISGPVRVCVKKSTQERFALKILL-----DRPKARNEVRLhMMCATHPNIVQIIEVFansvqfphESsp 94
Cdd:cd14192     4 YAVCPHEVLGGGRFGQVHKCTELSTGLTLAAKIIKvkgakEREEVKNEINI-MNQLNHVNLIQLYDAF--------ES-- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  95 RARLLIVMEMMEGGELFHRISQHR-HFTEKQASQVTKQ-----------------------------DAPVKLCDFGFA- 143
Cdd:cd14192    73 KTNLTLIMEYVDGGELFDRITDESyQLTELDAILFTRQicegvhylhqhyilhldlkpenilcvnstGNQIKIIDFGLAr 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 144 KIDQGDLMTPQF-TPYYVAPQVLEAQrrhqkeksgiIPTSPTpytynkscDLWSLGVIIYVMLCGYPPFYSKHHSRTIpk 222
Cdd:cd14192   153 RYKPREKLKVNFgTPEFLAPEVVNYD----------FVSFPT--------DMWSVGVITYMLLSGLSPFLGETDAETM-- 212
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1704602876 223 dmrRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14192   213 ---NNIVNCKWDFDAEAFENLSEEAKDFISRLLVKEKSCRMSATQCLKHEWL 261
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
18-274 7.66e-25

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: 102.69  E-value: 7.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  18 EEYSINWTQKLGAGISGPVRVCVKKSTQERFALKILLDR-PKARNEVRLHMMCA---THPNIVQIIEVFansvQFPHEss 93
Cdd:cd14190     2 STFSIHSKEVLGGGKFGKVHTCTEKRTGLKLAAKVINKQnSKDKEMVLLEIQVMnqlNHRNLIQLYEAI----ETPNE-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  94 prarLLIVMEMMEGGELFHRI-SQHRHFTEKQASQVTKQ-----------------------------DAPVKLCDFGFA 143
Cdd:cd14190    76 ----IVLFMEYVEGGELFERIvDEDYHLTEVDAMVFVRQicegiqfmhqmrvlhldlkpenilcvnrtGHQVKIIDFGLA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 144 K-IDQGDLMTPQF-TPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIp 221
Cdd:cd14190   152 RrYNPREKLKVNFgTPEFLSPEVVNYDQ------------------VSFPTDMWSMGVITYMLLSGLSPFLGDDDTETL- 212
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1704602876 222 kdmrRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14190   213 ----NNVLMGNWYFDEETFEHVSDEAKDFVSNLIIKERSARMSATQCLKHPWL 261
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
29-275 1.12e-24

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: 103.85  E-value: 1.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  29 GAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLH-------MMCATHPNIVQIIEVFANSVQfphessprarLLIV 101
Cdd:cd05599    10 GRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKEQVAHvraerdiLAEADNPWVVKLYYSFQDEEN----------LYLI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 102 MEMMEGGELFHRISQHRHFTEKQA-----------SQVTK----------------QDAPVKLCDFGFAKIDQGDLMTpq 154
Cdd:cd05599    80 MEFLPGGDMMTLLMKKDTLTEEETrfyiaetvlaiESIHKlgyihrdikpdnllldARGHIKLSDFGLCTGLKKSHLA-- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 155 F----TPYYVAPQVLEaqrrhqkeKSGiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHhsrtiPKDMRRKIMT 230
Cdd:cd05599   158 YstvgTPDYIAPEVFL--------QKG----------YGKECDWWSLGVIMYEMLIGYPPFCSDD-----PQETCRKIMN 214
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1704602876 231 --GSFEFPEEEwsQISEMAKDVVRKLLkVKPEERLTIEGVLD---HPWLN 275
Cdd:cd05599   215 wrETLVFPPEV--PISPEAKDLIERLL-CDAEHRLGANGVEEiksHPFFK 261
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
23-274 1.88e-24

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: 101.76  E-value: 1.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  23 NW--TQKLGAGISGPVRVCVKKSTQERFALKILLDRPKA----RNEVRLHMMCAT---------------HPNIVQIIEV 81
Cdd:cd14077     2 NWefVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPRASNAglkkEREKRLEKEISRdirtireaalssllnHPHICRLRDF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  82 FANSVQFphessprarlLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQDAP--------------------------- 134
Cdd:cd14077    82 LRTPNHY----------YMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASaldylhrnsivhrdlkienilisksgn 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 135 VKLCDFGFAKI--DQGDLMTPQFTPYYVAPQVLEAQrrhqkeksgiiptsptPYTyNKSCDLWSLGVIIYVMLCGYPPFY 212
Cdd:cd14077   152 IKIIDFGLSNLydPRRLLRTFCGSLYFAAPELLQAQ----------------PYT-GPEVDVWSFGVVLYVLVCGKVPFD 214
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1704602876 213 SKHHSRtipkdMRRKIMTGSFEFPeeewSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14077   215 DENMPA-----LHAKIKKGKVEYP----SYLSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
13-262 3.13e-24

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 104.71  E-value: 3.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  13 ETSILEEYSInwTQKLGAGISGPVRVCVKKSTQERFALKILL----DRPKAR----NEVRLhMMCATHPNIVQIIEVFan 84
Cdd:COG0515     2 SALLLGRYRI--LRLLGRGGMGVVYLARDLRLGRPVALKVLRpelaADPEARerfrREARA-LARLNHPNIVRVYDVG-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  85 svqfphesSPRARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ---------------------------DAPVKL 137
Cdd:COG0515    77 --------EEDGRPYLVMEYVEGESLADLLRRRGPLPPAEALRILAQlaealaaahaagivhrdikpanilltpDGRVKL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 138 CDFGFAKIDQGDLMTPQ----FTPYYVAPQVLEAQRrhqkeksgiiptsPTPYTynkscDLWSLGVIIYVMLCGYPPFys 213
Cdd:COG0515   149 IDFGIARALGGATLTQTgtvvGTPGYMAPEQARGEP-------------VDPRS-----DVYSLGVTLYELLTGRPPF-- 208
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1704602876 214 khhSRTIPKDMRRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEER 262
Cdd:COG0515   209 ---DGDSPAELLRAHLREPPPPPSELRPDLPPALDAIVLRALAKDPEER 254
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
26-273 4.81e-24

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: 100.75  E-value: 4.81e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKIL----LDRPKARNEV---RLHMMCATHPNIVQIIEVFansvQFPHesspraRL 98
Cdd:cd05581     7 KPLGEGSYSTVVLAKEKETGKEYAIKVLdkrhIIKEKKVKYVtieKEVLSRLAHPGIVKLYYTF----QDES------KL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  99 LIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ---------------------------DAPVKLCDFGFAKIDQGDLM 151
Cdd:cd05581    77 YFVLEYAPNGDLLEYIRKYGSLDEKCTRFYTAEivlaleylhskgiihrdlkpenilldeDMHIKITDFGTAKVLGPDSS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 152 TPQF--------------------TPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPF 211
Cdd:cd05581   157 PESTkgdadsqiaynqaraasfvgTAEYVSPELLNEKP------------------AGKSSDLWALGCIIYQMLTGKPPF 218
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1704602876 212 YSKHHSRTIpkdmrRKIMTGSFEFPEeewsQISEMAKDVVRKLLKVKPEERLTIEGVLD------HPW 273
Cdd:cd05581   219 RGSNEYLTF-----QKIVKLEYEFPE----NFPPDAKDLIQKLLVLDPSKRLGVNENGGydelkaHPF 277
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
28-273 7.22e-24

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 101.43  E-value: 7.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLH-------MMCATHPNIVQIIEVFANsvqfphesspRARLLI 100
Cdd:PTZ00263   26 LGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHvaqeksiLMELSHPFIVNMMCSFQD----------ENRVYF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 101 VMEMMEGGELFHRISQHRHFTE---------------------------KQASQVTKQDAPVKLCDFGFAKIDQGDLMTP 153
Cdd:PTZ00263   96 LLEFVVGGELFTHLRKAGRFPNdvakfyhaelvlafeylhskdiiyrdlKPENLLLDNKGHVKVTDFGFAKKVPDRTFTL 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 154 QFTPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIpkdmrRKIMTGSF 233
Cdd:PTZ00263  176 CGTPEYLAPEVIQSK------------------GHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIY-----EKILAGRL 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1704602876 234 EFPeeEWsqISEMAKDVVRKLLKVKPEERL-----TIEGVLDHPW 273
Cdd:PTZ00263  233 KFP--NW--FDGRARDLVKGLLQTDHTKRLgtlkgGVADVKNHPY 273
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
20-274 9.51e-24

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: 99.60  E-value: 9.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  20 YSINWTQKLGAGISGPVRVCVKKSTQERFALKILLDR-PKARNEVRLH---MMCATHPNIVQIIEVFansvqfphESspR 95
Cdd:cd14193     4 YNVNKEEILGGGRFGQVHKCEEKSSGLKLAAKIIKARsQKEKEEVKNEievMNQLNHANLIQLYDAF--------ES--R 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  96 ARLLIVMEMMEGGELFHRI-SQHRHFTE-------KQASQ----------------------VTKQDAPVKLCDFGFAK- 144
Cdd:cd14193    74 NDIVLVMEYVDGGELFDRIiDENYNLTEldtilfiKQICEgiqymhqmyilhldlkpenilcVSREANQVKIIDFGLARr 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 145 IDQGDLMTPQF-TPYYVAPQVLEAQrrhqkeksgiIPTSPTpytynkscDLWSLGVIIYVMLCGYPPFYSKHHSRTIpkd 223
Cdd:cd14193   154 YKPREKLRVNFgTPEFLAPEVVNYE----------FVSFPT--------DMWSLGVIAYMLLSGLSPFLGEDDNETL--- 212
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1704602876 224 mrRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14193   213 --NNILACQWDFEDEEFADISEEAKDFISKLLIKEKSWRMSASEALKHPWL 261
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
28-272 1.25e-23

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: 98.11  E-value: 1.25e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILL------DRPKARNEVRLHMMCaTHPNIVQIIEVFANsvqfphesspRARLLIV 101
Cdd:cd00180     1 LGKGSFGKVYKARDKETGKKVAVKVIPkeklkkLLEELLREIEILKKL-NHPNIVKLYDVFET----------ENFLYLV 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 102 MEMMEGGELFHRISQHRH-FTEKQASQVTKQ---------------------------DAPVKLCDFGFAKIDQGDLMTP 153
Cdd:cd00180    70 MEYCEGGSLKDLLKENKGpLSEEEALSILRQllsaleylhsngiihrdlkpenilldsDGTVKLADFGLAKDLDSDDSLL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 154 QFTPYYVAPQVLEAQRRHQKEksgiiptsptpytYNKSCDLWSLGVIIYVMlcgyppfyskhhsrtipkdmrrkimtgsf 233
Cdd:cd00180   150 KTTGGTTPPYYAPPELLGGRY-------------YGPKVDIWSLGVILYEL----------------------------- 187
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1704602876 234 efpeeewsqisEMAKDVVRKLLKVKPEERLTIEGVLDHP 272
Cdd:cd00180   188 -----------EELKDLIRRMLQYDPKKRPSAKELLEHL 215
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
25-274 1.90e-23

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: 99.23  E-value: 1.90e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  25 TQKLGAGISGPVRVCVKKSTQERFALKILLDRPKARN-------EVRLHMMCATHPNIVQIIEVFANSVQ---------- 87
Cdd:cd14198    13 SKELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDcraeilhEIAVLELAKSNPRVVNLHEVYETTSEiilileyaag 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  88 ---FPHESSPRARLL-------IVMEMMEGGELFHRiSQHRHFTEKQASQVTKQDAP---VKLCDFGFA-KIDQ-GDLMT 152
Cdd:cd14198    93 geiFNLCVPDLAEMVsendiirLIRQILEGVYYLHQ-NNIVHLDLKPQNILLSSIYPlgdIKIVDFGMSrKIGHaCELRE 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 153 PQFTPYYVAPQVLEAQrrhqkeksgiiptsptPYTynKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIpkdmrRKIMTGS 232
Cdd:cd14198   172 IMGTPEYLAPEILNYD----------------PIT--TATDMWNIGVIAYMLLTHESPFVGEDNQETF-----LNISQVN 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1704602876 233 FEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14198   229 VDYSEETFSSVSQLATDFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
28-281 2.56e-23

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: 100.08  E-value: 2.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILldRPK---ARNEVRlHMMcaTHPNIVQ-IIEVFANSVQFPHESspRARLLIVME 103
Cdd:cd05595     3 LGKGTFGKVILVREKATGRYYAMKIL--RKEviiAKDEVA-HTV--TESRVLQnTRHPFLTALKYAFQT--HDRLCFVME 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 104 MMEGGELFHRISQHRHFTEKQA---------------------------SQVTKQDAPVKLCDFGFAK---IDQGDLMTP 153
Cdd:cd05595    76 YANGGELFFHLSRERVFTEDRArfygaeivsaleylhsrdvvyrdikleNLMLDKDGHIKITDFGLCKegiTDGATMKTF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 154 QFTPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRtipkdMRRKIMTGSF 233
Cdd:cd05595   156 CGTPEYLAPEVLEDN------------------DYGRAVDWWGLGVVMYEMMCGRLPFYNQDHER-----LFELILMEEI 212
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1704602876 234 EFPEeewsQISEMAKDVVRKLLKVKPEERL-----TIEGVLDHPWLNSTEALD 281
Cdd:cd05595   213 RFPR----TLSPEAKSLLAGLLKKDPKQRLgggpsDAKEVMEHRFFLSINWQD 261
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
26-275 2.78e-23

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: 98.44  E-value: 2.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALK-ILLDRPKAR---NEVRLHMMCAtHPNIVQIIEvfanSVQFPHEssprarLLIV 101
Cdd:cd06614     6 EKIGEGASGEVYKATDRATGKEVAIKkMRLRKQNKEliiNEILIMKECK-HPNIVDYYD----SYLVGDE------LWVV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 102 MEMMEGGELFHRISQHRH-FTEKQASQVTKQ---------------------------DAPVKLCDFGFAkidqGDLMTP 153
Cdd:cd06614    75 MEYMDGGSLTDIITQNPVrMNESQIAYVCREvlqgleylhsqnvihrdiksdnillskDGSVKLADFGFA----AQLTKE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 154 QF-------TPYYVAPQVLeaqRRHQkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYskhhsRTIPKDMRR 226
Cdd:cd06614   151 KSkrnsvvgTPYWMAPEVI---KRKD---------------YGPKVDIWSLGIMCIEMAEGEPPYL-----EEPPLRALF 207
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1704602876 227 KIMT-GSFEFPE-EEWSQIsemAKDVVRKLLKVKPEERLTIEGVLDHPWLN 275
Cdd:cd06614   208 LITTkGIPPLKNpEKWSPE---FKDFLNKCLVKDPEKRPSAEELLQHPFLK 255
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
18-274 4.20e-23

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: 97.71  E-value: 4.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  18 EEYSInwTQKLGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLH------MMCATHPNIVQIIEVFANSVQFphe 91
Cdd:cd14002     1 ENYHV--LELIGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSEKELRNLrqeieiLRKLNHPNIIEMLDSFETKKEF--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  92 ssprarlLIVMEMMEGgELFHRISQHRHFTEKQASQVTKQ---------------------------DAPVKLCDFGFAK 144
Cdd:cd14002    76 -------VVVTEYAQG-ELFQILEDDGTLPEEEVRSIAKQlvsalhylhsnriihrdmkpqniligkGGVVKLCDFGFAR 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 145 ---IDQGDLMTPQFTPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIp 221
Cdd:cd14002   148 amsCNTLVLTSIKGTPLYMAPELVQEQP------------------YDHTADLWSLGCILYELFVGQPPFYTNSIYQLV- 208
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1704602876 222 kdmrRKIMTGSFEFPEEewsqISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14002   209 ----QMIVKDPVKWPSN----MSPEFKSFLQGLLNKDPSKRLSWPDLLEHPFV 253
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
26-273 9.53e-23

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: 96.98  E-value: 9.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLHMM---CATHPNIVQIIEVFANSVQfphessprarLLIVM 102
Cdd:cd14665     6 KDIGSGNFGVARLMRDKQTKELVAVKYIERGEKIDENVQREIInhrSLRHPNIVRFKEVILTPTH----------LAIVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 103 EMMEGGELFHRISQHRHFTEKQAS----------------QVTKQD------------AP-VKLCDFGFAKidqGDLMTP 153
Cdd:cd14665    76 EYAAGGELFERICNAGRFSEDEARfffqqlisgvsychsmQICHRDlklentlldgspAPrLKICDFGYSK---SSVLHS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 154 Q-----FTPYYVAPQVLEaqrrhQKEKSGiiptsptpytynKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDMRRkI 228
Cdd:cd14665   153 QpkstvGTPAYIAPEVLL-----KKEYDG------------KIADVWSCGVTLYVMLVGAYPFEDPEEPRNFRKTIQR-I 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1704602876 229 MTGSFEFPeeEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPW 273
Cdd:cd14665   215 LSVQYSIP--DYVHISPECRHLISRIFVADPATRITIPEIRNHEW 257
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
28-285 1.09e-22

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: 98.60  E-value: 1.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKIL-----LDRPKARN--EVRLHMMCATHPNIVQIIEVFANSvqfphessprARLLI 100
Cdd:cd05596    34 IGRGAFGEVQLVRHKSTKKVYAMKLLskfemIKRSDSAFfwEERDIMAHANSEWIVQLHYAFQDD----------KYLYM 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 101 VMEMMEGGELFHRISQHrHFTEKQASQVTKQ-----DA------------P----------VKLCDFGFA-KIDQGDLM- 151
Cdd:cd05596   104 VMDYMPGGDLVNLMSNY-DVPEKWARFYTAEvvlalDAihsmgfvhrdvkPdnmlldasghLKLADFGTCmKMDKDGLVr 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 152 --TPQFTPYYVAPQVLEAQRRHQKeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDMRRKim 229
Cdd:cd05596   183 sdTAVGTPDYISPEVLKSQGGDGV--------------YGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIMNHK-- 246
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1704602876 230 tGSFEFPEEEwsQISEMAKDVVRKLLkVKPEERLTIEGVLD---HP--------WLNSTEALDNVLP 285
Cdd:cd05596   247 -NSLQFPDDV--EISKDAKSLICAFL-TDREVRLGRNGIEEikaHPffkndqwtWDNIRETVPPVVP 309
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
29-274 1.68e-22

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: 96.17  E-value: 1.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  29 GAGISGPVRVCVKKSTQERFALKIL-----LDRPKARN---EVRLhMMCATHPNIVQIIEVFANsvqfphesspRARLLI 100
Cdd:cd05578     9 GKGSFGKVCIVQKKDTKKMFAMKYMnkqkcIEKDSVRNvlnELEI-LQELEHPFLVNLWYSFQD----------EEDMYM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 101 VMEMMEGGELFHRISQHRHFTEKQA----------------SQVTKQD-AP----------VKLCDFGFAKIDQGDLMTP 153
Cdd:cd05578    78 VVDLLLGGDLRYHLQQKVKFSEETVkfyiceivlaldylhsKNIIHRDiKPdnilldeqghVHITDFNIATKLTDGTLAT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 154 QF--TPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSkhHSRTIPKDMRRKIMTG 231
Cdd:cd05578   158 STsgTKPYMAPEVFMRA------------------GYSFAVDWWSLGVTAYEMLRGKRPYEI--HSRTSIEEIRAKFETA 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1704602876 232 SFEFPeEEWsqiSEMAKDVVRKLLKVKPEERL-TIEGVLDHPWL 274
Cdd:cd05578   218 SVLYP-AGW---SEEAIDLINKLLERDPQKRLgDLSDLKNHPYF 257
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
71-274 1.97e-22

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: 96.40  E-value: 1.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  71 THPNIVQIIEVFANSVQFPhessprarllIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ------------------- 131
Cdd:cd14076    64 THPNIVRLLDVLKTKKYIG----------IVLEFVSGGELFDYILARRRLKDSVACRLFAQlisgvaylhkkgvvhrdlk 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 132 --------DAPVKLCDFGFAK---IDQGDLM-TPQFTPYYVAPQVLeaqrrhqkeksgiipTSPTPYTYNKScDLWSLGV 199
Cdd:cd14076   134 lenllldkNRNLVITDFGFANtfdHFNGDLMsTSCGSPCYAAPELV---------------VSDSMYAGRKA-DIWSCGV 197
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1704602876 200 IIYVMLCGYPPFYSKHHSRT---IPKdMRRKIMTGSFEFPEeewsQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14076   198 ILYAMLAGYLPFDDDPHNPNgdnVPR-LYRYICNTPLIFPE----YVTPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
26-274 2.93e-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: 95.48  E-value: 2.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKILlDRPKA--------RNEVRLHMMCaTHPNIVQIIEvfansvqfpHESSPRAR 97
Cdd:cd14069     7 QTLGEGAFGEVFLAVNRNTEEAVAVKFV-DMKRApgdcpeniKKEVCIQKML-SHKNVVRFYG---------HRREGEFQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  98 LlIVMEMMEGGELFHRIS---------QHRHFTEKQAS-------QVTKQD-AP----------VKLCDFGFAKIDQGD- 149
Cdd:cd14069    76 Y-LFLEYASGGELFDKIEpdvgmpedvAQFYFQQLMAGlkylhscGITHRDiKPenllldendnLKISDFGLATVFRYKg 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 150 ----LMTPQFTPYYVAPQVLeAQRRHQKEKSgiiptsptpytynkscDLWSLGVIIYVMLCGYPPFysKHHSRTIPKDMR 225
Cdd:cd14069   155 kerlLNKMCGTLPYVAPELL-AKKKYRAEPV----------------DVWSCGIVLFAMLAGELPW--DQPSDSCQEYSD 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1704602876 226 RKIMTGSFEFPeeeWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14069   216 WKENKKTYLTP---WKKIDTAALSLLRKILTENPNKRITIEDIKKHPWY 261
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
44-274 3.37e-22

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: 95.17  E-value: 3.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  44 TQERFALKILlDRPKARNEVRLH-------MMCATHPNIVQIIEVFANSvqfphessprARLLIVMEMMEGGELFHRISQ 116
Cdd:cd14074    27 TGEKVAVKVI-DKTKLDDVSKAHlfqevrcMKLVQHPNVVRLYEVIDTQ----------TKLYLILELGDGGDMYDYIMK 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 117 H-RHFTEKQASQVTKQ----------------------------DAPVKLCDFGFA-KIDQGD-LMTPQFTPYYVAPQVL 165
Cdd:cd14074    96 HeNGLNEDLARKYFRQivsaisychklhvvhrdlkpenvvffekQGLVKLTDFGFSnKFQPGEkLETSCGSLAYSAPEIL 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 166 EAQrrhqkeksgiiptsptpyTYNK-SCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPkdmrrKIMTGSFEFPeeewSQIS 244
Cdd:cd14074   176 LGD------------------EYDApAVDIWSLGVILYMLVCGQPPFQEANDSETLT-----MIMDCKYTVP----AHVS 228
                         250       260       270
                  ....*....|....*....|....*....|
gi 1704602876 245 EMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14074   229 PECKDLIRRMLIRDPKKRASLEEIENHPWL 258
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
39-274 3.89e-22

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: 94.80  E-value: 3.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  39 CVKKSTQERFALKILlDRPKARNEVRLHMMCATHPNIVQIIEVFANSVQFP------HE---SSPRARLLIVMEmmEGGE 109
Cdd:cd13976    12 CVDIHTGEELVCKVV-PVPECHAVLRAYFRLPSHPNISGVHEVIAGETKAYvfferdHGdlhSYVRSRKRLREP--EAAR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 110 LFHRISQhrhftekqASQVTKQDAPV----KLCDFGFAK---------------IDQGD---LMTPQFTPYYVAPQVLEA 167
Cdd:cd13976    89 LFRQIAS--------AVAHCHRNGIVlrdlKLRKFVFADeertklrlesledavILEGEddsLSDKHGCPAYVSPEILNS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 168 QRRHqkekSGiiptsptpytynKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPkdmrrKIMTGSFEFPEeewsQISEMA 247
Cdd:cd13976   161 GATY----SG------------KAADVWSLGVILYTMLVGRYPFHDSEPASLFA-----KIRRGQFAIPE----TLSPRA 215
                         250       260
                  ....*....|....*....|....*..
gi 1704602876 248 KDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd13976   216 RCLIRSLLRREPSERLTAEDILLHPWL 242
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
28-285 5.07e-22

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: 96.23  E-value: 5.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKIL-----LDRPKAR--NEVRLHMMCATHPNIVQIIEVFANSVQfphessprarLLI 100
Cdd:cd05601     9 IGRGHFGEVQVVKEKATGDIYAMKVLkksetLAQEEVSffEEERDIMAKANSPWITKLQYAFQDSEN----------LYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 101 VMEMMEGGELFHRISQHRHFTEKQASQ------------------VTKQDAP----------VKLCDFG-FAKIDQGDLM 151
Cdd:cd05601    79 VMEYHPGGDLLSLLSRYDDIFEESMARfylaelvlaihslhsmgyVHRDIKPenilidrtghIKLADFGsAAKLSSDKTV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 152 T---PQFTPYYVAPQVLEAQRRHQKEksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDMRRKi 228
Cdd:cd05601   159 TskmPVGTPDYIAPEVLTSMNGGSKG------------TYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMNFK- 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1704602876 229 mtGSFEFPEEewSQISEMAKDVVRKLLkVKPEERLTIEGVLDHPWLNSTE--ALDNVLP 285
Cdd:cd05601   226 --KFLKFPED--PKVSESAVDLIKGLL-TDAKERLGYEGLCCHPFFSGIDwnNLRQTVP 279
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
17-274 1.48e-21

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: 93.48  E-value: 1.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  17 LEEYSINwtQKLGAGISGPVRVCVKKSTQERFALKILLDRP--------KARNEVRL--HMmcaTHPNIVQIIEVFansv 86
Cdd:cd14116     4 LEDFEIG--RPLGKGKFGNVYLAREKQSKFILALKVLFKAQlekagvehQLRREVEIqsHL---RHPNILRLYGYF---- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  87 qfpHESsprARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQDA---------------------------PVKLCD 139
Cdd:cd14116    75 ---HDA---TRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELAnalsychskrvihrdikpenlllgsagELKIAD 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 140 FGFAkidqgdLMTPQF-------TPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFY 212
Cdd:cd14116   149 FGWS------VHAPSSrrttlcgTLDYLPPEMIEGR------------------MHDEKVDLWSLGVLCYEFLVGKPPFE 204
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1704602876 213 SKHHSRTIpkdmrRKIMTGSFEFPeeewSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14116   205 ANTYQETY-----KRISRVEFTFP----DFVTEGARDLISRLLKHNPSQRPMLREVLEHPWI 257
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
27-279 2.74e-21

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: 92.65  E-value: 2.74e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  27 KLGAGISGPVRVCVKKSTQERFALKI--LLDRPKARNEVR--LHMMCAT-HPNIVQIIEVFANSvqfphessprARLLIV 101
Cdd:cd06623     8 VLGQGSSGVVYKVRHKPTGKIYALKKihVDGDEEFRKQLLreLKTLRSCeSPYVVKCYGAFYKE----------GEISIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 102 MEMMEGGELFHRISQHRHFTEKQASQVTKQ----------------------------DAPVKLCDFGFAK-IDQGDLMT 152
Cdd:cd06623    78 LEYMDGGSLADLLKKVGKIPEPVLAYIARQilkgldylhtkrhiihrdikpsnllinsKGEVKIADFGISKvLENTLDQC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 153 PQF--TPYYVAPQVLEAQrrhqkeksgiiptsptPYTYNksCDLWSLGVIIYVMLCGYPPFYSKHHSRTIpkDMRRKIMT 230
Cdd:cd06623   158 NTFvgTVTYMSPERIQGE----------------SYSYA--ADIWSLGLTLLECALGKFPFLPPGQPSFF--ELMQAICD 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1704602876 231 GSFEFPEEEwsQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEA 279
Cdd:cd06623   218 GPPPSLPAE--EFSPEFRDFISACLQKDPKKRPSAAELLQHPFIKKADN 264
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
26-274 3.95e-21

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: 92.32  E-value: 3.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKILLDRPK-------ARNEVRLhMMCATHPNIVQIIEVFANSvqfphessprARL 98
Cdd:cd14161     9 ETLGKGTYGRVKKARDSSGRLVAIKSIRKDRIKdeqdllhIRREIEI-MSSLNHPHIISVYEVFENS----------SKI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  99 LIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ---------------------------DAPVKLCDFGFAKIDQGD-- 149
Cdd:cd14161    78 VIVMEYASRGDLYDYISERQRLSELEARHFFRQivsavhychangivhrdlklenilldaNGNIKIADFGLSNLYNQDkf 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 150 LMTPQFTPYYVAPQVLEAQrrhqkeksgiiptsptPYTyNKSCDLWSLGVIIYVMLCGYPPFYSKHHsrtipKDMRRKIM 229
Cdd:cd14161   158 LQTYCGSPLYASPEIVNGR----------------PYI-GPEVDSWSLGVLLYILVHGTMPFDGHDY-----KILVKQIS 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1704602876 230 TGSFEFPeeewSQISEmAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14161   216 SGAYREP----TKPSD-ACGLIRWLLMVNPERRATLEDVASHWWV 255
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
31-276 5.14e-21

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: 92.16  E-value: 5.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  31 GISGPVRVCVKKSTQERFALKILldrPKA-----------RNEVRLHMMCATHPNIVQIIEVFANsvqfphesspRARLL 99
Cdd:cd05611     7 GAFGSVYLAKKRSTGDYFAIKVL---KKSdmiaknqvtnvKAERAIMMIQGESPYVAKLYYSFQS----------KDYLY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMEGG----------------------------ELFH-RISQHRHFteKQASQVTKQDAPVKLCDFGFAKIDQGDL 150
Cdd:cd05611    74 LVMEYLNGGdcasliktlgglpedwakqyiaevvlgvEDLHqRGIIHRDI--KPENLLIDQTGHLKLTDFGLSRNGLEKR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 151 MTPQF--TPYYVAPQVLEAQRRhqkeksgiiptsptpytyNKSCDLWSLGVIIYVMLCGYPPFyskhHSRTiPKDMRRKI 228
Cdd:cd05611   152 HNKKFvgTPDYLAPETILGVGD------------------DKMSDWWSLGCVIFEFLFGYPPF----HAET-PDAVFDNI 208
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1704602876 229 MTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERL---TIEGVLDHPWLNS 276
Cdd:cd05611   209 LSRRINWPEEVKEFCSPEAVDLINRLLCMDPAKRLganGYQEIKSHPFFKS 259
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
20-274 8.55e-21

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: 91.30  E-value: 8.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  20 YSINWTqkLGAGISGPVRVCVKKSTQERFALKIL----LDR---PKARNEVRLhMMCATHPNIVQIIEVFANSvqfphes 92
Cdd:cd14071     2 YDIERT--IGKGNFAVVKLARHRITKTEVAIKIIdksqLDEenlKKIYREVQI-MKMLNHPHIIKLYQVMETK------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  93 sprARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ---------------------------DAPVKLCDFGFAKI 145
Cdd:cd14071    72 ---DMLYLVTEYASNGEIFDYLAQHGRMSEKEARKKFWQilsaveychkrhivhrdlkaenllldaNMNIKIADFGFSNF 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 146 DQGD--LMTPQFTPYYVAPQVLEAQRRHQKEksgiiptsptpytynksCDLWSLGVIIYVMLCGYPPFyskhHSRTIPKd 223
Cdd:cd14071   149 FKPGelLKTWCGSPPYAAPEVFEGKEYEGPQ-----------------LDIWSLGVVLYVLVCGALPF----DGSTLQT- 206
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1704602876 224 MRRKIMTGSFEFPeeewSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14071   207 LRDRVLSGRFRIP----FFMSTDCEHLIRRMLVLDPSKRLTIEQIKKHKWM 253
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
28-276 9.59e-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: 91.73  E-value: 9.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILLDRPKAR--------NEVRLhMMCATHPNIVQIievFANSvqfpHESSpraRLL 99
Cdd:cd05612     9 IGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRlkqeqhvhNEKRV-LKEVSHPFIIRL---FWTE----HDQR---FLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMEGGELFHRISQHRHFTE---------------------------KQASQVTKQDAPVKLCDFGFAKIDQGDLMT 152
Cdd:cd05612    78 MLMEYVPGGELFSYLRNSGRFSNstglfyaseivcaleylhskeivyrdlKPENILLDKEGHIKLTDFGFAKKLRDRTWT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 153 PQFTPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHhsrtiPKDMRRKIMTGS 232
Cdd:cd05612   158 LCGTPEYLAPEVIQSK------------------GHNKAVDWWALGILIYEMLVGYPPFFDDN-----PFGIYEKILAGK 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1704602876 233 FEFPEeewsQISEMAKDVVRKLLKVKPEERL-----TIEGVLDHPWLNS 276
Cdd:cd05612   215 LEFPR----HLDLYAKDLIKKLLVVDRTRRLgnmknGADDVKNHRWFKS 259
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
27-274 5.57e-20

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: 88.83  E-value: 5.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  27 KLGAGISGPVRVCVKKSTQERFALKILLDRP----KARNEVRL--HMMCAT-HPNIVQIIEVFansvqFPHESSpraRLL 99
Cdd:cd05118     6 KIGEGAFGTVWLARDKVTGEKVAIKKIKNDFrhpkAALREIKLlkHLNDVEgHPNIVKLLDVF-----EHRGGN---HLC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMeGGELFHRI-SQHRHFTEKQASQVTKQ----------------------------DAPVKLCDFGFAKIDQGDL 150
Cdd:cd05118    78 LVFELM-GMNLYELIkDYPRGLPLDLIKSYLYQllqaldflhsngiihrdlkpenilinleLGQLKLADFGLARSFTSPP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 151 MTPQFTP-YYVAPQVLEAQRRhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKdMRRKIM 229
Cdd:cd05118   157 YTPYVATrWYRAPEVLLGAKP-----------------YGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAK-IVRLLG 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1704602876 230 TgsfefpeeewsqisEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd05118   219 T--------------PEALDLLSKMLKYDPAKRITASQALAHPYF 249
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
28-263 6.10e-20

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: 90.07  E-value: 6.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILLDRP-KARNEVRlHMMC--------ATHPNIVQIIEVFANsvqfphesspRARL 98
Cdd:cd05575     3 IGKGSFGKVLLARHKAEGKLYAVKVLQKKAiLKRNEVK-HIMAernvllknVKHPFLVGLHYSFQT----------KDKL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  99 LIVMEMMEGGELFHRISQHRHFTEKQAS----------------QVTKQD-AP----------VKLCDFGFAK--IDQGD 149
Cdd:cd05575    72 YFVLDYVNGGELFFHLQRERHFPEPRARfyaaeiasalgylhslNIIYRDlKPenilldsqghVVLTDFGLCKegIEPSD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 150 lMTPQF--TPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSrtipkDMRRK 227
Cdd:cd05575   152 -TTSTFcgTPEYLAPEVLRKQ------------------PYDRTVDWWCLGAVLYEMLYGLPPFYSRDTA-----EMYDN 207
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1704602876 228 IMTGSFEFPEeewsQISEMAKDVVRKLLKVKPEERL 263
Cdd:cd05575   208 ILHKPLRLRT----NVSPSARDLLEGLLQKDRTKRL 239
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
28-276 1.06e-19

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: 89.17  E-value: 1.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALK-ILLDRPKARNEVRlHMMcATHPNIVQIIEVFANSVQFPHESspRARLLIVMEMME 106
Cdd:cd05585     2 IGKGSFGKVMQVRKKDTSRIYALKtIRKAHIVSRSEVT-HTL-AERTVLAQVDCPFIVPLKFSFQS--PEKLYLVLAFIN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 107 GGELFHRISQHRHFTEKQASQVTKQ---------------------------DAPVKLCDFGFAKID-QGDLMTPQF--T 156
Cdd:cd05585    78 GGELFHHLQREGRFDLSRARFYTAEllcaleclhkfnviyrdlkpenilldyTGHIALCDFGLCKLNmKDDDKTNTFcgT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 157 PYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHhsrtIPKdMRRKIMTGSFEFP 236
Cdd:cd05585   158 PEYLAPELLLGH------------------GYTKAVDWWTLGVLLYEMLTGLPPFYDEN----TNE-MYRKILQEPLRFP 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1704602876 237 EeewsQISEMAKDVVRKLLKVKPEERLTIEG---VLDHPWLNS 276
Cdd:cd05585   215 D----GFDRDAKDLLIGLLNRDPTKRLGYNGaqeIKNHPFFDQ 253
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
20-274 3.93e-19

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: 86.76  E-value: 3.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  20 YSINWTqkLGAGISGPVRVCVKKSTQERFALKILlDRPKARNEV-------------RLHmmcatHPNIVQIIEVFANSv 86
Cdd:cd14165     3 YILGIN--LGEGSYAKVKSAYSERLKCNVAIKII-DKKKAPDDFvekflpreleilaRLN-----HKSIIKTYEIFETS- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  87 qfphesspRARLLIVMEMMEGGEL------------------FHRISQ-----------HRHFteKQASQVTKQDAPVKL 137
Cdd:cd14165    74 --------DGKVYIVMELGVQGDLlefiklrgalpedvarkmFHQLSSaikycheldivHRDL--KCENLLLDKDFNIKL 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 138 CDFGFAKIDQGD-----LMTPQF--TPYYVAPQVLEAqrrhqkeksgiIPTSPTPYtynkscDLWSLGVIIYVMLCGYPP 210
Cdd:cd14165   144 TDFGFSKRCLRDengriVLSKTFcgSAAYAAPEVLQG-----------IPYDPRIY------DIWSLGVILYIMVCGSMP 206
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1704602876 211 FYSKHhsrtiPKDMRRKIMTGSFEFPEEEwSQISEMaKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14165   207 YDDSN-----VKKMLKIQKEHRVRFPRSK-NLTSEC-KDLIYRLLQPDVSQRLCIDEVLSHPWL 263
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
28-273 5.52e-19

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: 87.46  E-value: 5.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVrVCVKKSTQER----FALKILLDRPKARNEV--------RLHMMCATHPNIVQIIEVFANSvqfphesspr 95
Cdd:cd05584     4 LGKGGYGKV-FQVRKTTGSDkgkiFAMKVLKKASIVRNQKdtahtkaeRNILEAVKHPFIVDLHYAFQTG---------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  96 ARLLIVMEMMEGGELFHRISQHRHFTEKQAS----QVT-----------------------KQDAPVKLCDFGFAKID-Q 147
Cdd:cd05584    73 GKLYLILEYLSGGELFMHLEREGIFMEDTACfylaEITlalghlhslgiiyrdlkpenillDAQGHVKLTDFGLCKESiH 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 148 GDLMTPQF--TPYYVAPQVLEaqrrhqkeKSGiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIpkdmr 225
Cdd:cd05584   153 DGTVTHTFcgTIEYMAPEILT--------RSG----------HGKAVDWWSLGALMYDMLTGAPPFTAENRKKTI----- 209
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1704602876 226 RKIMTGSFEFPeeewSQISEMAKDVVRKLLKVKPEERL-----TIEGVLDHPW 273
Cdd:cd05584   210 DKILKGKLNLP----PYLTNEARDLLKKLLKRNVSSRLgsgpgDAEEIKAHPF 258
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
26-272 1.61e-18

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: 84.90  E-value: 1.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALK-----ILLDRPKAR--NEVRLhMMCATHPNIVQIIEVFANSvqfphessPRARL 98
Cdd:cd08217     6 ETIGKGSFGTVRKVRRKSDGKILVWKeidygKMSEKEKQQlvSEVNI-LRELKHPNIVRYYDRIVDR--------ANTTL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  99 LIVMEMMEGGELFHRISQHR----HFTEKQASQVTKQ--------------------------------DAPVKLCDFGF 142
Cdd:cd08217    77 YIVMEYCEGGDLAQLIKKCKkenqYIPEEFIWKIFTQlllalyechnrsvgggkilhrdlkpanifldsDNNVKLGDFGL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 143 AK-IDQGDLMTPQF--TPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHsrt 219
Cdd:cd08217   157 ARvLSHDSSFAKTYvgTPYYMSPELLNEQS------------------YDEKSDIWSLGCLIYELCALHPPFQAANQ--- 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1704602876 220 ipKDMRRKIMTGSFEF-PeeewSQISEMAKDVVRKLLKVKPEERLTIEGVLDHP 272
Cdd:cd08217   216 --LELAKKIKEGKFPRiP----SRYSSELNEVIKSMLNVDPDKRPSVEELLQLP 263
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
26-274 4.35e-18

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: 83.59  E-value: 4.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALK------ILLD---RPKARNEVRL--HMM----CATHPNIVQIIEVFANSVQFph 90
Cdd:cd14004     6 KEMGEGAYGQVNLAIYKSKGKEVVIKfifkerILVDtwvRDRKLGTVPLeiHILdtlnKRSHPNIVKLLDFFEDDEFY-- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  91 essprarlLIVMEMM-EGGELFHRISQHRHFTEKQASQVTKQ---------------------------DAPVKLCDFGF 142
Cdd:cd14004    84 --------YLVMEKHgSGMDLFDFIERKPNMDEKEAKYIFRQvadavkhlhdqgivhrdikdenvildgNGTIKLIDFGS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 143 AK-IDQGDLMTPQFTPYYVAPQVLEAQRRHQKEKsgiiptsptpytynkscDLWSLGVIIYVMLCGYPPFYSKHHsrtip 221
Cdd:cd14004   156 AAyIKSGPFDTFVGTIDYAAPEVLRGNPYGGKEQ-----------------DIWALGVLLYTLVFKENPFYNIEE----- 213
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1704602876 222 kdmrrkIMTGSFEFPEEEwsqiSEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14004   214 ------ILEADLRIPYAV----SEDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
26-274 5.03e-18

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: 83.76  E-value: 5.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKIL----LDRPKARNEVRLhMMCATHPNIVQIIEVFANsvqfpHEsspraRLLIV 101
Cdd:cd14104     6 EELGRGQFGIVHRCVETSSKKTYMAKFVkvkgADQVLVKKEISI-LNIARHRNILRLHESFES-----HE-----ELVMI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 102 MEMMEGGELFHRISQHR-HFTEKQASQVTKQ-----------------------------DAPVKLCDFGFAK-IDQGDL 150
Cdd:cd14104    75 FEFISGVDIFERITTARfELNEREIVSYVRQvcealeflhsknighfdirpeniiyctrrGSYIKIIEFGQSRqLKPGDK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 151 MTPQFT-PYYVAPQVleaqrrHQKEKSGiiptsptpytynKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIpkdmrRKIM 229
Cdd:cd14104   155 FRLQYTsAEFYAPEV------HQHESVS------------TATDMWSLGCLVYVLLSGINPFEAETNQQTI-----ENIR 211
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1704602876 230 TGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14104   212 NAEYAFDDEAFKNISIEALDFVDRLLVKERKSRMTAQEALNHPWL 256
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
26-273 5.27e-18

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: 83.11  E-value: 5.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAG----------ISGPVRV----CVKKSTQERFALKILLDRPKARNEVRlhmmcatHPNIVQIIEVFANSvqfphe 91
Cdd:cd14121     1 EKLGSGtyatvykayrKSGAREVvavkCVSKSSLNKASTENLLTEIELLKKLK-------HPHIVELKDFQWDE------ 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  92 ssprARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQDA----------------------------PV-KLCDFGF 142
Cdd:cd14121    68 ----EHIYLIMEYCSGGDLSRFIRSRRTLPESTVRRFLQQLAsalqflrehnishmdlkpqnlllssrynPVlKLADFGF 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 143 AK-IDQGDLMTP-QFTPYYVAPQVLeaqRRHQkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFyskhHSRTI 220
Cdd:cd14121   144 AQhLKPNDEAHSlRGSPLYMAPEMI---LKKK---------------YDARVDLWSVGVILYECLFGRAPF----ASRSF 201
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1704602876 221 pKDMRRKIMTGS-FEFPEEewSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPW 273
Cdd:cd14121   202 -EELEEKIRSSKpIEIPTR--PELSADCRDLLLRLLQRDPDRRISFEEFFAHPF 252
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
58-274 6.26e-18

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: 82.99  E-value: 6.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  58 KARNEVRLHMMCaTHPNIVQIIEVFANSvqfphessprARLLIVMEMMEGGELfHRISQHRH--FTEKQASQVTKQ---- 131
Cdd:cd14186    47 RVRNEVEIHCQL-KHPSILELYNYFEDS----------NYVYLVLEMCHNGEM-SRYLKNRKkpFTEDEARHFMHQivtg 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 132 -----------------------DAPVKLCDFGFA---KIDQGDLMTPQFTPYYVAPQVLeaqrrhqkeksgiiptspTP 185
Cdd:cd14186   115 mlylhshgilhrdltlsnllltrNMNIKIADFGLAtqlKMPHEKHFTMCGTPNYISPEIA------------------TR 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 186 YTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIpkdmrRKIMTGSFEFPeeewSQISEMAKDVVRKLLKVKPEERLTI 265
Cdd:cd14186   177 SAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTL-----NKVVLADYEMP----AFLSREAQDLIHQLLRKNPADRLSL 247

                  ....*....
gi 1704602876 266 EGVLDHPWL 274
Cdd:cd14186   248 SSVLDHPFM 256
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
27-274 7.82e-18

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: 82.66  E-value: 7.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  27 KLGAGISGPVRVCVKKSTQERFALK--ILLDRPKA-----RNEVRLhMMCATHPNIVQIIEVFansvqfphESspRARLL 99
Cdd:cd06627     7 LIGRGAFGSVYKGLNLNTGEFVAIKqiSLEKIPKSdlksvMGEIDL-LKKLNHPNIVKYIGSV--------KT--KDSLY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMEGGELFHRISQHRHFTEKQA----SQVTK-----------------------QDAPVKLCDFGFA-KID--QGD 149
Cdd:cd06627    76 IILEYVENGSLASIIKKFGKFPESLVavyiYQVLEglaylheqgvihrdikganilttKDGLVKLADFGVAtKLNevEKD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 150 LMTPQFTPYYVAPQVLEAQrrhqkeksgiiptsptPYTynKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTipkdMRRKIM 229
Cdd:cd06627   156 ENSVVGTPYWMAPEVIEMS----------------GVT--TASDIWSVGCTVIELLTGNPPYYDLQPMAA----LFRIVQ 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1704602876 230 TGSFEFPEEewsqISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd06627   214 DDHPPLPEN----ISPELRDFLLQCFQKDPTLRPSAKELLKHPWL 254
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
24-274 9.14e-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: 82.74  E-value: 9.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  24 WTQ--KLGAGISGPVRVCVKKSTQERFALKILL---DRPKARNEVRLHMMC---ATHPNIVQI--IEVfansvqfpHess 93
Cdd:cd06626     2 WQRgnKIGEGTFGKVYTAVNLDTGELMAMKEIRfqdNDPKTIKEIADEMKVlegLDHPNLVRYygVEV--------H--- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  94 pRARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ---------------------------DAPVKLCDFGFAKI- 145
Cdd:cd06626    71 -REEVYIFMEYCQEGTLEELLRHGRILDEAVIRVYTLQlleglaylhengivhrdikpanifldsNGLIKLGDFGSAVKl 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 146 -DQGDLMTP------QFTPYYVAPQVLEAQRRHQKEKSgiiptsptpytynksCDLWSLGVIIYVMLCGYPPFYSKHHSR 218
Cdd:cd06626   150 kNNTTTMAPgevnslVGTPAYMAPEVITGNKGEGHGRA---------------ADIWSLGCVVLEMATGKRPWSELDNEW 214
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1704602876 219 TIpkdMRRKIMTGSFEFPEEEwsQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd06626   215 AI---MYHVGMGHKPPIPDSL--QLSPEGKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
28-263 9.82e-18

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: 83.42  E-value: 9.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILL--------DRPKARNEVRLHMMCATHPNIVQIIEVFansvQFPHesspraRLL 99
Cdd:cd05570     3 LGKGSFGKVMLAERKKTDELYAIKVLKkeviieddDVECTMTEKRVLALANRHPFLTGLHACF----QTED------RLY 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMEGGELFHRISQHRHFTEKQ----ASQVT----------------KQD-------APVKLCDFGFAKID-QGDLM 151
Cdd:cd05570    73 FVMEYVNGGDLMFHIQRARRFTEERarfyAAEIClalqflhergiiyrdlKLDnvlldaeGHIKIADFGMCKEGiWGGNT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 152 TPQF--TPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFyskhHSRTiPKDMRRKIM 229
Cdd:cd05570   153 TSTFcgTPDYIAPEILREQD------------------YGFSVDWWALGVLLYEMLAGQSPF----EGDD-EDELFEAIL 209
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1704602876 230 TGSFEFPeeewSQISEMAKDVVRKLLKVKPEERL 263
Cdd:cd05570   210 NDEVLYP----RWLSREAVSILKGLLTKDPARRL 239
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
28-285 1.14e-17

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: 82.60  E-value: 1.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILLDRPKARN----------EVRLHMmcaTHPNIVQIIEVFANsvqfphesspRAR 97
Cdd:cd14117    14 LGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEgvehqlrreiEIQSHL---RHPNILRLYNYFHD----------RKR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  98 LLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQDA---------------------------PVKLCDFGFAkidqgdL 150
Cdd:cd14117    81 IYLILEYAPRGELYKELQKHGRFDEQRTATFMEELAdalhychekkvihrdikpenllmgykgELKIADFGWS------V 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 151 MTPQF-------TPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTipkd 223
Cdd:cd14117   155 HAPSLrrrtmcgTLDYLPPEMIEGR------------------THDEKVDLWCIGVLCYELLVGMPPFESASHTET---- 212
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1704602876 224 mRRKIMTGSFEFPeeewSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEAldNVLP 285
Cdd:cd14117   213 -YRRIVKVDLKFP----PFLSDGSRDLISKLLRYHPSERLPLKGVMEHPWVKANSR--RVLP 267
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
28-274 2.20e-17

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: 81.58  E-value: 2.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQER--FALKILldRPKARNEVRLHMM--CAT---------HPNIVQIIEVFAnsvqfphesSP 94
Cdd:cd13994     1 IGKGATSVVRIVTKKNPRSGvlYAVKEY--RRRDDESKRKDYVkrLTSeyiissklhHPNIVKVLDLCQ---------DL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  95 RARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ---------------------------DAPVKLCDFGFAKI-- 145
Cdd:cd13994    70 HGKWCLVMEYCPGGDLFTLIEKADSLSLEEKDCFFKQilrgvaylhshgiahrdlkpenilldeDGVLKLTDFGTAEVfg 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 146 DQGDLMTPQF-----TPYYVAPQVLeaqrrhqkeksgiiptspTPYTYN-KSCDLWSLGVIIYVMLCGYPPFYSKHHSrt 219
Cdd:cd13994   150 MPAEKESPMSaglcgSEPYMAPEVF------------------TSGSYDgRAVDVWSCGIVLFALFTGRFPWRSAKKS-- 209
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1704602876 220 ipkDMRRKIMTGSFEFPEEEWSQISEM----AKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd13994   210 ---DSAYKAYEKSGDFTNGPYEPIENLlpseCRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
135-271 3.42e-17

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: 81.68  E-value: 3.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 135 VKLCDFGFAK--IDQGDLMTPQF-TPYYVAPQVLeaqrrhqkeksgiiptSPTPYTyNKSCDLWSLGVIIYVMLCGYPPF 211
Cdd:cd13974   172 ITITNFCLGKhlVSEDDLLKDQRgSPAYISPDVL----------------SGKPYL-GKPSDMWALGVVLFTMLYGQFPF 234
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 212 YSkhhsrTIPKDMRRKIMTGSFEFPEEewSQISEMAKDVVRKLLKVKPEERLTIEGVLDH 271
Cdd:cd13974   235 YD-----SIPQELFRKIKAAEYTIPED--GRVSENTVCLIRKLLVLNPQKRLTASEVLDS 287
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
23-263 6.15e-17

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: 81.67  E-value: 6.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  23 NWTQKLGAGISGPVRVCVKKSTQERFALKILLDRPK-ARNEVRlHMMCAT-------HPnivqiievFANSVQFPHESsp 94
Cdd:cd05593    18 DYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIiAKDEVA-HTLTESrvlkntrHP--------FLTSLKYSFQT-- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  95 RARLLIVMEMMEGGELFHRISQHRHFTE---------------------------KQASQVTKQDAPVKLCDFGFAK--- 144
Cdd:cd05593    87 KDRLCFVMEYVNGGELFFHLSRERVFSEdrtrfygaeivsaldylhsgkivyrdlKLENLMLDKDGHIKITDFGLCKegi 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 145 IDQGDLMTPQFTPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRtipkdM 224
Cdd:cd05593   167 TDAATMKTFCGTPEYLAPEVLEDN------------------DYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEK-----L 223
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1704602876 225 RRKIMTGSFEFPEeewsQISEMAKDVVRKLLKVKPEERL 263
Cdd:cd05593   224 FELILMEDIKFPR----TLSADAKSLLSGLLIKDPNKRL 258
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
72-273 6.64e-17

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: 80.48  E-value: 6.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  72 HPNIVQIIEVFANsvqfPHESSprarLLIVMEMMEGGELFHRISQH--------RHFTE------------------KQA 125
Cdd:cd14118    73 HPNVVKLVEVLDD----PNEDN----LYMVFELVDKGAVMEVPTDNplseetarSYFRDivlgieylhyqkiihrdiKPS 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 126 SQVTKQDAPVKLCDFGFAKIDQGD---LMTPQFTPYYVAPQVLEAQRrhqKEKSGiiptsptpytynKSCDLWSLGVIIY 202
Cdd:cd14118   145 NLLLGDDGHVKIADFGVSNEFEGDdalLSSTAGTPAFMAPEALSESR---KKFSG------------KALDIWAMGVTLY 209
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1704602876 203 VMLCGYPPFYSKHhsrtiPKDMRRKIMTGSFEFPEEewSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPW 273
Cdd:cd14118   210 CFVFGRCPFEDDH-----ILGLHEKIKTDPVVFPDD--PVVSEQLKDLILRMLDKNPSERITLPEIKEHPW 273
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
72-274 6.89e-17

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: 80.03  E-value: 6.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  72 HPNIVQIIEVFansvqfphESSprARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ-------------------- 131
Cdd:cd14162    59 HPNLICFYEAI--------ETT--SRVYIIMELAENGDLLDYIRKNGALPEPQARRWFRQlvagveychskgvvhrdlkc 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 132 -------DAPVKLCDFGFAKidqGDLMTPQFTPY----------YVAPQVLEAqrrhqkeksgiIPTSPTpytynkSCDL 194
Cdd:cd14162   129 enllldkNNNLKITDFGFAR---GVMKTKDGKPKlsetycgsyaYASPEILRG-----------IPYDPF------LSDI 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 195 WSLGVIIYVMLCGYPPFYSKHHsRTIPKDMRRKIMtgsfeFPEEEwsQISEMAKDVVRKLLkVKPEERLTIEGVLDHPWL 274
Cdd:cd14162   189 WSMGVVLYTMVYGRLPFDDSNL-KVLLKQVQRRVV-----FPKNP--TVSEECKDLILRML-SPVKKRITIEEIKRDPWF 259
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
62-274 1.02e-16

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: 79.59  E-value: 1.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  62 EVRLHMMCAT--HPNIVQIIEVFANSVQFphessprarlLIVMEMMEGGE-LFHRISQHRHFTEKQASQVTKQ------- 131
Cdd:cd14005    53 EIALLLKASKpgVPGVIRLLDWYERPDGF----------LLIMERPEPCQdLFDFITERGALSENLARIIFRQvveavrh 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 132 ---------------------DAPVKLCDFGF-AKIDQGDLMTPQFTPYYVAPQVLEAQRRHqkeksgiiptsPTPYTyn 189
Cdd:cd14005   123 chqrgvlhrdikdenllinlrTGEVKLIDFGCgALLKDSVYTDFDGTRVYSPPEWIRHGRYH-----------GRPAT-- 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 190 kscdLWSLGVIIYVMLCGYPPFYSkhhsrtipkdmRRKIMTGSFEFpeeeWSQISEMAKDVVRKLLKVKPEERLTIEGVL 269
Cdd:cd14005   190 ----VWSLGILLYDMLCGDIPFEN-----------DEQILRGNVLF----RPRLSKECCDLISRCLQFDPSKRPSLEQIL 250

                  ....*
gi 1704602876 270 DHPWL 274
Cdd:cd14005   251 SHPWF 255
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
15-289 1.03e-16

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


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 80.41  E-value: 1.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  15 SILEEYSinwtqKLGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLH----MMCATHPNIVQIIEVFANSVQfph 90
Cdd:cd06659    21 QLLENYV-----KIGEGSTGVVCIAREKHSGRQVAVKMMDLRKQQRRELLFNevviMRDYQHPNVVEMYKSYLVGEE--- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  91 essprarLLIVMEMMEGGELFHRISQHRhFTEKQASQV--------------------TKQDAP-------VKLCDFGFA 143
Cdd:cd06659    93 -------LWVLMEYLQGGALTDIVSQTR-LNEEQIATVceavlqalaylhsqgvihrdIKSDSIlltldgrVKLSDFGFC 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 144 KIDQGDLMTPQF---TPYYVAPQVLeaqrrhqkeksgiiptSPTPYTynKSCDLWSLGVIIYVMLCGYPPFYSKhhsrTI 220
Cdd:cd06659   165 AQISKDVPKRKSlvgTPYWMAPEVI----------------SRCPYG--TEVDIWSLGIMVIEMVDGEPPYFSD----SP 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1704602876 221 PKDMRRkiMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEALDNVLPSAQL 289
Cdd:cd06659   223 VQAMKR--LRDSPPPKLKNSHKASPVLRDFLERMLVRDPQERATAQELLDHPFLLQTGLPECLVPLIQQ 289
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
41-273 1.18e-16

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: 79.65  E-value: 1.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  41 KKSTQERFALKIL--LDRPKARNEVRL-HMMcaTHPNIVQIIEVFansvqfphESSprARLLIVMEMMEGGELFHRISQH 117
Cdd:cd14010    21 RKGTIEFVAIKCVdkSKRPEVLNEVRLtHEL--KHPNVLKFYEWY--------ETS--NHLWLVVEYCTGGDLETLLRQD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 118 RHFTEK--------------------------QASQVTkQDAP--VKLCDFGFAKIDQGDL------------------- 150
Cdd:cd14010    89 GNLPESsvrkfgrdlvrglhyihskgiiycdlKPSNIL-LDGNgtLKLSDFGLARREGEILkelfgqfsdegnvnkvskk 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 151 MTPQFTPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKhhSRTipkDMRRKIMT 230
Cdd:cd14010   168 QAKRGTPYYMAPELFQGG------------------VHSFASDLWALGCVLYEMFTGKPPFVAE--SFT---ELVEKILN 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1704602876 231 GSFEFPEEEWS-QISEMAKDVVRKLLKVKPEERLTIEGVLDHP-W 273
Cdd:cd14010   225 EDPPPPPPKVSsKPSPDFKSLLKGLLEKDPAKRLSWDELVKHPfW 269
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
28-263 1.97e-16

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: 80.46  E-value: 1.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILLDRP-KARNEVRlHMMC-------ATHPnivqiievFANSVQFPHESspRARLL 99
Cdd:cd05594    33 LGKGTFGKVILVKEKATGRYYAMKILKKEViVAKDEVA-HTLTenrvlqnSRHP--------FLTALKYSFQT--HDRLC 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMEGGELFHRISQHRHFTEKQA----------------------------SQVTKQDAPVKLCDFGFAK--IDQGD 149
Cdd:cd05594   102 FVMEYANGGELFFHLSRERVFSEDRArfygaeivsaldylhseknvvyrdlkleNLMLDKDGHIKITDFGLCKegIKDGA 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 150 LM-TPQFTPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRtipkdMRRKI 228
Cdd:cd05594   182 TMkTFCGTPEYLAPEVLEDN------------------DYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEK-----LFELI 238
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1704602876 229 MTGSFEFPEeewsQISEMAKDVVRKLLKVKPEERL 263
Cdd:cd05594   239 LMEEIRFPR----TLSPEAKSLLSGLLKKDPKQRL 269
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
39-266 2.16e-16

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: 78.93  E-value: 2.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  39 CVKKSTQERFALKILLDRPKARnEVRLHMMCATHPNIVQIIEVFANSVQfphessprarLLIVMEMMEGGELFHRISQHR 118
Cdd:cd13993    32 CLYKSGPNSKDGNDFQKLPQLR-EIDLHRRVSRHPNIITLHDVFETEVA----------IYIVLEYCPNGDLFEAITENR 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 119 HFTEKQAS------------------------------QVTKQDAPVKLCDFGFAKIDQgdlMTPQF---TPYYVAPQVL 165
Cdd:cd13993   101 IYVGKTELiknvflqlidavkhchslgiyhrdikpeniLLSQDEGTVKLCDFGLATTEK---ISMDFgvgSEFYMAPECF 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 166 EaqrrhqkEKSGIIPTSPTpytynKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDMRRKIMTgsfefpeeEWSQISE 245
Cdd:cd13993   178 D-------EVGRSLKGYPC-----AAGDIWSLGIILLNLTFGRNPWKIASESDPIFYDYYLNSPN--------LFDVILP 237
                         250       260
                  ....*....|....*....|....
gi 1704602876 246 MAKD---VVRKLLKVKPEERLTIE 266
Cdd:cd13993   238 MSDDfynLLRQIFTVNPNNRILLP 261
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
28-274 2.22e-16

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: 78.33  E-value: 2.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKIL-------LDRPKARNEVRLhMMCATHPNIVQIIEVFANsvqfphesspRARLLI 100
Cdd:cd14072     8 IGKGNFAKVKLARHVLTGREVAIKIIdktqlnpSSLQKLFREVRI-MKILNHPNIVKLFEVIET----------EKTLYL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 101 VMEMMEGGELFHRISQHRHFTEKQASQVTKQ---------------------------DAPVKLCDFGFAK--IDQGDLM 151
Cdd:cd14072    77 VMEYASGGEVFDYLVAHGRMKEKEARAKFRQivsavqychqkrivhrdlkaenllldaDMNIKIADFGFSNefTPGNKLD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 152 TPQFTPYYVAPQVLEAQRRHQKEksgiiptsptpytynksCDLWSLGVIIYVMLCGYPPFYSKHHsrtipKDMRRKIMTG 231
Cdd:cd14072   157 TFCGSPPYAAPELFQGKKYDGPE-----------------VDVWSLGVILYTLVSGSLPFDGQNL-----KELRERVLRG 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1704602876 232 SFEFPeeewSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14072   215 KYRIP----FYMSTDCENLLKKFLVLNPSKRGTLEQIMKDRWM 253
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
24-274 2.43e-16

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: 78.60  E-value: 2.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  24 WT--QKLGAGISGPVRVCVKKSTQERFALK--ILLDRPKARNEV--RLHMMCA-----THPNIVQIIEVfansvqfpheS 92
Cdd:cd06632     2 WQkgQLLGSGSFGSVYEGFNGDTGDFFAVKevSLVDDDKKSRESvkQLEQEIAllsklRHPNIVQYYGT----------E 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  93 SPRARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ---------------------------DAPVKLCDFGFAKI 145
Cdd:cd06632    72 REEDNLYIFLEYVPGGSIHKLLQRYGAFEEPVIRLYTRQilsglaylhsrntvhrdikganilvdtNGVVKLADFGMAKH 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 146 DQGDLMTPQF--TPYYVAPQVLEAQRrhqkeksgiiptspTPYTYnkSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKD 223
Cdd:cd06632   152 VEAFSFAKSFkgSPYWMAPEVIMQKN--------------SGYGL--AVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKI 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1704602876 224 MRRKIMTgsfEFPEeewsQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd06632   216 GNSGELP---PIPD----HLSPDAKDFIRLCLQRDPEDRPTASQLLEHPFV 259
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
28-273 2.44e-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: 78.46  E-value: 2.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVR------LHMMcatHPNIVQIIEVFansvqfpheSSPrARLLIV 101
Cdd:cd14115     1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMKKKEQAAheaallQHLQ---HPQYITLHDTY---------ESP-TSYILV 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 102 MEMMEGGELFHRISQHRHFTEKQAS----------------QVTKQDAPVKLCDFGFAK-------IDQGDL--MTPQF- 155
Cdd:cd14115    68 LELMDDGRLLDYLMNHDELMEEKVAfyirdimealqylhncRVAHLDIKPENLLIDLRIpvprvklIDLEDAvqISGHRh 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 156 ------TPYYVAPQVLEAqrrhqkeksgiIPTSptpytynKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDMRRkim 229
Cdd:cd14115   148 vhhllgNPEFAAPEVIQG-----------TPVS-------LATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRV--- 206
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1704602876 230 tgSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPW 273
Cdd:cd14115   207 --DFSFPDEYFGDVSQAARDFINVILQEDPRRRPTAATCLQHPW 248
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
26-274 2.63e-16

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: 79.57  E-value: 2.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKILL--------DRPKARNEVRLHMMCATHPNIVQIIEVFansvQFPHesspraR 97
Cdd:cd05590     1 RVLGKGSFGKVMLARLKESGRLYAVKVLKkdvilqddDVECTMTEKRILSLARNHPFLTQLYCCF----QTPD------R 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  98 LLIVMEMMEGGELFHRISQHRHFTEKQA----SQVTK-----------------------QDAPVKLCDFGFAK--IDQG 148
Cdd:cd05590    71 LFFVMEFVNGGDLMFHIQKSRRFDEARArfyaAEITSalmflhdkgiiyrdlkldnvlldHEGHCKLADFGMCKegIFNG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 149 dLMTPQF--TPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSrtipkDMRR 226
Cdd:cd05590   151 -KTTSTFcgTPDYIAPEILQEML------------------YGPSVDWWAMGVLLYEMLCGHAPFEAENED-----DLFE 206
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1704602876 227 KIMTGSFEFPeeewSQISEMAKDVVRKLLKVKPEERLTI------EGVLDHPWL 274
Cdd:cd05590   207 AILNDEVVYP----TWLSQDAVDILKAFMTKNPTMRLGSltlggeEAILRHPFF 256
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
28-274 2.91e-16

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: 78.07  E-value: 2.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILlDRPKAR----------NEV----RLHmmcatHPNIVQIIEVFANsvqfpHESS 93
Cdd:cd14119     1 LGEGSYGKVKEVLDTETLCRRAVKIL-KKRKLRripngeanvkREIqilrRLN-----HRNVIKLVDVLYN-----EEKQ 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  94 praRLLIVMEMMEGGEL-------FHRISQ---HRHFTE------------------KQASQVTKQDAPVKLCDFGFA-- 143
Cdd:cd14119    70 ---KLYMVMEYCVGGLQemldsapDKRLPIwqaHGYFVQlidgleylhsqgiihkdiKPGNLLLTTDGTLKISDFGVAea 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 144 --KIDQGDLM-TPQFTPYYVAPQVLEAQRRHQKEKsgiiptsptpytynksCDLWSLGVIIYVMLCGYPPFYSkhhsrTI 220
Cdd:cd14119   147 ldLFAEDDTCtTSQGSPAFQPPEIANGQDSFSGFK----------------VDIWSAGVTLYNMTTGKYPFEG-----DN 205
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1704602876 221 PKDMRRKIMTGSFEFPEEewsqISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14119   206 IYKLFENIGKGEYTIPDD----VDPDLQDLLRGMLEKDPEKRFTIEQIRQHPWF 255
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
26-274 3.25e-16

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: 78.01  E-value: 3.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKILLDRPKARNEV---RLHMMCATHPNIVQIIEVFansvqfphesSPRARLLIVM 102
Cdd:cd14107     8 EEIGRGTFGFVKRVTHKGNGECCAAKFIPLRSSTRARAfqeRDILARLSHRRLTCLLDQF----------ETRKTLILIL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 103 EMMEGGELFHRISQHRHFTEKQASQVTKQ-----------------------------DAPVKLCDFGFA-KIDQGDLMT 152
Cdd:cd14107    78 ELCSSEELLDRLFLKGVVTEAEVKLYIQQvlegigylhgmnilhldikpdnilmvsptREDIKICDFGFAqEITPSEHQF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 153 PQF-TPYYVAPQvleaqrrhqkeksgIIPTSPTpytyNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIpkdmrRKIMTG 231
Cdd:cd14107   158 SKYgSPEFVAPE--------------IVHQEPV----SAATDIWALGVIAYLSLTCHSPFAGENDRATL-----LNVAEG 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1704602876 232 SFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14107   215 VVSWDTPEITHLSEDAKDFIKRVLQPDPEKRPSASECLSHEWF 257
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
157-274 5.29e-16

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


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 77.38  E-value: 5.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 157 PYYVAPQVLEAQRRHqkekSGiiptsptpytynKSCDLWSLGVIIYVMLCGYPPFYSKHhsrtiPKDMRRKIMTGSFEFP 236
Cdd:cd14022   150 PAYVSPEILNTSGSY----SG------------KAADVWSLGVMLYTMLVGRYPFHDIE-----PSSLFSKIRRGQFNIP 208
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1704602876 237 EeewsQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14022   209 E----TLSPKAKCLIRSILRREPSERLTSQEILDHPWF 242
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
28-272 5.38e-16

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: 78.58  E-value: 5.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILL--------DRPKARNEVRLHMMCATHPNIVQIIEVFANsvqfphesspRARLL 99
Cdd:cd05592     3 LGKGSFGKVMLAELKGTNQYFAIKALKkdvvleddDVECTMIERRVLALASQHPFLTHLFCTFQT----------ESHLF 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMEGGELFHRISQHRHFTEKQA---------------------------SQVTKQDAPVKLCDFGFAKID-QGDLM 151
Cdd:cd05592    73 FVMEYLNGGDLMFHIQQSGRFDEDRArfygaeiicglqflhsrgiiyrdlkldNVLLDREGHIKIADFGMCKENiYGENK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 152 TPQF--TPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSrtipkDMRRKIM 229
Cdd:cd05592   153 ASTFcgTPDYIAPEILKGQK------------------YNQSVDWWSFGVLLYEMLIGQSPFHGEDED-----ELFWSIC 209
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1704602876 230 TGSFEFPeeEWsqISEMAKDVVRKLLKVKPEERLTIEG-----VLDHP 272
Cdd:cd05592   210 NDTPHYP--RW--LTKEAASCLSLLLERNPEKRLGVPEcpagdIRDHP 253
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
26-274 5.68e-16

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: 77.66  E-value: 5.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKI--LLDRPKAR---NEVrLHMMCATHPNIVQIIEVFANSVQfphessprarLLI 100
Cdd:cd06647    13 EKIGQGASGTVYTAIDVATGQEVAIKQmnLQQQPKKEliiNEI-LVMRENKNPNIVNYLDSYLVGDE----------LWV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 101 VMEMMEGGEL--------------------------FHRISQHRHFTEKQASQVTKQDAPVKLCDFGF-AKI--DQGDLM 151
Cdd:cd06647    82 VMEYLAGGSLtdvvtetcmdegqiaavcreclqaleFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQItpEQSKRS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 152 TPQFTPYYVAPQVLeaqrrhqkeksgiiptspTPYTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIpkdmrRKIMT- 230
Cdd:cd06647   162 TMVGTPYWMAPEVV------------------TRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRAL-----YLIATn 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1704602876 231 GSFEFPEEEwsQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd06647   219 GTPELQNPE--KLSAIFRDFLNRCLEMDVEKRGSAKELLQHPFL 260
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
23-273 5.77e-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: 77.40  E-value: 5.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  23 NWTQK--LGAGISGPVRVCVKKSTQERFALK---ILLDRPKARNEVR-----LHMMCA-THPNIVQIievfansvqFPHE 91
Cdd:cd06625     1 NWKQGklLGQGAFGQVYLCYDADTGRELAVKqveIDPINTEASKEVKaleceIQLLKNlQHERIVQY---------YGCL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  92 SSPRaRLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ-------------------------DAP--VKLCDFGFAK 144
Cdd:cd06625    72 QDEK-SLSIFMEYMPGGSVKDEIKAYGALTENVTRKYTRQileglaylhsnmivhrdikganilrDSNgnVKLGDFGASK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 145 -----IDQGDLMTPQFTPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRT 219
Cdd:cd06625   151 rlqtiCSSTGMKSVTGTPYWMSPEVINGE------------------GYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAA 212
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1704602876 220 IpkdmrRKIMTG--SFEFPeeewSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPW 273
Cdd:cd06625   213 I-----FKIATQptNPQLP----PHVSEDARDFLSLIFVRNKKQRPSAEELLSHSF 259
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
28-263 7.00e-16

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: 78.38  E-value: 7.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLHMMcaTHPNIVQIIEV----FANSVQFPHESSprARLLIVME 103
Cdd:cd05586     1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVAHTI--GERNILVRTALdespFIVGLKFSFQTP--TDLYLVTD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 104 MMEGGELFHRISQHRHFTEKQA---------------------------SQVTKQDAPVKLCDFGFAKID-QGDLMTPQF 155
Cdd:cd05586    77 YMSGGELFWHLQKEGRFSEDRAkfyiaelvlalehlhkndivyrdlkpeNILLDANGHIALCDFGLSKADlTDNKTTNTF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 156 --TPYYVAPQVLeaqrrhqKEKSGiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHsrtipKDMRRKIMTGSF 233
Cdd:cd05586   157 cgTTEYLAPEVL-------LDEKG----------YTKMVDFWSLGVLVFEMCCGWSPFYAEDT-----QQMYRNIAFGKV 214
                         250       260       270
                  ....*....|....*....|....*....|
gi 1704602876 234 EFPEEewsQISEMAKDVVRKLLKVKPEERL 263
Cdd:cd05586   215 RFPKD---VLSDEGRSFVKGLLNRNPKHRL 241
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
96-276 1.66e-15

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: 76.28  E-value: 1.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  96 ARLLIVMEMMEGGELFHRISQHRHFTEKQA----SQVT-----------------------KQDAPVKLCDFGFAK--ID 146
Cdd:cd05583    72 AKLHLILDYVNGGELFTHLYQREHFTESEVriyiGEIVlalehlhklgiiyrdiklenillDSEGHVVLTDFGLSKefLP 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 147 QGDLMTPQF--TPYYVAPQVLEAQRRhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFySKHHSRTIPKDM 224
Cdd:cd05583   152 GENDRAYSFcgTIEYMAPEVVRGGSD----------------GHDKAVDWWSLGVLTYELLTGASPF-TVDGERNSQSEI 214
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1704602876 225 RRKIMTGSFEFPEEewsqISEMAKDVVRKLLKVKPEERL--TIEGVLD---HPWLNS 276
Cdd:cd05583   215 SKRILKSHPPIPKT----FSAEAKDFILKLLEKDPKKRLgaGPRGAHEikeHPFFKG 267
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
26-274 1.72e-15

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


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 76.00  E-value: 1.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALK-ILLDR--PKARNEVRLHMMCAT---HPNIVQIIEVFANsvqfphesspRARLL 99
Cdd:cd08218     6 KKIGEGSFGKALLVKSKEDGKQYVIKeINISKmsPKEREESRKEVAVLSkmkHPNIVQYQESFEE----------NGNLY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMEGGELFHRISQHR--HFTEKQ-------------------------ASQ---VTKqDAPVKLCDFGFAKI--DQ 147
Cdd:cd08218    76 IVMDYCDGGDLYKRINAQRgvLFPEDQildwfvqlclalkhvhdrkilhrdiKSQnifLTK-DGIIKLGDFGIARVlnST 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 148 GDLM-TPQFTPYYVAPQVLEAQrrhqkeksgiiptsptPYTyNKScDLWSLGVIIYVMLCGYPPFYSKHHsrtipKDMRR 226
Cdd:cd08218   155 VELArTCIGTPYYLSPEICENK----------------PYN-NKS-DIWALGCVLYEMCTLKHAFEAGNM-----KNLVL 211
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1704602876 227 KIMTGSF-EFPeeewSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd08218   212 KIIRGSYpPVP----SRYSYDLRSLVSQLFKRNPRDRPSINSILEKPFI 256
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
27-279 2.58e-15

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: 75.92  E-value: 2.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  27 KLGAGISGPVRVCVKKSTQERFALKILLDRPKAR------NEVRLHMMCAtHPNIVQIIEVFANSvqfpHESSprarLLI 100
Cdd:cd06621     8 SLGEGAGGSVTKCRLRNTKTIFALKTITTDPNPDvqkqilRELEINKSCA-SPYIVKYYGAFLDE----QDSS----IGI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 101 VMEMMEGGEL----------FHRISQHR---------------------HFTEKQASQVTKQDAPVKLCDFGFAkidqGD 149
Cdd:cd06621    79 AMEYCEGGSLdsiykkvkkkGGRIGEKVlgkiaesvlkglsylhsrkiiHRDIKPSNILLTRKGQVKLCDFGVS----GE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 150 L-----MTPQFTPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDM 224
Cdd:cd06621   155 LvnslaGTFTGTSYYMAPERIQGG------------------PYSITSDVWSLGLTLLEVAQNRFPFPPEGEPPLGPIEL 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1704602876 225 RRKIMTGS-FEFPEEEWSQI--SEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEA 279
Cdd:cd06621   217 LSYIVNMPnPELKDEPENGIkwSESFKDFIEKCLEKDGTRRPGPWQMLAHPWIKAQEK 274
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
18-287 3.50e-15

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: 76.58  E-value: 3.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  18 EEYSInwTQKLGAGISGPVRVCVKKSTQERFALKILLDRPKARN-------EVRLHMMCATHPNIVQIIEVFANSvqfph 90
Cdd:cd05621    52 EDYDV--VKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRsdsaffwEERDIMAFANSPWVVQLFCAFQDD----- 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  91 essprARLLIVMEMMEGGELFHRISQHR--------------------------HFTEKQASQVTKQDAPVKLCDFGFA- 143
Cdd:cd05621   125 -----KYLYMVMEYMPGGDLVNLMSNYDvpekwakfytaevvlaldaihsmgliHRDVKPDNMLLDKYGHLKLADFGTCm 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 144 KIDQGDLM---TPQFTPYYVAPQVLEAQrrhqkeksgiiptSPTPYtYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTI 220
Cdd:cd05621   200 KMDETGMVhcdTAVGTPDYISPEVLKSQ-------------GGDGY-YGRECDWWSVGVFLFEMLVGDTPFYADSLVGTY 265
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1704602876 221 PKDMRRKimtGSFEFPEEewSQISEMAKDVVRKLLKVKpEERLTIEGVLD---HPWL-NSTEALDNVLPSA 287
Cdd:cd05621   266 SKIMDHK---NSLNFPDD--VEISKHAKNLICAFLTDR-EVRLGRNGVEEikqHPFFrNDQWNWDNIRETA 330
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
26-274 5.52e-15

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: 74.64  E-value: 5.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKILLDR-----------PKARNEVRLhmmcATHPNIVQIIEVFansvqfpheSSP 94
Cdd:cd14163     6 KTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSggpeefiqrflPRELQIVER----LDHKNIIHVYEML---------ESA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  95 RARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ--DA------------------------PVKLCDFGFAKI--D 146
Cdd:cd14163    73 DGKIYLVMELAEDGDVFDCVLHGGPLPEHRAKALFRQlvEAirychgcgvahrdlkcenallqgfTLKLTDFGFAKQlpK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 147 QGDLMTPQF--TPYYVAPQVLEAqrrhqkeksgiiptspTPYTYNKScDLWSLGVIIYVMLCGYPPFyskhHSRTIPKDM 224
Cdd:cd14163   153 GGRELSQTFcgSTAYAAPEVLQG----------------VPHDSRKG-DIWSMGVVLYVMLCAQLPF----DDTDIPKML 211
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1704602876 225 RRKimTGSFEFPEEewSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14163   212 CQQ--QKGVSLPGH--LGVSRTCQDLLKRLLEPDMVLRPSIEEVSWHPWL 257
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
135-275 7.21e-15

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: 75.46  E-value: 7.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 135 VKLCDFGFA-KIDQGDLM---TPQFTPYYVAPQVLEAQrrhqKEKSGiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPP 210
Cdd:cd05597   141 IRLADFGSClKLREDGTVqssVAVGTPDYISPEILQAM----EDGKG---------RYGPECDWWSLGVCMYEMLYGETP 207
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1704602876 211 FYSKHHSRTIPKDMRRKimtGSFEFPEEEwSQISEMAKDVVRKLLkVKPEERLTIEGVLD---HPWLN 275
Cdd:cd05597   208 FYAESLVETYGKIMNHK---EHFSFPDDE-DDVSEEAKDLIRRLI-CSRERRLGQNGIDDfkkHPFFE 270
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
157-274 1.17e-14

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: 73.16  E-value: 1.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 157 PYYVAPQVLEaqrrhqkeksgiiptspTPYTYN-KSCDLWSLGVIIYVMLCGYPPFYSKHhsrtiPKDMRRKIMTGSFEF 235
Cdd:cd14023   150 PAYVSPEILN-----------------TTGTYSgKSADVWSLGVMLYTLLVGRYPFHDSD-----PSALFSKIRRGQFCI 207
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1704602876 236 PEeewsQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14023   208 PD----HVSPKARCLIRSLLRREPSERLTAPEILLHPWF 242
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
156-276 1.27e-14

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: 74.66  E-value: 1.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 156 TPYYVAPQVLEaqrrhqkeKSGiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSkhhsrTIPKDMRRKIM--TGSF 233
Cdd:cd05598   168 TPNYIAPEVLL--------RTG----------YTQLCDWWSVGVILYEMLVGQPPFLA-----QTPAETQLKVInwRTTL 224
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1704602876 234 EFPEEewSQISEMAKDVVRKLLkVKPEERLTIEGVLD---HPWLNS 276
Cdd:cd05598   225 KIPHE--ANLSPEAKDLILRLC-CDAEDRLGRNGADEikaHPFFAG 267
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
28-263 1.36e-14

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: 74.35  E-value: 1.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILL--------DRPKARNEVRLHMMCATHPNIVQIIEVFANSvqfphessprARLL 99
Cdd:cd05587     4 LGKGSFGKVMLAERKGTDELYAIKILKkdviiqddDVECTMVEKRVLALSGKPPFLTQLHSCFQTM----------DRLY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMEGGELFHRISQHRHFTEKQA---------------------------SQVTKQDAPVKLCDFGFAKID-QGDLM 151
Cdd:cd05587    74 FVMEYVNGGDLMYHIQQVGKFKEPVAvfyaaeiavglfflhskgiiyrdlkldNVMLDAEGHIKIADFGMCKEGiFGGKT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 152 TPQF--TPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHsrtipKDMRRKIM 229
Cdd:cd05587   154 TRTFcgTPDYIAPEIIAYQ------------------PYGKSVDWWAYGVLLYEMLAGQPPFDGEDE-----DELFQSIM 210
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1704602876 230 TGSFEFPEeewsQISEMAKDVVRKLLKVKPEERL 263
Cdd:cd05587   211 EHNVSYPK----SLSKEAVSICKGLLTKHPAKRL 240
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
27-274 1.40e-14

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: 73.25  E-value: 1.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  27 KLGAGISGPVRVCVKKSTQERFALKILLDRPKAR-----NEVRLhMMCATHPNIVQiievFANSVQFPHEssprarLLIV 101
Cdd:cd06648    14 KIGEGSTGIVCIATDKSTGRQVAVKKMDLRKQQRrellfNEVVI-MRDYQHPNIVE----MYSSYLVGDE------LWVV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 102 MEMMEGGELFHRISQHRhFTEKQASQVTKQ---------------------------DAPVKLCDFGFAKidQGDLMTPQ 154
Cdd:cd06648    83 MEFLEGGALTDIVTHTR-MNEEQIATVCRAvlkalsflhsqgvihrdiksdsilltsDGRVKLSDFGFCA--QVSKEVPR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 155 F-----TPYYVAPQVleaqrrhqkeksgiIPTSPtpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHhsrtiPKDMRRKIM 229
Cdd:cd06648   160 RkslvgTPYWMAPEV--------------ISRLP----YGTEVDIWSLGIMVIEMVDGEPPYFNEP-----PLQAMKRIR 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1704602876 230 TGSFEFPEEEwSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd06648   217 DNEPPKLKNL-HKVSPRLRSFLDRMLVRDPAQRATAAELLNHPFL 260
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
72-274 1.54e-14

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: 73.83  E-value: 1.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  72 HPNIVQIIEVFANsvqfPHESSprarLLIVMEMMEGGELFHRISQHRhFTEKQASQVTKQ-------------------- 131
Cdd:cd14200    82 HVNIVKLIEVLDD----PAEDN----LYMVFDLLRKGPVMEVPSDKP-FSEDQARLYFRDivlgieylhyqkivhrdikp 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 132 -------DAPVKLCDFGFAKIDQGD---LMTPQFTPYYVAPQVLEAQRrhqKEKSGiiptsptpytynKSCDLWSLGVII 201
Cdd:cd14200   153 snlllgdDGHVKIADFGVSNQFEGNdalLSSTAGTPAFMAPETLSDSG---QSFSG------------KALDVWAMGVTL 217
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1704602876 202 YVMLCGYPPFYSKHhsrtiPKDMRRKIMTGSFEFPEEewSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14200   218 YCFVYGKCPFIDEF-----ILALHNKIKNKPVEFPEE--PEISEELKDLILKMLDKNPETRITVPEIKVHPWV 283
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
26-274 1.94e-14

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: 73.07  E-value: 1.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALK-------ILLDRPKARNEVRLhMMCATHPNIVqiieVFANSVQfphessPRARL 98
Cdd:cd08225     6 KKIGEGSFGKIYLAKAKSDSEHCVIKeidltkmPVKEKEASKKEVIL-LAKMKHPNIV----TFFASFQ------ENGRL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  99 LIVMEMMEGGELFHRISQHRH--FTEKQ-------------------------ASQ---VTKQDAPVKLCDFGFAKI--D 146
Cdd:cd08225    75 FIVMEYCDGGDLMKRINRQRGvlFSEDQilswfvqislglkhihdrkilhrdiKSQnifLSKNGMVAKLGDFGIARQlnD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 147 QGDL-MTPQFTPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDMR 225
Cdd:cd08225   155 SMELaYTCVGTPYYLSPEICQNR------------------PYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQ 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1704602876 226 RKIMTGSFEFPEEEWSQISEmakdvvrkLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd08225   217 GYFAPISPNFSRDLRSLISQ--------LFKVSPRDRPSITSILKRPFL 257
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
28-273 1.96e-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: 73.68  E-value: 1.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILL--------DRPKARNEVRLHMMCATHPNIVQIIEVFANsvqfphesspRARLL 99
Cdd:cd05591     3 LGKGSFGKVMLAERKGTDEVYAIKVLKkdvilqddDVDCTMTEKRILALAAKHPFLTALHSCFQT----------KDRLF 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMEGGELFHRISQHRHFTEKQ----ASQVT-----------------------KQDAPVKLCDFGFAKID-QGDLM 151
Cdd:cd05591    73 FVMEYVNGGDLMFQIQRARKFDEPRarfyAAEVTlalmflhrhgviyrdlkldnillDAEGHCKLADFGMCKEGiLNGKT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 152 TPQF--TPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSrtipkDMRRKIM 229
Cdd:cd05591   153 TTTFcgTPDYIAPEILQELE------------------YGPSVDWWALGVLMYEMMAGQPPFEADNED-----DLFESIL 209
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1704602876 230 TGSFEFPeeEWsqISEMAKDVVRKLLKVKPEERL-------TIEGVLDHPW 273
Cdd:cd05591   210 HDDVLYP--VW--LSKEAVSILKAFMTKNPAKRLgcvasqgGEDAIRQHPF 256
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
25-276 2.12e-14

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


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 73.71  E-value: 2.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  25 TQKLGAGISGPVRVCVKKSTQERFALK-------ILLDRPKARNEVRLhMMCATHPNIVQIIEVFansvqfPHESSPRAR 97
Cdd:cd07834     5 LKPIGSGAYGVVCSAYDKRTGRKVAIKkisnvfdDLIDAKRILREIKI-LRHLKHENIIGLLDIL------RPPSPEEFN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  98 -LLIVMEMMEGGelFHR-ISQHRHFTE---------------------------KQASQVTKQDAPVKLCDFGFAKIDQG 148
Cdd:cd07834    78 dVYIVTELMETD--LHKvIKSPQPLTDdhiqyflyqilrglkylhsagvihrdlKPSNILVNSNCDLKICDFGLARGVDP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 149 DLMTPQFTPY-----YVAPQVLEAQRRhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHsrtipKD 223
Cdd:cd07834   156 DEDKGFLTEYvvtrwYRAPELLLSSKK-----------------YTKAIDIWSVGCIFAELLTRKPLFPGRDY-----ID 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 224 MRRKIMT--GSfefPEEE------------------------WSQI----SEMAKDVVRKLLKVKPEERLTIEGVLDHPW 273
Cdd:cd07834   214 QLNLIVEvlGT---PSEEdlkfissekarnylkslpkkpkkpLSEVfpgaSPEAIDLLEKMLVFNPKKRITADEALAHPY 290

                  ...
gi 1704602876 274 LNS 276
Cdd:cd07834   291 LAQ 293
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
135-273 2.45e-14

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: 72.82  E-value: 2.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 135 VKLCDFGFAKI-----------DQGDLMTPQF-------TPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWS 196
Cdd:cd05609   139 IKLTDFGLSKIglmslttnlyeGHIEKDTREFldkqvcgTPEYIAPEVILRQ------------------GYGKPVDWWA 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 197 LGVIIYVMLCGYPPFYSKhhsrtIPKDMRRKIMTGSFEFPEEEwSQISEMAKDVVRKLLKVKPEERLTIEG---VLDHPW 273
Cdd:cd05609   201 MGIILYEFLVGCVPFFGD-----TPEELFGQVISDEIEWPEGD-DALPDDAQDLITRLLQQNPLERLGTGGaeeVKQHPF 274
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
23-263 2.45e-14

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: 73.49  E-value: 2.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  23 NWTQKLGAGISGPVRVCVKKSTQERFALKILL--------DRPKARNEVRLHMMCATHPNIVQIIEVFANsvqfphessp 94
Cdd:cd05616     3 NFLMVLGKGSFGKVMLAERKGTDELYAVKILKkdvviqddDVECTMVEKRVLALSGKPPFLTQLHSCFQT---------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  95 RARLLIVMEMMEGGELFHRISQHRHFTEKQA---------------------------SQVTKQDAPVKLCDFGFAKIDQ 147
Cdd:cd05616    73 MDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAvfyaaeiaiglfflqskgiiyrdlkldNVMLDSEGHIKIADFGMCKENI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 148 GDLMTPQF---TPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSrtipkDM 224
Cdd:cd05616   153 WDGVTTKTfcgTPDYIAPEIIAYQ------------------PYGKSVDWWAFGVLLYEMLAGQAPFEGEDED-----EL 209
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1704602876 225 RRKIMTGSFEFPEeewsQISEMAKDVVRKLLKVKPEERL 263
Cdd:cd05616   210 FQSIMEHNVAYPK----SMSKEAVAICKGLMTKHPGKRL 244
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
28-282 4.23e-14

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: 73.03  E-value: 4.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILL--------DRPKARNEVRLHMMCATHPNIVQIIEVFANsvqfphesspRARLL 99
Cdd:cd05619    13 LGKGSFGKVFLAELKGTNQFFAIKALKkdvvlmddDVECTMVEKRVLSLAWEHPFLTHLFCTFQT----------KENLF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMEGGEL-FHRISQHR-----------------HFTE---------KQASQVTKQDAPVKLCDFGFAKIDQ-GDLM 151
Cdd:cd05619    83 FVMEYLNGGDLmFHIQSCHKfdlpratfyaaeiicglQFLHskgivyrdlKLDNILLDKDGHIKIADFGMCKENMlGDAK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 152 TPQF--TPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHsrtipKDMRRKIM 229
Cdd:cd05619   163 TSTFcgTPDYIAPEILLGQK------------------YNTSVDWWSFGVLLYEMLIGQSPFHGQDE-----EELFQSIR 219
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1704602876 230 TGSFEFPeeEWsqISEMAKDVVRKLLKVKPEERLTIEG-VLDHPWLNST--EALDN 282
Cdd:cd05619   220 MDNPFYP--RW--LEKEAKDILVKLFVREPERRLGVRGdIRQHPFFREInwEALEE 271
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
28-263 5.84e-14

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: 72.31  E-value: 5.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLHMMCATHPNIVQIIEVFANSVQFPHESSprARLLIVMEMMEG 107
Cdd:cd05603     3 IGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNHIMAERNVLLKNLKHPFLVGLHYSFQTS--EKLYFVLDYVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 108 GELFHRISQHRHFTEKQASQVTKQDAP---------------------------VKLCDFGFAK--IDQGDlMTPQF--T 156
Cdd:cd05603    81 GELFFHLQRERCFLEPRARFYAAEVASaigylhslniiyrdlkpenilldcqghVVLTDFGLCKegMEPEE-TTSTFcgT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 157 PYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRtipkdMRRKIMTGSFEFP 236
Cdd:cd05603   160 PEYLAPEVLRKE------------------PYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQ-----MYDNILHKPLHLP 216
                         250       260
                  ....*....|....*....|....*..
gi 1704602876 237 EEEwsqiSEMAKDVVRKLLKVKPEERL 263
Cdd:cd05603   217 GGK----TVAACDLLQGLLHKDQRRRL 239
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
18-306 5.86e-14

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: 73.12  E-value: 5.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  18 EEYSInwTQKLGAGISGPVRVCVKKSTQERFALKIL--LDRPKARN-----EVRLHMMCATHPNIVQIIEVFANSvqfph 90
Cdd:cd05622    73 EDYEV--VKVIGRGAFGEVQLVRHKSTRKVYAMKLLskFEMIKRSDsaffwEERDIMAFANSPWVVQLFYAFQDD----- 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  91 essprARLLIVMEMMEGGELFHRISQH-------RHFTE-------------------KQASQVTKQDAPVKLCDFGFA- 143
Cdd:cd05622   146 -----RYLYMVMEYMPGGDLVNLMSNYdvpekwaRFYTAevvlaldaihsmgfihrdvKPDNMLLDKSGHLKLADFGTCm 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 144 KIDQGDLM---TPQFTPYYVAPQVLEAQrrhqkeksgiiptSPTPYtYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTI 220
Cdd:cd05622   221 KMNKEGMVrcdTAVGTPDYISPEVLKSQ-------------GGDGY-YGRECDWWSVGVFLYEMLVGDTPFYADSLVGTY 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 221 PKDMRRKimtGSFEFPEEewSQISEMAKDVVRKLLKVKpEERLTIEGVLD---HP--------WLNSTEALDNVLPSAQL 289
Cdd:cd05622   287 SKIMNHK---NSLTFPDD--NDISKEAKNLICAFLTDR-EVRLGRNGVEEikrHLffkndqwaWETLRDTVAPVVPDLSS 360
                         330
                  ....*....|....*..
gi 1704602876 290 MMDKAVVAGIQQAHAEQ 306
Cdd:cd05622   361 DIDTSNFDDLEEDKGEE 377
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
26-274 8.49e-14

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: 71.00  E-value: 8.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKILlDRPKA----------RNEVRLHMMCaTHPNIVQIIEVFANSVQFphesspr 95
Cdd:cd14070     8 RKLGEGSFAKVREGLHAVTGEKVAIKVI-DKKKAkkdsyvtknlRREGRIQQMI-RHPNITQLLDILETENSY------- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  96 arlLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ---------------------------DAPVKLCDFGF---AKI 145
Cdd:cd14070    79 ---YLVMELCPGGNLMHRIYDKKRLEEREARRYIRQlvsavehlhragvvhrdlkienllldeNDNIKLIDFGLsncAGI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 146 DQG--DLMTPQFTPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRtipKD 223
Cdd:cd14070   156 LGYsdPFSTQCGSPAYAAPELLARKK------------------YGPKVDVWSIGVNMYAMLTGTLPFTVEPFSL---RA 214
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1704602876 224 MRRKIMTGSFE-FPeeewSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14070   215 LHQKMVDKEMNpLP----TDLSPGAISFLRSLLEPDPLKRPNIKQALANRWL 262
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
28-274 1.02e-13

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: 70.76  E-value: 1.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILLDRPK----ARNEVR-LHMM----CATHPNIVQIIEVFANsvqfphesspRARL 98
Cdd:cd14133     7 LGKGTFGQVVKCYDLLTGEEVALKIIKNNKDyldqSLDEIRlLELLnkkdKADKYHIVRLKDVFYF----------KNHL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  99 LIVMEMMEGG-ELFHRISQHRHFTEKQASQVTKQ-----------------------------DAPVKLCDFGFAKIDQG 148
Cdd:cd14133    77 CIVFELLSQNlYEFLKQNKFQYLSLPRIRKIAQQilealvflhslglihcdlkpenillasysRCQIKIIDFGSSCFLTQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 149 DLMTPQFTPYYVAPQVLEAqrrhqkeksgiiptsptpYTYNKSCDLWSLGVIIYVMLCGYPPFYSKHhsrtiPKDMRRKI 228
Cdd:cd14133   157 RLYSYIQSRYYRAPEVILG------------------LPYDEKIDMWSLGCILAELYTGEPLFPGAS-----EVDQLARI 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1704602876 229 MTGSFEFPEEEWSQIS---EMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14133   214 IGTIGIPPAHMLDQGKaddELFVDFLKKLLEIDPKERPTASQALSHPWL 262
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
135-274 1.17e-13

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: 70.71  E-value: 1.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 135 VKLCDFGFAKIDQGD----LMTPQF-TPYYVAPQVLEAQRRHQKEKSgiiptsptPYTYNKSCDLWSLGVIIYVMLCGYP 209
Cdd:cd14131   141 LKLIDFGIAKAIQNDttsiVRDSQVgTLNYMSPEAIKDTSASGEGKP--------KSKIGRPSDVWSLGCILYQMVYGKT 212
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1704602876 210 PFYskHHSRTIPKDMRrkIMTGSFEFpeeEWSQISE-MAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14131   213 PFQ--HITNPIAKLQA--IIDPNHEI---EFPDIPNpDLIDVMKRCLQRDPKKRPSIPELLNHPFL 271
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
157-274 1.44e-13

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


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 69.91  E-value: 1.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 157 PYYVAPQVLEAQRRHqkekSGiiptsptpytynKSCDLWSLGVIIYVMLCGYPPFYSkhhsrTIPKDMRRKIMTGSFEFP 236
Cdd:cd14024   150 PAYVGPEILSSRRSY----SG------------KAADVWSLGVCLYTMLLGRYPFQD-----TEPAALFAKIRRGAFSLP 208
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1704602876 237 EeewsQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14024   209 A----WLSPGARCLVSCMLRRSPAERLKASEILLHPWL 242
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
26-272 1.81e-13

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


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 70.03  E-value: 1.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKILL-----DRPKARNEVRLHMMCaTHPNIVQiievFANSVQfphessPRARLLI 100
Cdd:cd06613     6 QRIGSGTYGDVYKARNIATGELAAVKVIKlepgdDFEIIQQEISMLKEC-RHPNIVA----YFGSYL------RRDKLWI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 101 VMEMMEGGELFHRISQHRHFTEKQASQVTKQ---------------------------DAPVKLCDFGF-AKIDQGDLMT 152
Cdd:cd06613    75 VMEYCGGGSLQDIYQVTGPLSELQIAYVCREtlkglaylhstgkihrdikganillteDGDVKLADFGVsAQLTATIAKR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 153 PQF--TPYYVAPQVLEAQRrhqkeKSGiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHhsrtiPkdMRRKIMT 230
Cdd:cd06613   155 KSFigTPYWMAPEVAAVER-----KGG----------YDGKCDIWALGITAIELAELQPPMFDLH-----P--MRALFLI 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1704602876 231 GSFEFP------EEEWSqiSEMaKDVVRKLLKVKPEERLTIEGVLDHP 272
Cdd:cd06613   213 PKSNFDppklkdKEKWS--PDF-HDFIKKCLTKNPKKRPTATKLLQHP 257
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
72-274 1.83e-13

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: 70.38  E-value: 1.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  72 HPNIVQIIEVFANsvqfPHESspraRLLIVMEMMEGGELFHrISQHRHFTEKQA-------------------------- 125
Cdd:cd14199    84 HPNVVKLVEVLDD----PSED----HLYMVFELVKQGPVME-VPTLKPLSEDQArfyfqdlikgieylhyqkiihrdvkp 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 126 -SQVTKQDAPVKLCDFGFAKIDQGD---LMTPQFTPYYVAPQVLEAQRrhqKEKSGiiptsptpytynKSCDLWSLGVII 201
Cdd:cd14199   155 sNLLVGEDGHIKIADFGVSNEFEGSdalLTNTVGTPAFMAPETLSETR---KIFSG------------KALDVWAMGVTL 219
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1704602876 202 YVMLCGYPPFYSKhhsRTIpkDMRRKIMTGSFEFPEEewSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14199   220 YCFVFGQCPFMDE---RIL--SLHSKIKTQPLEFPDQ--PDISDDLKDLLFRMLDKNPESRISVPEIKLHPWV 285
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
27-274 1.85e-13

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: 70.13  E-value: 1.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  27 KLGAGISGPVRVCVKKSTQERFALKIL-------LDRPKARNEVRLhMMCATHPNIVQIIEVFANsvqfphesspRARLL 99
Cdd:cd08529     7 KLGKGSFGVVYKVVRKVDGRVYALKQIdisrmsrKMREEAIDEARV-LSKLNSPYVIKYYDSFVD----------KGKLN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMEGGELFHRISQH--RHFTEKQASQVTKQ---------------------------DAPVKLCDFGFAKI--DQG 148
Cdd:cd08529    76 IVMEYAENGDLHSLIKSQrgRPLPEDQIWKFFIQtllglshlhskkilhrdiksmnifldkGDNVKIGDLGVAKIlsDTT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 149 DL-MTPQFTPYYVAPQVLEaqrrhqkEKSgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIpkdmrRK 227
Cdd:cd08529   156 NFaQTIVGTPYYLSPELCE-------DKP-----------YNEKSDVWALGCVLYELCTGKHPFEAQNQGALI-----LK 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1704602876 228 IMTGSFEFPEEEWSQisEMAkDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd08529   213 IVRGKYPPISASYSQ--DLS-QLIDSCLTKDYRQRPDTTELLRNPSL 256
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
28-262 3.28e-13

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


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 69.45  E-value: 3.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPV-RVCVKKSTQERFALK-ILLDRPKAR--------------NEVRLHMMCATHPNIVQIIEVFANSvqfphe 91
Cdd:cd08528     8 LGSGAFGCVyKVRKKSNGQTLLALKeINMTNPAFGrteqerdksvgdiiSEVNIIKEQLRHPNIVRYYKTFLEN------ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  92 ssprARLLIVMEMMEG---GELFHRISQ-HRHFTEKQASQVTKQ----------------------------DAPVKLCD 139
Cdd:cd08528    82 ----DRLYIVMELIEGaplGEHFSSLKEkNEHFTEDRIWNIFVQmvlalrylhkekqivhrdlkpnnimlgeDDKVTITD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 140 FGFAKIDQGD---LMTPQFTPYYVAPQVLEAQrrhqkeksgiiptsptPYTynKSCDLWSLGVIIYVMLCGYPPFYSkhh 216
Cdd:cd08528   158 FGLAKQKGPEsskMTSVVGTILYSCPEIVQNE----------------PYG--EKADIWALGCILYQMCTLQPPFYS--- 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1704602876 217 srTIPKDMRRKIMTGSFE-FPEEEWsqiSEMAKDVVRKLLKVKPEER 262
Cdd:cd08528   217 --TNMLTLATKIVEAEYEpLPEGMY---SDDITFVIRSCLTPDPEAR 258
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
13-274 3.51e-13

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


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 70.28  E-value: 3.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  13 ETSILEEYSInwTQKLGAGISGPVRVCVKKSTQERFALKILLDrpkA-RN---------EVRLHMMCATHPNIVQIIEVF 82
Cdd:cd07852     2 DKHILRRYEI--LKKLGKGAYGIVWKAIDKKTGEVVALKKIFD---AfRNatdaqrtfrEIMFLQELNDHPNIIKLLNVI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  83 ------------------------ANSVQFPHESSPRARLLIVMEMMEGGELFHRisqhrhfTEKQASQVTKQDAPVKLC 138
Cdd:cd07852    77 raendkdiylvfeymetdlhavirANILEDIHKQYIMYQLLKALKYLHSGGVIHR-------DLKPSNILLNSDCRVKLA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 139 DFGFAK---IDQGDLMTPQFTPY-----YVAPQVLEAQRRhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPP 210
Cdd:cd07852   150 DFGLARslsQLEEDDENPVLTDYvatrwYRAPEILLGSTR-----------------YTKGVDMWSVGCILGEMLLGKPL 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 211 FYSkhhSRTIpkDMRRKIMTgSFEFPEEE----------WSQISEM------------------AKDVVRKLLKVKPEER 262
Cdd:cd07852   213 FPG---TSTL--NQLEKIIE-VIGRPSAEdiesiqspfaATMLESLppsrpksldelfpkaspdALDLLKKLLVFNPNKR 286
                         330
                  ....*....|..
gi 1704602876 263 LTIEGVLDHPWL 274
Cdd:cd07852   287 LTAEEALRHPYV 298
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
27-274 4.25e-13

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: 69.23  E-value: 4.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  27 KLGAGISGPVRVCVKKSTQE----RFALKILLDRPKARNEVRLhMMCATHPNIVQIIEVFANSVQFPH--ESSPRARLL- 99
Cdd:cd14113    14 ELGRGRFSVVKKCDQRGTKRavatKFVNKKLMKRDQVTHELGV-LQSLQHPQLVGLLDTFETPTSYILvlEMADQGRLLd 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 -IVM--------------EMMEGGELFH--RISqhrHFTEKQASQVTKQDAP---VKLCDFGfakiDQGDLMTPQF---- 155
Cdd:cd14113    93 yVVRwgnlteekirfylrEILEALQYLHncRIA---HLDLKPENILVDQSLSkptIKLADFG----DAVQLNTTYYihql 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 156 --TPYYVAPQvleaqrrhqkeksgIIPTSPTPYTynksCDLWSLGVIIYVMLCGYPPFYSKHHSRTIpkdmrRKIMTGSF 233
Cdd:cd14113   166 lgSPEFAAPE--------------IILGNPVSLT----SDLWSIGVLTYVLLSGVSPFLDESVEETC-----LNICRLDF 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1704602876 234 EFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14113   223 SFPDDYFKGVSQKAKDFVCFLLQMDPAKRPSAALCLQEQWL 263
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
28-276 4.74e-13

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: 69.09  E-value: 4.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKIL-LDRPKARNEVRLHMmcathpNIVQIIEV----FANSVQFPHESspRARLLIVM 102
Cdd:cd05577     1 LGRGGFGEVCACQVKATGKMYACKKLdKKRIKKKKGETMAL------NEKIILEKvsspFIVSLAYAFET--KDKLCLVL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 103 EMMEGGELFHRISQH--RHFTEKQASQVTKQ---------------------------DAPVKLCDFGFAKIDQGDLMTP 153
Cdd:cd05577    73 TLMNGGDLKYHIYNVgtRGFSEARAIFYAAEiicglehlhnrfivyrdlkpenillddHGHVRISDLGLAVEFKGGKKIK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 154 QF--TPYYVAPQVLEAQRrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFySKHHSRTIPKDMRRKIMTG 231
Cdd:cd05577   153 GRvgTHGYMAPEVLQKEV-----------------AYDFSVDWFALGCMLYEMIAGRSPF-RQRKEKVDKEELKRRTLEM 214
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1704602876 232 SFEFPEEewsqISEMAKDVVRKLLKVKPEERL-----TIEGVLDHPWLNS 276
Cdd:cd05577   215 AVEYPDS----FSPEARSLCEGLLQKDPERRLgcrggSADEVKEHPFFRS 260
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
28-263 5.35e-13

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: 69.66  E-value: 5.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLHMMCATHPNIVQIIEVFANSVQFPHESSprARLLIVMEMMEG 107
Cdd:cd05602    15 IGKGSFGKVLLARHKSDEKFYAVKVLQKKAILKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTT--DKLYFVLDYING 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 108 GELFHRISQHRHFTEKQASQVTKQDAP---------------------------VKLCDFGFAKID-QGDLMTPQF--TP 157
Cdd:cd05602    93 GELFYHLQRERCFLEPRARFYAAEIASalgylhslnivyrdlkpenilldsqghIVLTDFGLCKENiEPNGTTSTFcgTP 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 158 YYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSrtipkDMRRKIMTGSFEFPe 237
Cdd:cd05602   173 EYLAPEVLHKQ------------------PYDRTVDWWCLGAVLYEMLYGLPPFYSRNTA-----EMYDNILNKPLQLK- 228
                         250       260
                  ....*....|....*....|....*.
gi 1704602876 238 eewSQISEMAKDVVRKLLKVKPEERL 263
Cdd:cd05602   229 ---PNITNSARHLLEGLLQKDRTKRL 251
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
60-227 7.64e-13

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 67.95  E-value: 7.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  60 RNEVRLhMMCATHPNIVQIIEVFANSvqfPHessprarLLIVMEMMEGGELFHRI-SQHRHFTEKQASQVTKQ------- 131
Cdd:cd13999    38 RREVSI-LSKLRHPNIVQFIGACLSP---PP-------LCIVTEYMPGGSLYDLLhKKKIPLSWSLRLKIALDiargmny 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 132 ------------------DAP--VKLCDFGFAKI---DQGDLMTPQFTPYYVAPQVLEAQRrhqkeksgiiptsptpytY 188
Cdd:cd13999   107 lhsppiihrdlkslnillDENftVKIADFGLSRIknsTTEKMTGVVGTPRWMAPEVLRGEP------------------Y 168
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1704602876 189 NKSCDLWSLGVIIYVMLCGYPPFySKHHSRTIPKDMRRK 227
Cdd:cd13999   169 TEKADVYSFGIVLWELLTGEVPF-KELSPIQIAAAVVQK 206
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
28-276 1.04e-12

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: 68.82  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILL--------DRPKARNEVRLHMMCATHPNIVQIIEVFANsvqfphesspRARLL 99
Cdd:cd05620     3 LGKGSFGKVLLAELKGKGEYFAVKALKkdvvliddDVECTMVEKRVLALAWENPFLTHLYCTFQT----------KEHLF 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMEGGELFHRISQHRHFTEKQAS---------------------------QVTKQDAPVKLCDFGFAKIDQ-GDLM 151
Cdd:cd05620    73 FVMEFLNGGDLMFHIQDKGRFDLYRATfyaaeivcglqflhskgiiyrdlkldnVMLDRDGHIKIADFGMCKENVfGDNR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 152 TPQF--TPYYVAPQVLEAQRrhqkeksgiiptsptpYTYnkSCDLWSLGVIIYVMLCGYPPFYSKHHSrtipkDMRRKIM 229
Cdd:cd05620   153 ASTFcgTPDYIAPEILQGLK----------------YTF--SVDWWSFGVLLYEMLIGQSPFHGDDED-----ELFESIR 209
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1704602876 230 TGSFEFPeeEWsqISEMAKDVVRKLLKVKPEERLTIEG-VLDHPWLNS 276
Cdd:cd05620   210 VDTPHYP--RW--ITKESKDILEKLFERDPTRRLGVVGnIRGHPFFKT 253
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
97-274 1.13e-12

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: 68.04  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  97 RLLIVMEMMEGGELFHRIsQHRHFTEKQASQVTKQ---------------------------DAPVKLCDFGFAkidqGD 149
Cdd:cd06609    73 KLWIIMEYCGGGSVLDLL-KPGPLDETYIAFILREvllgleylhsegkihrdikaanillseEGDVKLADFGVS----GQ 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 150 L---MTPQF----TPYYVAPQVLEaqrrhqkeKSGiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRT--- 219
Cdd:cd06609   148 LtstMSKRNtfvgTPFWMAPEVIK--------QSG----------YDEKADIWSLGITAIELAKGEPPLSDLHPMRVlfl 209
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1704602876 220 IPKDmrrkimtgsfEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd06609   210 IPKN----------NPPSLEGNKFSKPFKDFVELCLNKDPKERPSAKELLKHKFI 254
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
28-263 1.54e-12

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: 68.41  E-value: 1.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKS---TQERFALKIL-----LDRPKARNEVRlhmmcaTHPNIVQIIEVFANSVQFPHESSPRARLL 99
Cdd:cd05614     8 LGTGAYGKVFLVRKVSghdANKLYAMKVLrkaalVQKAKTVEHTR------TERNVLEHVRQSPFLVTLHYAFQTDAKLH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMEGGELFHRISQHRHFTE---------------------------KQASQVTKQDAPVKLCDFGFAK--IDQGDL 150
Cdd:cd05614    82 LILDYVSGGELFTHLYQRDHFSEdevrfysgeiilalehlhklgivyrdiKLENILLDSEGHVVLTDFGLSKefLTEEKE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 151 MTPQF--TPYYVAPQVLEAQRRHqkeksgiiptsptpytyNKSCDLWSLGVIIYVMLCGYPPFySKHHSRTIPKDMRRKI 228
Cdd:cd05614   162 RTYSFcgTIEYMAPEIIRGKSGH-----------------GKAVDWWSLGILMFELLTGASPF-TLEGEKNTQSEVSRRI 223
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1704602876 229 MTGSFEFPeeewSQISEMAKDVVRKLLKVKPEERL 263
Cdd:cd05614   224 LKCDPPFP----SFIGPVARDLLQKLLCKDPKKRL 254
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
28-283 2.07e-12

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: 68.50  E-value: 2.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKIL-----LDRPKA---RNE------------VRLHMMCATHPNIVQIIEVFANSVQ 87
Cdd:cd05623    80 IGRGAFGEVAVVKLKNADKVFAMKILnkwemLKRAETacfREErdvlvngdsqwiTTLHYAFQDDNNLYLVMDYYVGGDL 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  88 FPHESSPRARL------LIVMEMMEGGELFHRIsQHRHFTEKQASQVTKQDAPVKLCDFG--FAKIDQGDLMTPQF--TP 157
Cdd:cd05623   160 LTLLSKFEDRLpedmarFYLAEMVLAIDSVHQL-HYVHRDIKPDNILMDMNGHIRLADFGscLKLMEDGTVQSSVAvgTP 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 158 YYVAPQVLEAQRRHQKEksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDMRRKimtGSFEFPe 237
Cdd:cd05623   239 DYISPEILQAMEDGKGK-------------YGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHK---ERFQFP- 301
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1704602876 238 EEWSQISEMAKDVVRKLLKVKpEERLTIEGVLD---HPWLNSTEaLDNV 283
Cdd:cd05623   302 TQVTDVSENAKDLIRRLICSR-EHRLGQNGIEDfknHPFFVGID-WDNI 348
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
25-270 3.54e-12

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: 66.59  E-value: 3.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  25 TQKLGAGISGPVRVCVKKSTQERFALKILL--DRPK---ARNEVRLHMMCATHPNIVQIIEVFANSvqfpheSSPRARLL 99
Cdd:cd13985     5 TKQLGEGGFSYVYLAHDVNTGRRYALKRMYfnDEEQlrvAIKEIEIMKRLCGHPNIVQYYDSAILS------SEGRKEVL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMeGGELFHRISQ--HRHFTEKQASQVT-----------KQDAPV------------------KLCDFGFAkidqg 148
Cdd:cd13985    79 LLMEYC-PGSLVDILEKspPSPLSEEEVLRIFyqicqavghlhSQSPPIihrdikienilfsntgrfKLCDFGSA----- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 149 dlmTPQFTPYYVAPQVLEAQRRHQKEksgiipTSPT--------PYTYNKSC---DLWSLGVIIYVMLCGYPPFYSkhhs 217
Cdd:cd13985   153 ---TTEHYPLERAEEVNIIEEEIQKN------TTPMyrapemidLYSKKPIGekaDIWALGCLLYKLCFFKLPFDE---- 219
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1704602876 218 rtipkDMRRKIMTGSFEFPEEEwsQISEMAKDVVRKLLKVKPEERLTIEGVLD 270
Cdd:cd13985   220 -----SSKLAIVAGKYSIPEQP--RYSPELHDLIRHMLTPDPAERPDIFQVIN 265
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
26-274 4.05e-12

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: 66.40  E-value: 4.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKilldRPKAR----------NEVRLHMMCATHPNIVQIIEVFANSVQfphesspr 95
Cdd:cd07830     5 KQLGDGTFGSVYLARNKETGELVAIK----KMKKKfysweecmnlREVKSLRKLNEHPNIVKLKEVFRENDE-------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  96 arLLIVMEMMEgGELFHRISQH--RHFTEKQASQVTKQDAP---------------------------VKLCDFGFAK-I 145
Cdd:cd07830    73 --LYFVFEYME-GNLYQLMKDRkgKPFSESVIRSIIYQILQglahihkhgffhrdlkpenllvsgpevVKIADFGLAReI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 146 DQgdlmTPQFTPY-----YVAPQVLeaqRRHQKeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFysKHHSRTi 220
Cdd:cd07830   150 RS----RPPYTDYvstrwYRAPEIL---LRSTS--------------YSSPVDIWALGCIMAELYTLRPLF--PGSSEI- 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 221 pkDMRRKIMT--GSFEfpEEEWS--------------------------QISEMAKDVVRKLLKVKPEERLTIEGVLDHP 272
Cdd:cd07830   206 --DQLYKICSvlGTPT--KQDWPegyklasklgfrfpqfaptslhqlipNASPEAIDLIKDMLRWDPKKRPTASQALQHP 281

                  ..
gi 1704602876 273 WL 274
Cdd:cd07830   282 YF 283
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
23-263 5.17e-12

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: 66.94  E-value: 5.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  23 NWTQKLGAGISGPVRVCVKKSTQERFALKILL--------DRPKARNEVRLHMMCATHPNIVQIIEVFANSvqfphessp 94
Cdd:cd05615    13 NFLMVLGKGSFGKVMLAERKGSDELYAIKILKkdvviqddDVECTMVEKRVLALQDKPPFLTQLHSCFQTV--------- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  95 rARLLIVMEMMEGGELFHRISQHRHFTEKQA---------------------------SQVTKQDAPVKLCDFGFAKIDQ 147
Cdd:cd05615    84 -DRLYFVMEYVNGGDLMYHIQQVGKFKEPQAvfyaaeisvglfflhkkgiiyrdlkldNVMLDSEGHIKIADFGMCKEHM 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 148 GD-LMTPQF--TPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSrtipkDM 224
Cdd:cd05615   163 VEgVTTRTFcgTPDYIAPEIIAYQ------------------PYGRSVDWWAYGVLLYEMLAGQPPFDGEDED-----EL 219
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1704602876 225 RRKIMTGSFEFPEeewsQISEMAKDVVRKLLKVKPEERL 263
Cdd:cd05615   220 FQSIMEHNVSYPK----SLSKEAVSICKGLMTKHPAKRL 254
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
28-277 5.48e-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: 66.22  E-value: 5.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKIL-LDRPKARNEVRLHMmcathpNIVQIIE----VFANSVQFPHESspRARLLIVM 102
Cdd:cd05605     8 LGKGGFGEVCACQVRATGKMYACKKLeKKRIKKRKGEAMAL------NEKQILEkvnsRFVVSLAYAYET--KDALCLVL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 103 EMMEGGEL-FHRISQHR-HFTEKQ----ASQVT----------------KQD-------APVKLCDFGFA-KIDQGDLMT 152
Cdd:cd05605    80 TIMNGGDLkFHIYNMGNpGFEEERavfyAAEITcglehlhserivyrdlKPEnillddhGHVRISDLGLAvEIPEGETIR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 153 PQF-TPYYVAPQVLEAQRrhqkeksgiiptsptpYTYnkSCDLWSLGVIIYVMLCGYPPFySKHHSRTIPKDMRRKIMtg 231
Cdd:cd05605   160 GRVgTVGYMAPEVVKNER----------------YTF--SPDWWGLGCLIYEMIEGQAPF-RARKEKVKREEVDRRVK-- 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1704602876 232 sfEFPEEEWSQISEMAKDVVRKLLKVKPEERL-----TIEGVLDHPWLNST 277
Cdd:cd05605   219 --EDQEEYSEKFSEEAKSICSQLLQKDPKTRLgcrgeGAEDVKSHPFFKSI 267
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
135-275 5.65e-12

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: 65.80  E-value: 5.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 135 VKLCDFGFAKIDQGDLMTPQF--TPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFY 212
Cdd:cd14201   153 IKIADFGFARYLQSNMMAATLcgSPMYMAPEVIMSQH------------------YDAKADLWSIGTVIYQCLVGKPPFQ 214
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1704602876 213 SKHhsrtiPKDMR---RKIMTGSFEFPEEEWSQISemakDVVRKLLKVKPEERLTIEGVLDHPWLN 275
Cdd:cd14201   215 ANS-----PQDLRmfyEKNKNLQPSIPRETSPYLA----DLLLGLLQRNQKDRMDFEAFFSHPFLE 271
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
28-273 6.51e-12

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: 65.42  E-value: 6.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILldrPKAR-------NEVRLHMMCATHPNIVQIIEVFANSVQ---FPHESSPR-- 95
Cdd:cd13987     1 LGEGTYGKVLLAVHKGSGTKMALKFV---PKPStklkdflREYNISLELSVHPHIIKTYDVAFETEDyyvFAQEYAPYgd 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  96 --------------------ARLLIVMEMMEGGELFHRisqhrhftEKQASQVTKQDAP---VKLCDFGFAKIdQGDLM- 151
Cdd:cd13987    78 lfsiippqvglpeervkrcaAQLASALDFMHSKNLVHR--------DIKPENVLLFDKDcrrVKLCDFGLTRR-VGSTVk 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 152 -----TPqftpyYVAPQVLEAqRRHQkeksgiiptsptPYTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHS----RTIPK 222
Cdd:cd13987   149 rvsgtIP-----YTAPEVCEA-KKNE------------GFVVDPSIDVWAFGVLLFCCLTGNFPWEKADSDdqfyEEFVR 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1704602876 223 DMRRKIMTgsfefPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGV---LDHPW 273
Cdd:cd13987   211 WQKRKNTA-----VPSQWRRFTPKALRMFKKLLAPEPERRCSIKEVfkyLGDRW 259
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
28-281 6.63e-12

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: 66.14  E-value: 6.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLHMMCATHPNIVQIIEVFANSVQFPHESSPRarLLIVMEMMEG 107
Cdd:cd05604     4 IGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDK--LYFVLDFVNG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 108 GELFHRISQHRHFTEKQASQVTKQDAP---------------------------VKLCDFGFAK--IDQGDlMTPQF--T 156
Cdd:cd05604    82 GELFFHLQRERSFPEPRARFYAAEIASalgylhsinivyrdlkpenilldsqghIVLTDFGLCKegISNSD-TTTTFcgT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 157 PYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDMRRKIMTGsfefp 236
Cdd:cd05604   161 PEYLAPEVIRKQ------------------PYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLR----- 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1704602876 237 eeewSQISEMAKDVVRKLLKVKPEERLTIEG----VLDHPWLNSTEALD 281
Cdd:cd05604   218 ----PGISLTAWSILEELLEKDRQLRLGAKEdfleIKNHPFFESINWTD 262
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
135-275 8.19e-12

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: 65.42  E-value: 8.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 135 VKLCDFGFAKIDQGDLMTPQF--TPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFY 212
Cdd:cd14202   149 IKIADFGFARYLQNNMMAATLcgSPMYMAPEVIMSQH------------------YDAKADLWSIGTIIYQCLTGKAPFQ 210
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1704602876 213 SkhhsrTIPKDMR---RKIMTGSFEFPEEEWSQIsemaKDVVRKLLKVKPEERLTIEGVLDHPWLN 275
Cdd:cd14202   211 A-----SSPQDLRlfyEKNKSLSPNIPRETSSHL----RQLLLGLLQRNQKDRMDFDEFFHHPFLD 267
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
28-274 8.54e-12

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: 65.27  E-value: 8.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILlDRPKA----------RNEVRLHMMcaTHPNIVQIIEVFANSvqfphesspRAR 97
Cdd:cd14164     8 IGEGSFSKVKLATSQKYCCKVAIKIV-DRRRAspdfvqkflpRELSILRRV--NHPNIVQMFECIEVA---------NGR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  98 LLIVMEMMEGgELFHRISQHRHFTEKQASQVTKQ----------------------------DAPVKLCDFGFAKIDQG- 148
Cdd:cd14164    76 LYIVMEAAAT-DLLQKIQEVHHIPKDLARDMFAQmvgavnylhdmnivhrdlkcenillsadDRKIKIADFGFARFVEDy 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 149 -DLMTpQF--TPYYVAPQVLEAqrrhqkeksgiIPTSPTPYtynkscDLWSLGVIIYVMLCGYPPFYSKHHSRtiPKDMR 225
Cdd:cd14164   155 pELST-TFcgSRAYTPPEVILG-----------TPYDPKKY------DVWSLGVVLYVMVTGTMPFDETNVRR--LRLQQ 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1704602876 226 RKIMtgsfeFPEEewSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14164   215 RGVL-----YPSG--VALEEPCRALIRTLLQFNPSTRPSIQQVAGNSWL 256
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
28-278 8.68e-12

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: 66.23  E-value: 8.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILldrpkaRNEVRLHMMCATHPNIVQIIEVFANS---VQFPHESSPRARLLIVMEM 104
Cdd:cd05627    10 IGRGAFGEVRLVQKKDTGHIYAMKIL------RKADMLEKEQVAHIRAERDILVEADGawvVKMFYSFQDKRNLYLIMEF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 105 MEGGELFHRISQHRHFTEKQ-----ASQVTKQDA----------------------PVKLCDFGFAKidqgDLMTPQFTP 157
Cdd:cd05627    84 LPGGDMMTLLMKKDTLSEEAtqfyiAETVLAIDAihqlgfihrdikpdnllldakgHVKLSDFGLCT----GLKKAHRTE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 158 YY----------VAPQVLEAQRRHQKEKSG--------------IIPTSPTPYTYNKSCDLWSLGVIIYVMLCGYPPFYS 213
Cdd:cd05627   160 FYrnlthnppsdFSFQNMNSKRKAETWKKNrrqlaystvgtpdyIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCS 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 214 KhhsrtIPKDMRRKIMT--GSFEFPEEewSQISEMAKDVVRKLLkVKPEERL---TIEGVLDHPWLNSTE 278
Cdd:cd05627   240 E-----TPQETYRKVMNwkETLVFPPE--VPISEKAKDLILRFC-TDAENRIgsnGVEEIKSHPFFEGVD 301
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
135-272 1.28e-11

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: 64.70  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 135 VKLCDFGFAKIDQGDLMTPQF--TPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFY 212
Cdd:cd14120   140 LKIADFGFARFLQDGMMAATLcgSPMYMAPEVIMSLQ------------------YDAKADLWSIGTIVYQCLTGKAPFQ 201
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 213 SKHhsrtiPKDMRRKIMTGSFEFPEEEwSQISEMAKDVVRKLLKVKPEERLTIEGVLDHP 272
Cdd:cd14120   202 AQT-----PQELKAFYEKNANLRPNIP-SGTSPALKDLLLGLLKRNPKDRIDFEDFFSHP 255
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
26-274 1.49e-11

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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: 64.81  E-value: 1.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALK-ILLDRPK------ARNEVRLhMMCATHPNIVQIIEVFANSvqfphessprARL 98
Cdd:cd07829     5 EKLGEGTYGVVYKAKDKKTGEIVALKkIRLDNEEegipstALREISL-LKELKHPNIVKLLDVIHTE----------NKL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  99 LIVMEMMEGgELFHRISQHR-HFTEKQASQVTKQ---------------------------DAPVKLCDFGFAKIDQGDL 150
Cdd:cd07829    74 YLVFEYCDQ-DLKKYLDKRPgPLPPNLIKSIMYQllrglaychshrilhrdlkpqnllinrDGVLKLADFGLARAFGIPL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 151 --MTPQF-TPYYVAPQVLEAQRrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHsrtipKDMRRK 227
Cdd:cd07829   153 rtYTHEVvTLWYRAPEILLGSK-----------------HYSTAVDIWSVGCIFAELITGKPLFPGDSE-----IDQLFK 210
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1704602876 228 ImtgsFEF----PEEEWSQISEM-------------------------AKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd07829   211 I----FQIlgtpTEESWPGVTKLpdykptfpkwpkndlekvlprldpeGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
97-276 1.67e-11

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: 64.64  E-value: 1.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  97 RLLIVMEMMEGGELFHRISQHRHFTE---------------------------KQASQVTKQDAPVKLCDFGFAKIDQGD 149
Cdd:cd05613    79 KLHLILDYINGGELFTHLSQRERFTEnevqiyigeivlalehlhklgiiyrdiKLENILLDSSGHVVLTDFGLSKEFLLD 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 150 LMTPQF----TPYYVAPQVLEAQrrhqkeKSGiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFY--SKHHSRTipkD 223
Cdd:cd05613   159 ENERAYsfcgTIEYMAPEIVRGG------DSG----------HDKAVDWWSLGVLMYELLTGASPFTvdGEKNSQA---E 219
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1704602876 224 MRRKIMTGSFEFPEEewsqISEMAKDVVRKLLKVKPEERL-----TIEGVLDHPWLNS 276
Cdd:cd05613   220 ISRRILKSEPPYPQE----MSALAKDIIQRLLMKDPKKRLgcgpnGADEIKKHPFFQK 273
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
28-272 1.74e-11

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 66.05  E-value: 1.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKIL-------LDRPKARNEVRLHMMC----------------ATHPNIVQIIEV--- 81
Cdd:PTZ00283   40 LGSGATGTVLCAKRVSDGEPFAVKVVdmegmseADKNRAQAEVCCLLNCdffsivkchedfakkdPRNPENVLMIALvld 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  82 FANSVQFPHESSPRARLLIVMEMMEGGELF--------HRISQHR-HFTEKQASQVTKQDAPVKLCDFGFAKI------- 145
Cdd:PTZ00283  120 YANAGDLRQEIKSRAKTNRTFREHEAGLLFiqvllavhHVHSKHMiHRDIKSANILLCSNGLVKLGDFGFSKMyaatvsd 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 146 DQGDlmTPQFTPYYVAPqvlEAQRRhqkeksgiiptspTPYTynKSCDLWSLGVIIYVMLCGYPPFYSKHHsrtipKDMR 225
Cdd:PTZ00283  200 DVGR--TFCGTPYYVAP---EIWRR-------------KPYS--KKADMFSLGVLLYELLTLKRPFDGENM-----EEVM 254
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1704602876 226 RKIMTGSFE-FPEEewsqISEMAKDVVRKLLKVKPEERLTIEGVLDHP 272
Cdd:PTZ00283  255 HKTLAGRYDpLPPS----ISPEMQEIVTALLSSDPKRRPSSSKLLNMP 298
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
26-285 1.93e-11

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: 64.74  E-value: 1.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKI--LLDRPKAR---NEVrLHMMCATHPNIVQIIEVFANSVQfphessprarLLI 100
Cdd:cd06656    25 EKIGQGASGTVYTAIDIATGQEVAIKQmnLQQQPKKEliiNEI-LVMRENKNPNIVNYLDSYLVGDE----------LWV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 101 VMEMMEGGEL--------------------------FHRISQHRHFTEKQASQVTKQDAPVKLCDFGF-AKI--DQGDLM 151
Cdd:cd06656    94 VMEYLAGGSLtdvvtetcmdegqiaavcreclqaldFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQItpEQSKRS 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 152 TPQFTPYYVAPQVLeaqrrhqkeksgiiptspTPYTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTipkdMRRKIMTG 231
Cdd:cd06656   174 TMVGTPYWMAPEVV------------------TRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRA----LYLIATNG 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1704602876 232 SFEFPEEEwsQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEALDNVLP 285
Cdd:cd06656   232 TPELQNPE--RLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAKPLSSLTP 283
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
25-274 2.02e-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: 64.42  E-value: 2.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  25 TQKLGAGISGPVRVCVKKSTQERFALKIL-LDRPK-----ARNEVRL--HMMCATHPNIVQ------------IIEVFAN 84
Cdd:cd06917     6 LELVGRGSYGAVYRGYHVKTGRVVALKVLnLDTDDddvsdIQKEVALlsQLKLGQPKNIIKyygsylkgpslwIIMDYCE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  85 --SVQFPHESSPRARL---LIVMEMMEGGELFHRISQ-HRHFteKQASQVTKQDAPVKLCDFGFA-KIDQGDLMTPQF-- 155
Cdd:cd06917    86 ggSIRTLMRAGPIAERyiaVIMREVLVALKFIHKDGIiHRDI--KAANILVTNTGNVKLCDFGVAaSLNQNSSKRSTFvg 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 156 TPYYVAPQVLEAQRrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPfYSKHhsrtipkDMRRKIM-TGSFE 234
Cdd:cd06917   164 TPYWMAPEVITEGK-----------------YYDTKADIWSLGITTYEMATGNPP-YSDV-------DALRAVMlIPKSK 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1704602876 235 FPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd06917   219 PPRLEGNGYSPLLKEFVAACLDEEPKDRLSADELLKSKWI 258
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
59-269 2.23e-11

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 65.42  E-value: 2.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  59 ARNEVRLHMMCaTHPNIVQIIEVFANSvqfphessprARLLIVMEMMEGGELFHRISQ----HRHFTEKQASQVTKQ--- 131
Cdd:PTZ00267  112 ARSELHCLAAC-DHFGIVKHFDDFKSD----------DKLLLIMEYGSGGDLNKQIKQrlkeHLPFQEYEVGLLFYQivl 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 132 ------------------------DAPVKLCDFGFAK--IDQGDL-MTPQF--TPYYVAPQVLEAQRrhqkeksgiipts 182
Cdd:PTZ00267  181 aldevhsrkmmhrdlksaniflmpTGIIKLGDFGFSKqySDSVSLdVASSFcgTPYYLAPELWERKR------------- 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 183 ptpytYNKSCDLWSLGVIIYVMLCGYPPFysKHHSRtipKDMRRKIMTGSFE-FPeeewSQISEMAKDVVRKLLKVKPEE 261
Cdd:PTZ00267  248 -----YSKKADMWSLGVILYELLTLHRPF--KGPSQ---REIMQQVLYGKYDpFP----CPVSSGMKALLDPLLSKNPAL 313

                  ....*...
gi 1704602876 262 RLTIEGVL 269
Cdd:PTZ00267  314 RPTTQQLL 321
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
27-274 2.70e-11

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: 63.44  E-value: 2.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  27 KLGAGISGPVRVCVKKSTQERFALKILL---DRPKARNEVRLHMMCaTHPNIVQIIEVFANSVQfphessprarLLIVME 103
Cdd:cd06612    10 KLGEGSYGSVYKAIHKETGQVVAIKVVPveeDLQEIIKEISILKQC-DSPYIVKYYGSYFKNTD----------LWIVME 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 104 MMEGGEL--FHRISQhRHFTEKQASQVTKQ---------------------------DAPVKLCDFGFAKI---DQGDLM 151
Cdd:cd06612    79 YCGAGSVsdIMKITN-KTLTEEEIAAILYQtlkgleylhsnkkihrdikagnillneEGQAKLADFGVSGQltdTMAKRN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 152 TPQFTPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIpkdmrrkIMTG 231
Cdd:cd06612   158 TVIGTPFWMAPEVIQEIG------------------YNNKADIWSLGITAIEMAEGKPPYSDIHPMRAI-------FMIP 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1704602876 232 -----SFEFPeEEWSQisEMaKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd06612   213 nkpppTLSDP-EKWSP--EF-NDFVKKCLVKDPEERPSAIQLLQHPFI 256
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
23-282 3.16e-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: 63.61  E-value: 3.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  23 NW--TQKLGAGISGPVRVCVKKSTQERFALKILldRPKARNEVRLHMM-------CaTHPNIVQIIEVFANsvqfphess 93
Cdd:cd06611     6 IWeiIGELGDGAFGKVYKAQHKETGLFAAAKII--QIESEEELEDFMVeidilseC-KHPNIVGLYEAYFY--------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  94 pRARLLIVMEMMEGGELFHRISQ-HRHFTEKQASQVTKQ---------------------------DAPVKLCDFGF-AK 144
Cdd:cd06611    74 -ENKLWILIEFCDGGALDSIMLElERGLTEPQIRYVCRQmlealnflhshkvihrdlkagnilltlDGDVKLADFGVsAK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 145 IDQGDLMTPQF--TPYYVAPQVLEAQRrhqkeksgiipTSPTPYTYNksCDLWSLGVIIYVMLCGYPPfyskhHSRTIPK 222
Cdd:cd06611   153 NKSTLQKRDTFigTPYWMAPEVVACET-----------FKDNPYDYK--ADIWSLGITLIELAQMEPP-----HHELNPM 214
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1704602876 223 DMRRKIMTG---SFEFPeEEWSqiSEMaKDVVRKLLKVKPEERLTIEGVLDHPWLNstEALDN 282
Cdd:cd06611   215 RVLLKILKSeppTLDQP-SKWS--SSF-NDFLKSCLVKDPDDRPTAAELLKHPFVS--DQSDN 271
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
28-274 3.18e-11

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: 64.64  E-value: 3.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKIL-----LDRPKA---RNE------------VRLHMMCATHPNIVQIIEVFANSVQ 87
Cdd:cd05624    80 IGRGAFGEVAVVKMKNTERIYAMKILnkwemLKRAETacfREErnvlvngdcqwiTTLHYAFQDENYLYLVMDYYVGGDL 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  88 FPHESSPRARLLIVMEMMEGGEL---FHRISQHR--HFTEKQASQVTKQDAPVKLCDFGFA-KIDQGDLMTPQF---TPY 158
Cdd:cd05624   160 LTLLSKFEDKLPEDMARFYIGEMvlaIHSIHQLHyvHRDIKPDNVLLDMNGHIRLADFGSClKMNDDGTVQSSVavgTPD 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 159 YVAPQVLEAQRRHQKEksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDMRRKimtGSFEFPeE 238
Cdd:cd05624   240 YISPEILQAMEDGMGK-------------YGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHE---ERFQFP-S 302
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1704602876 239 EWSQISEMAKDVVRKLLKVKpEERLTIEGVLD---HPWL 274
Cdd:cd05624   303 HVTDVSEEAKDLIQRLICSR-ERRLGQNGIEDfkkHAFF 340
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
59-273 3.49e-11

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: 63.49  E-value: 3.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  59 ARNEVRLHMMCaTHPNIVQIIEVFANSVqfphessprARLLIVMEMMEGGELFHRISQHRHFTEKQAS----QV------ 128
Cdd:cd13990    51 ALREYEIHKSL-DHPRIVKLYDVFEIDT---------DSFCTVLEYCDGNDLDFYLKQHKSIPEREARsiimQVvsalky 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 129 -TKQDAPV---------------------KLCDFGFAKI-------DQGDLMTPQF--TPYYVAPQVLEaqrrhqkeksg 177
Cdd:cd13990   121 lNEIKPPIihydlkpgnillhsgnvsgeiKITDFGLSKImddesynSDGMELTSQGagTYWYLPPECFV----------- 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 178 iipTSPTPYTYNKSCDLWSLGVIIYVMLCGYPPFyskHHSRTIPKDMRRKIMTGS--FEFPEEewSQISEMAKDVVRKLL 255
Cdd:cd13990   190 ---VGKTPPKISSKVDVWSVGVIFYQMLYGRKPF---GHNQSQEAILEENTILKAteVEFPSK--PVVSSEAKDFIRRCL 261
                         250
                  ....*....|....*...
gi 1704602876 256 KVKPEERLTIEGVLDHPW 273
Cdd:cd13990   262 TYRKEDRPDVLQLANDPY 279
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
28-268 4.22e-11

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: 64.29  E-value: 4.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILldrpkaRNEVRLHMMCATHPNIVQIIEVFANS---VQFPHESSPRARLLIVMEM 104
Cdd:cd05628     9 IGRGAFGEVRLVQKKDTGHVYAMKIL------RKADMLEKEQVGHIRAERDILVEADSlwvVKMFYSFQDKLNLYLIMEF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 105 MEGGELFHRISQHRHFTEKQ-----ASQVTKQDA----------------------PVKLCDFGFAKidqgDLMTPQFTP 157
Cdd:cd05628    83 LPGGDMMTLLMKKDTLTEEEtqfyiAETVLAIDSihqlgfihrdikpdnllldskgHVKLSDFGLCT----GLKKAHRTE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 158 YY-----VAPQVLEAQRRHQKEKSG-------------------IIPTSPTPYTYNKSCDLWSLGVIIYVMLCGYPPFYS 213
Cdd:cd05628   159 FYrnlnhSLPSDFTFQNMNSKRKAEtwkrnrrqlafstvgtpdyIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCS 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1704602876 214 KhhsrtIPKDMRRKIMT--GSFEFPEEewSQISEMAKDVVRKLLkVKPEERLTIEGV 268
Cdd:cd05628   239 E-----TPQETYKKVMNwkETLIFPPE--VPISEKAKDLILRFC-CEWEHRIGAPGV 287
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
28-273 4.97e-11

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: 63.41  E-value: 4.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILlDRPKARNEVRLHMMCA--------THPNIVQIIEVFANSvqfphessprARLL 99
Cdd:cd05574     9 LGKGDVGRVYLVRLKGTGKLFAMKVL-DKEEMIKRNKVKRVLTereilatlDHPFLPTLYASFQTS----------THLC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMEGGELFH-RISQ-HRHFTEKQ----ASQVT-----------------------KQDAPVKLCDFGFAKidQGDL 150
Cdd:cd05574    78 FVMDYCPGGELFRlLQKQpGKRLPEEVarfyAAEVLlaleylhllgfvyrdlkpenillHESGHIMLTDFDLSK--QSSV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 151 MTPQftpyyVAPQVLEAQRRHQKEKSGIIPTSPTPYTYNKSC---------------------DLWSLGVIIYVMLCGYP 209
Cdd:cd05574   156 TPPP-----VRKSLRKGSRRSSVKSIEKETFVAEPSARSNSFvgteeyiapevikgdghgsavDWWTLGILLYEMLYGTT 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1704602876 210 PFYSKHHSRTIpkdmrRKIMTGSFEFPEEewSQISEMAKDVVRKLLKVKPEERL-TIEGVLD---HPW 273
Cdd:cd05574   231 PFKGSNRDETF-----SNILKKELTFPES--PPVSSEAKDLIRKLLVKDPSKRLgSKRGASEikrHPF 291
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
26-285 5.50e-11

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: 63.20  E-value: 5.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKI--LLDRPKAR---NEVrLHMMCATHPNIVQIIEVFANSVQfphessprarLLI 100
Cdd:cd06655    25 EKIGQGASGTVFTAIDVATGQEVAIKQinLQKQPKKEliiNEI-LVMKELKNPNIVNFLDSFLVGDE----------LFV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 101 VMEMMEGGEL--------------------------FHRISQHRHFTEKQASQVTKQDAPVKLCDFGF-AKI--DQGDLM 151
Cdd:cd06655    94 VMEYLAGGSLtdvvtetcmdeaqiaavcreclqaleFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFcAQItpEQSKRS 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 152 TPQFTPYYVAPQVLeaqrrhqkeksgiiptspTPYTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTipkdMRRKIMTG 231
Cdd:cd06655   174 TMVGTPYWMAPEVV------------------TRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRA----LYLIATNG 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1704602876 232 SFEFPEEEwsQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEALDNVLP 285
Cdd:cd06655   232 TPELQNPE--KLSPIFRDFLNRCLEMDVEKRGSAKELLQHPFLKLAKPLSSLTP 283
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
27-274 6.43e-11

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 62.72  E-value: 6.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  27 KLGAGISGPVRVCVKKSTQERFALKILLDRP-------KARNEVRLhMMCATHPNIVQIIEVF--ANSVQFPHESSPRAr 97
Cdd:cd07833     8 VVGEGAYGVVLKCRNKATGEIVAIKKFKESEddedvkkTALREVKV-LRQLRHENIVNLKEAFrrKGRLYLVFEYVERT- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  98 LLIVMEMMEGG-----------ELFHRISQ-HR----HFTEKQASQVTKQDAPVKLCDFGFAKIDQGDlMTPQFTPY--- 158
Cdd:cd07833    86 LLELLEASPGGlppdavrsyiwQLLQAIAYcHShniiHRDIKPENILVSESGVLKLCDFGFARALTAR-PASPLTDYvat 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 159 --YVAPQVLeaqrrhqkeksgiipTSPTPytYNKSCDLWSLGVIIYVMLCGYPPFYSKHH-------SRTI-PKDMRRKI 228
Cdd:cd07833   165 rwYRAPELL---------------VGDTN--YGKPVDVWAIGCIMAELLDGEPLFPGDSDidqlyliQKCLgPLPPSHQE 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1704602876 229 MTGS------FEFPEEEWSQ---------ISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd07833   228 LFSSnprfagVAFPEPSQPEslerrypgkVSSPALDFLKACLRMDPKERLTCDELLQHPYF 288
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
98-278 6.46e-11

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 63.46  E-value: 6.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  98 LLIVMEMMEGGELFHRISQHRHFTEK----QASQVT-----------------------KQDAPVKLCDFGFAKIDQGDL 150
Cdd:PTZ00426  106 LYLVLEFVIGGEFFTFLRRNKRFPNDvgcfYAAQIVlifeylqslnivyrdlkpenlllDKDGFIKMTDFGFAKVVDTRT 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 151 MTPQFTPYYVAPQVLeaqrrhqkeksgiiptspTPYTYNKSCDLWSLGVIIYVMLCGYPPFYSKHhsrtiPKDMRRKIMT 230
Cdd:PTZ00426  186 YTLCGTPEYIAPEIL------------------LNVGHGKAADWWTLGIFIYEILVGCPPFYANE-----PLLIYQKILE 242
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1704602876 231 GSFEFPEeewsQISEMAKDVVRKLLKVKPEERL-----TIEGVLDHPWLNSTE 278
Cdd:PTZ00426  243 GIIYFPK----FLDNNCKHLMKKLLSHDLTKRYgnlkkGAQNVKEHPWFGNID 291
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
28-272 7.30e-11

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


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 62.44  E-value: 7.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALK-ILLD------RPKARNEVRLHMMCaTHPNIVQIIEVFANSvqfphesspRArLLI 100
Cdd:cd08220     8 VGRGAYGTVYLCRRKDDNKLVIIKqIPVEqmtkeeRQAALNEVKVLSML-HHPNIIEYYESFLED---------KA-LMI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 101 VMEMMEGGELFHRISQHR---------------------HFTEKQ------ASQ---VTKQDAPVKLCDFGFAKI--DQG 148
Cdd:cd08220    77 VMEYAPGGTLFEYIQQRKgsllseeeilhffvqillalhHVHSKQilhrdlKTQnilLNKKRTVVKIGDFGISKIlsSKS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 149 DLMTPQFTPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFyskhHSRTIPKdMRRKI 228
Cdd:cd08220   157 KAYTVVGTPCYISPELCEGK------------------PYNQKSDIWALGCVLYELASLKRAF----EAANLPA-LVLKI 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1704602876 229 MTGSFEFPEEEWsqiSEMAKDVVRKLLKVKPEERLTIEGVLDHP 272
Cdd:cd08220   214 MRGTFAPISDRY---SEELRHLILSMLHLDPNKRPTLSEIMAQP 254
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
28-278 7.43e-11

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: 63.33  E-value: 7.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLHMMC-------ATHPNIVQIIEVFANSvqfphessprARLLI 100
Cdd:cd05629     9 IGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQLAHVKAerdvlaeSDSPWVVSLYYSFQDA----------QYLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 101 VMEMMEGGELFHRISQHRHFTE---------------------------KQASQVTKQDAPVKLCDFG------------ 141
Cdd:cd05629    79 IMEFLPGGDLMTMLIKYDTFSEdvtrfymaecvlaieavhklgfihrdiKPDNILIDRGGHIKLSDFGlstgfhkqhdsa 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 142 -FAKIDQGDLMTPQF-------------------------------------TPYYVAPQVLEAQrrhqkeksgiiptsp 183
Cdd:cd05629   159 yYQKLLQGKSNKNRIdnrnsvavdsinltmsskdqiatwkknrrlmaystvgTPDYIAPEIFLQQ--------------- 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 184 tpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHhsrtiPKDMRRKIMT--GSFEFPEEewSQISEMAKDVVRKLLkVKPEE 261
Cdd:cd05629   224 ---GYGQECDWWSLGAIMFECLIGWPPFCSEN-----SHETYRKIINwrETLYFPDD--IHLSVEAEDLIRRLI-TNAEN 292
                         330       340
                  ....*....|....*....|
gi 1704602876 262 RLTIEGVLD---HPWLNSTE 278
Cdd:cd05629   293 RLGRGGAHEiksHPFFRGVD 312
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
28-272 8.98e-11

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: 62.32  E-value: 8.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKIL-LDRPKARnevRLHMMCATHPNIVQIIEV-FANSVQFPHESspRARLLIVMEMM 105
Cdd:cd05631     8 LGKGGFGEVCACQVRATGKMYACKKLeKKRIKKR---KGEAMALNEKRILEKVNSrFVVSLAYAYET--KDALCLVLTIM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 106 EGGEL-FHRISQ-HRHFTEKQA----------------SQVTKQD-----------APVKLCDFGFA-KIDQGDLMTPQF 155
Cdd:cd05631    83 NGGDLkFHIYNMgNPGFDEQRAifyaaelccgledlqrERIVYRDlkpenillddrGHIRISDLGLAvQIPEGETVRGRV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 156 -TPYYVAPQVLEAQRrhqkeksgiiptsptpYTYnkSCDLWSLGVIIYVMLCGYPPFySKHHSRTIPKDMRRKIMTGSFE 234
Cdd:cd05631   163 gTVGYMAPEVINNEK----------------YTF--SPDWWGLGCLIYEMIQGQSPF-RKRKERVKREEVDRRVKEDQEE 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1704602876 235 FPEeewsQISEMAKDVVRKLLKVKPEERLTIEG-----VLDHP 272
Cdd:cd05631   224 YSE----KFSEDAKSICRMLLTKNPKERLGCRGngaagVKQHP 262
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
36-274 1.18e-10

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: 61.86  E-value: 1.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  36 VRVCVKKSTQERFALKILLDRPKARNEV--------RLHmmcatHPNIVQIIEVFAnsvqfphesSPRaRLLIVMEMMEG 107
Cdd:cd14110    19 VRQCEEKRSGQMLAAKIIPYKPEDKQLVlreyqvlrRLS-----HPRIAQLHSAYL---------SPR-HLVLIEELCSG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 108 GELFHRISQHRHFTEKQASQVTKQDAP---------------------------VKLCDFGFAK-IDQGD-LMTPQFTpY 158
Cdd:cd14110    84 PELLYNLAERNSYSEAEVTDYLWQILSavdylhsrrilhldlrsenmiiteknlLKIVDLGNAQpFNQGKvLMTDKKG-D 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 159 YV---APQVLEAQrrhqkeksGIIPTSptpytynkscDLWSLGVIIYVMLCGYPPFYSKhhsrtIPKDMRRKIMTGSFEF 235
Cdd:cd14110   163 YVetmAPELLEGQ--------GAGPQT----------DIWAIGVTAFIMLSADYPVSSD-----LNWERDRNIRKGKVQL 219
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1704602876 236 pEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14110   220 -SRCYAGLSGGAVNFLKSTLCAKPWGRPTASECLQNPWL 257
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
28-269 1.19e-10

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: 61.53  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALK-ILL-----DRPKARNE-VRLHMMcaTHPNIVQIIEVFANSvqfphessprARLLI 100
Cdd:cd08219     8 VGEGSFGRALLVQHVNSDQKYAMKeIRLpksssAVEDSRKEaVLLAKM--KHPNIVAFKESFEAD----------GHLYI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 101 VMEMMEGGELFHRISQHRH--FTE---------------------------KQASQVTKQDAPVKLCDFGFAKIdqgdLM 151
Cdd:cd08219    76 VMEYCDGGDLMQKIKLQRGklFPEdtilqwfvqmclgvqhihekrvlhrdiKSKNIFLTQNGKVKLGDFGSARL----LT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 152 TPQF-------TPYYVAPQVLEAqrrhqkeksgiIPtsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHsrtipKDM 224
Cdd:cd08219   152 SPGAyactyvgTPYYVPPEIWEN-----------MP-------YNNKSDIWSLGCILYELCTLKHPFQANSW-----KNL 208
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1704602876 225 RRKIMTGSFE-FPeeewSQISEMAKDVVRKLLKVKPEERLTIEGVL 269
Cdd:cd08219   209 ILKVCQGSYKpLP----SHYSYELRSLIKQMFKRNPRSRPSATTIL 250
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
101-274 1.23e-10

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: 61.76  E-value: 1.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 101 VMEMMEGGELFHrisQHR--HFTEKQASQVTKQDAPVKLCDFGFAK------IDQGDLMTPqfTPYYVAPQVLEAQrrhq 172
Cdd:cd14111   105 LVQILQGLEYLH---GRRvlHLDIKPDNIMVTNLNAIKIVDFGSAQsfnplsLRQLGRRTG--TLEYMAPEMVKGE---- 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 173 keksgiiPTSPtpytynkSCDLWSLGVIIYVMLCGYPPFYSKHhsrtiPKDMRRKIMTGSFEfPEEEWSQISEMAKDVVR 252
Cdd:cd14111   176 -------PVGP-------PADIWSIGVLTYIMLSGRSPFEDQD-----PQETEAKILVAKFD-AFKLYPNVSQSASLFLK 235
                         170       180
                  ....*....|....*....|..
gi 1704602876 253 KLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14111   236 KVLSSYPWSRPTTKDCFAHAWL 257
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
26-285 1.40e-10

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: 62.05  E-value: 1.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKI--LLDRPKAR---NEVrLHMMCATHPNIVQIIEVFANSVQfphessprarLLI 100
Cdd:cd06654    26 EKIGQGASGTVYTAMDVATGQEVAIRQmnLQQQPKKEliiNEI-LVMRENKNPNIVNYLDSYLVGDE----------LWV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 101 VMEMMEGGEL--------------------------FHRISQHRHFTEKQASQVTKQDAPVKLCDFGF-AKI--DQGDLM 151
Cdd:cd06654    95 VMEYLAGGSLtdvvtetcmdegqiaavcreclqaleFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQItpEQSKRS 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 152 TPQFTPYYVAPQVLeaqrrhqkeksgiiptspTPYTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTipkdMRRKIMTG 231
Cdd:cd06654   175 TMVGTPYWMAPEVV------------------TRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRA----LYLIATNG 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1704602876 232 SFEFPEEEwsQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEALDNVLP 285
Cdd:cd06654   233 TPELQNPE--KLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTP 284
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
26-269 1.40e-10

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


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 61.54  E-value: 1.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKIL------LDRPKARNEVRLHMmCATHPNIVQIievFANSVQFPHessprarLL 99
Cdd:cd13996    12 ELLGSGGFGSVYKVRNKVDGVTYAIKKIrlteksSASEKVLREVKALA-KLNHPNIVRY---YTAWVEEPP-------LY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMEGGELFHRISQHRHFT---EKQASQVTKQ----------------------------DAPVKLCDFGFAK---- 144
Cdd:cd13996    81 IQMELCEGGTLRDWIDRRNSSSkndRKLALELFKQilkgvsyihskgivhrdlkpsnifldndDLQVKIGDFGLATsign 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 145 --IDQGDLMTPQF-----------TPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCgypPF 211
Cdd:cd13996   161 qkRELNNLNNNNNgntsnnsvgigTPLYASPEQLDGEN------------------YNEKADIYSLGIILFEMLH---PF 219
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 212 YSKHHSRTIPKDMRRKIMTGSF--EFPEEewsqisemaKDVVRKLLKVKPEERLTIEGVL 269
Cdd:cd13996   220 KTAMERSTILTDLRNGILPESFkaKHPKE---------ADLIQSLLSKNPEERPSAEQLL 270
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
132-274 1.43e-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: 61.55  E-value: 1.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 132 DAPVKLCDFGF-AKID--QGDLMTPQFTPYYVAPQVLEAQRrhqkeksgiiptSPTpYTYNKSCDLWSLGVIIYVMLCGY 208
Cdd:cd06608   149 EAEVKLVDFGVsAQLDstLGRRNTFIGTPYWMAPEVIACDQ------------QPD-ASYDARCDVWSLGITAIELADGK 215
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1704602876 209 PPFYSKHHSRT---IPKDMRRKIMtgsfefPEEEWSQiseMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd06608   216 PPLCDMHPMRAlfkIPRNPPPTLK------SPEKWSK---EFNDFISECLIKNYEQRPFTEELLEHPFI 275
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
44-270 1.49e-10

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: 61.76  E-value: 1.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  44 TQERFALKILLDRPKARN-----EVRLHMMCATHPNIVQIIEvfANSVQFPHESSPRARLLIVMEMMEGG--ELFHRISQ 116
Cdd:cd14036    24 TGKEYALKRLLSNEEEKNkaiiqEINFMKKLSGHPNIVQFCS--AASIGKEESDQGQAEYLLLTELCKGQlvDFVKKVEA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 117 HRHF-----------TEKQASQVTKQDAPV------------------KLCDFGFAKidqgdlmTPQFTPYYVapqvLEA 167
Cdd:cd14036   102 PGPFspdtvlkifyqTCRAVQHMHKQSPPIihrdlkienllignqgqiKLCDFGSAT-------TEAHYPDYS----WSA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 168 QRRHQKEKSGIIPTSP---TP--------YTYNKSCDLWSLGVIIYvMLCgyppfYSKHhsrTIPKDMRRKIMTGSFEFP 236
Cdd:cd14036   171 QKRSLVEDEITRNTTPmyrTPemidlysnYPIGEKQDIWALGCILY-LLC-----FRKH---PFEDGAKLRIINAKYTIP 241
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1704602876 237 EEEWSQisEMAKDVVRKLLKVKPEERLTIEGVLD 270
Cdd:cd14036   242 PNDTQY--TVFHDLIRSTLKVNPEERLSITEIVE 273
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
26-276 1.69e-10

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: 62.28  E-value: 1.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKILLdRP--------KARNEVRL--HMmcaTHPNIVQIIEVFANSVQF------- 88
Cdd:cd07880    21 KQVGSGAYGTVCSALDRRTGAKVAIKKLY-RPfqselfakRAYRELRLlkHM---KHENVIGLLDVFTPDLSLdrfhdfy 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  89 --------------PHESSPRARL-LIVMEMMEGGELFHRISQ-HRHFteKQASQVTKQDAPVKLCDFGFAKIDQGDLMT 152
Cdd:cd07880    97 lvmpfmgtdlgklmKHEKLSEDRIqFLVYQMLKGLKYIHAAGIiHRDL--KPGNLAVNEDCELKILDFGLARQTDSEMTG 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 153 PQFTPYYVAPQVLEAQRRhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHH----------SRTIPK 222
Cdd:cd07880   175 YVVTRWYRAPEVILNWMH-----------------YTQTVDIWSVGCIMAEMLTGKPLFKGHDHldqlmeimkvTGTPSK 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1704602876 223 DMRRKI--------MTGSFEFPEEEWSQI----SEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNS 276
Cdd:cd07880   238 EFVQKLqsedaknyVKKLPRFRKKDFRSLlpnaNPLAVNVLEKMLVLDAESRITAAEALAHPYFEE 303
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
28-276 1.80e-10

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


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 62.23  E-value: 1.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKiLLDRP--------KARNEVRL--HMmcaTHPNIVQIIEVFANSVQFP-------- 89
Cdd:cd07879    23 VGSGAYGSVCSAIDKRTGEKVAIK-KLSRPfqseifakRAYRELTLlkHM---QHENVIGLLDVFTSAVSGDefqdfylv 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  90 -------------HESSPRARLLIVMEMMEGGELFHRISQ-HRHFteKQASQVTKQDAPVKLCDFGFAKIDQGDLMTPQF 155
Cdd:cd07879    99 mpymqtdlqkimgHPLSEDKVQYLVYQMLCGLKYIHSAGIiHRDL--KPGNLAVNEDCELKILDFGLARHADAEMTGYVV 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 156 TPYYVAPQVLEAQRRhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPK------------- 222
Cdd:cd07879   177 TRWYRAPEVILNWMH-----------------YNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQilkvtgvpgpefv 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1704602876 223 ----DMRRKIMTGSF-EFPEEEWSQI----SEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNS 276
Cdd:cd07879   240 qkleDKAAKSYIKSLpKYPRKDFSTLfpkaSPQAVDLLEKMLELDVDKRLTATEALEHPYFDS 302
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
135-271 2.32e-10

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: 60.71  E-value: 2.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 135 VKLCDFGFA-KIDQGDLMTPQF--TPYYVAPQVLEAQrrhqkeksGIIPTSptpytynkscDLWSLGVIIYVMLCGYPPF 211
Cdd:cd14189   140 LKVGDFGLAaRLEPPEQRKKTIcgTPNYLAPEVLLRQ--------GHGPES----------DVWSLGCVMYTLLCGNPPF 201
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 212 YSKHHsrtipKDMRRKIMTGSFEFPeeewSQISEMAKDVVRKLLKVKPEERLTIEGVLDH 271
Cdd:cd14189   202 ETLDL-----KETYRCIKQVKYTLP----ASLSLPARHLLAGILKRNPGDRLTLDQILEH 252
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
28-278 2.40e-10

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: 60.91  E-value: 2.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKiLLDRPK---------ARNEVRLHMMCATH---PNIVQIIEVFansvQFPHesspr 95
Cdd:cd05606     2 IGRGGFGEVYGCRKADTGKMYAMK-CLDKKRikmkqgetlALNERIMLSLVSTGgdcPFIVCMTYAF----QTPD----- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  96 aRLLIVMEMMEGGELFHRISQHRHFTEKQ----ASQVTK---------------QDAPVKLCDFGFAKIDqgDL-MTPQF 155
Cdd:cd05606    72 -KLCFILDLMNGGDLHYHLSQHGVFSEAEmrfyAAEVILglehmhnrfivyrdlKPANILLDEHGHVRIS--DLgLACDF 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 156 ----------TPYYVAPQVLeaqrrhQKeksGIiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFysKHHSRTIPKDMR 225
Cdd:cd05606   149 skkkphasvgTHGYMAPEVL------QK---GV--------AYDSSADWFSLGCMLYKLLKGHSPF--RQHKTKDKHEID 209
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1704602876 226 RKIMTGSFEFPeEEWSqiSEMaKDVVRKLLKVKPEERLTIEG-----VLDHPWLNSTE 278
Cdd:cd05606   210 RMTLTMNVELP-DSFS--PEL-KSLLEGLLQRDVSKRLGCLGrgateVKEHPFFKGVD 263
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
26-273 3.01e-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: 60.96  E-value: 3.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALK-ILLDRPK-----ARNEVRLhMMCATHPNIVQIIEVFansvqfpHESSpraRLL 99
Cdd:cd07836     6 EKLGEGTYATVYKGRNRTTGEIVALKeIHLDAEEgtpstAIREISL-MKELKHENIVRLHDVI-------HTEN---KLM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMEGG------------------------ELFHRIS---QHR--HFTEKQASQVTKQDAPVKLCDFGFAK---IDQ 147
Cdd:cd07836    75 LVFEYMDKDlkkymdthgvrgaldpntvksftyQLLKGIAfchENRvlHRDLKPQNLLINKRGELKLADFGLARafgIPV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 148 GDLMTPQFTPYYVAPQVLEAQRrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDMRrk 227
Cdd:cd07836   155 NTFSNEVVTLWYRAPDVLLGSR-----------------TYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFR-- 215
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1704602876 228 IMtGSfefPEEE-WSQISEMAK-------------------------DVVRKLLKVKPEERLTIEGVLDHPW 273
Cdd:cd07836   216 IM-GT---PTEStWPGISQLPEykptfpryppqdlqqlfphadplgiDLLHRLLQLNPELRISAHDALQHPW 283
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
22-274 3.07e-10

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: 60.47  E-value: 3.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  22 INWT--QKLGAGISGPVRVCVKKSTQERFALK-ILLDRPKA-RNEVRLHMMCAT------------HPNIVQIIEvFANS 85
Cdd:cd06629     1 FKWVkgELIGKGTYGRVYLAMNATTGEMLAVKqVELPKTSSdRADSRQKTVVDAlkseidtlkdldHPNIVQYLG-FEET 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  86 VQFphessprarLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ---------------------------DAPVKLC 138
Cdd:cd06629    80 EDY---------FSIFLEYVPGGSIGSCLRKYGKFEEDLVRFFTRQildglaylhskgilhrdlkadnilvdlEGICKIS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 139 DFGFAK-----IDQGDLMTPQFTPYYVAPQVLEAQRRhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYS 213
Cdd:cd06629   151 DFGISKksddiYGNNGATSMQGSVFWMAPEVIHSQGQ----------------GYSAKVDIWSLGCVVLEMLAGRRPWSD 214
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1704602876 214 KHHSRTIpkdmrRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd06629   215 DEAIAAM-----FKLGNKRSAPPVPEDVNLSPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
7-276 3.74e-10

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 60.26  E-value: 3.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876   7 MDKAIKE-TSILEEYSINWTQKLGAGISGPVRVCVKKSTQERFALKILldRPKARN--EVRLHMMCATHPNIVQIIevfa 83
Cdd:PHA03390    2 MDKSLSElVQFLKNCEIVKKLKLIDGKFGKVSVLKHKPTQKLFVQKII--KAKNFNaiEPMVHQLMKDNPNFIKLY---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  84 NSVqfpheSSPRARLLIvMEMMEGGELFHRISQHRHFTEKQASQVTKQ--DA--------------------------PV 135
Cdd:PHA03390   76 YSV-----TTLKGHVLI-MDYIKDGDLFDLLKKEGKLSEAEVKKIIRQlvEAlndlhkhniihndiklenvlydrakdRI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 136 KLCDFGFAKIDQgdlmTPQF---TPYYVAPqvlEAQRRHQkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCG-YPpf 211
Cdd:PHA03390  150 YLCDYGLCKIIG----TPSCydgTLDYFSP---EKIKGHN---------------YDVSFDWWAVGVLTYELLTGkHP-- 205
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1704602876 212 YSKHHSRTI-PKDMRRKImTGSFEFPeeewSQISEMAKDVVRKLLKVKPEERL-TIEGVLDHPWLNS 276
Cdd:PHA03390  206 FKEDEDEELdLESLLKRQ-QKKLPFI----KNVSKNANDFVQSMLKYNINYRLtNYNEIIKHPFLKI 267
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
26-272 3.97e-10

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: 60.06  E-value: 3.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKIL-LDRPKA-----RNEVRLHMMCAtHPNIVQIIEVFansvqfphesSPRARLL 99
Cdd:cd06610     7 EVIGSGATAVVYAAYCLPKKEKVAIKRIdLEKCQTsmdelRKEIQAMSQCN-HPNVVSYYTSF----------VVGDELW 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMEGGELFHrISQHRH----FTEKQASQVTK---------------------------QDAPVKLCDFGF-AKIDQ 147
Cdd:cd06610    76 LVMPLLSGGSLLD-IMKSSYprggLDEAIIATVLKevlkgleylhsngqihrdvkagnillgEDGSVKIADFGVsASLAT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 148 GDLMTPQF------TPYYVAPQVLEAQRrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPfYSKHhsrtip 221
Cdd:cd06610   155 GGDRTRKVrktfvgTPCWMAPEVMEQVR-----------------GYDFKADIWSFGITAIELATGAAP-YSKY------ 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1704602876 222 KDMRRKIMTGSFEFP----EEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHP 272
Cdd:cd06610   211 PPMKVLMLTLQNDPPsletGADYKKYSKSFRKMISLCLQKDPSKRPTAEELLKHK 265
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
28-211 4.38e-10

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: 60.54  E-value: 4.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALK---ILL---DRPKAR--NEVRLhMMCATHPNIVQiievfANSVQFPHESSPRARL- 98
Cdd:cd13989     1 LGSGGFGYVTLWKHQDTGEYVAIKkcrQELspsDKNRERwcLEVQI-MKKLNHPNVVS-----ARDVPPELEKLSPNDLp 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  99 LIVMEMMEGGELFHRISQ--------------------------------HRHFT-EKQASQVTKQDAPVKLCDFGFAK- 144
Cdd:cd13989    75 LLAMEYCSGGDLRKVLNQpenccglkesevrtllsdissaisylhenriiHRDLKpENIVLQQGGGRVIYKLIDLGYAKe 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1704602876 145 IDQGDLMTpQF--TPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPF 211
Cdd:cd13989   155 LDQGSLCT-SFvgTLQYLAPELFESKK------------------YTCTVDYWSFGTLAFECITGYRPF 204
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
28-263 4.42e-10

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: 60.78  E-value: 4.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILldrpK-----ARNEVRlHMMC----------ATHPNIVQIIEVFansvQFPHEs 92
Cdd:cd05589     7 LGRGHFGKVLLAEYKPTGELFAIKAL----KkgdiiARDEVE-SLMCekrifetvnsARHPFLVNLFACF----QTPEH- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  93 sprarLLIVMEMMEGGELFHRISQHRhFTEKQ----ASQVT-----------------------KQDAPVKLCDFGFAK- 144
Cdd:cd05589    77 -----VCFVMEYAAGGDLMMHIHEDV-FSEPRavfyAACVVlglqflhehkivyrdlkldnlllDTEGYVKIADFGLCKe 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 145 -IDQGDlMTPQF--TPYYVAPQVLeaqrrhqkeksgiiptspTPYTYNKSCDLWSLGVIIYVMLCGYPPFyskhhsrtiP 221
Cdd:cd05589   151 gMGFGD-RTSTFcgTPEFLAPEVL------------------TDTSYTRAVDWWGLGVLIYEMLVGESPF---------P 202
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1704602876 222 KDMRRK----IMTGSFEFPEeewsQISEMAKDVVRKLLKVKPEERL 263
Cdd:cd05589   203 GDDEEEvfdsIVNDEVRYPR----FLSTEAISIMRRLLRKNPERRL 244
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
72-274 6.10e-10

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


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 59.98  E-value: 6.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  72 HPNIVQIIEVFANsVQFPHESSprarLLIVME-----------------------------MMEGGELFH--RISqHRHF 120
Cdd:cd07838    60 HPNVVRLLDVCHG-PRTDRELK----LTLVFEhvdqdlatyldkcpkpglppetikdlmrqLLRGLDFLHshRIV-HRDL 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 121 teKQASQVTKQDAPVKLCDFGFAKI-DQGDLMTPQF-TPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLG 198
Cdd:cd07838   134 --KPQNILVTSDGQVKLADFGLARIySFEMALTSVVvTLWYRAPEVLLQS------------------SYATPVDMWSVG 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 199 VIIYVMLCGYPPFYSKHHsrtipKDMRRKImtgsFEF----PEEEWSQ-----------------------ISEMAKDVV 251
Cdd:cd07838   194 CIFAELFNRRPLFRGSSE-----ADQLGKI----FDViglpSEEEWPRnsalprssfpsytprpfksfvpeIDEEGLDLL 264
                         250       260
                  ....*....|....*....|...
gi 1704602876 252 RKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd07838   265 KKMLTFNPHKRISAFEALQHPYF 287
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
27-276 8.40e-10

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


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 59.66  E-value: 8.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  27 KLGAGISGPVRVCVKKSTQERFALKILldRPKARNEVRLHMM------CATHPNIVQIIEVFAnsvqfpHESspraRLLI 100
Cdd:cd06643    12 ELGDGAFGKVYKAQNKETGILAAAKVI--DTKSEEELEDYMVeidilaSCDHPNIVKLLDAFY------YEN----NLWI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 101 VMEMMEGGELFHRISQ-HRHFTEKQASQVTKQ---------------------------DAPVKLCDFGFAKIDQGDLMT 152
Cdd:cd06643    80 LIEFCAGGAVDAVMLElERPLTEPQIRVVCKQtlealvylhenkiihrdlkagnilftlDGDIKLADFGVSAKNTRTLQR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 153 -PQF--TPYYVAPQVLEAQRRHQKeksgiiptsptPYTYNksCDLWSLGVIIYVMLCGYPPfyskHHSRTipkDMRRKIM 229
Cdd:cd06643   160 rDSFigTPYWMAPEVVMCETSKDR-----------PYDYK--ADVWSLGVTLIEMAQIEPP----HHELN---PMRVLLK 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1704602876 230 TGSFEFPE-EEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNS 276
Cdd:cd06643   220 IAKSEPPTlAQPSRWSPEFKDFLRKCLEKNVDARWTTSQLLQHPFVSV 267
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
26-274 9.30e-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: 9.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVR--LHMMCathpnivqiiEVFANSVQFPHESSPRARLLIVME 103
Cdd:cd14108     8 KEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTSARreLALLA----------ELDHKSIVRFHDAFEKRRVVIIVT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 104 MMEGGELFHRISQHRHFTEKQASQVTKQ-----------------------------DAPVKLCDFGFA-KIDQGDLMTP 153
Cdd:cd14108    78 ELCHEELLERITKRPTVCESEVRSYMRQllegieylhqndvlhldlkpenllmadqkTDQVRICDFGNAqELTPNEPQYC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 154 QF-TPYYVAPQvleaqrrhqkeksgIIPTSPTpytyNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIpkdmrRKIMTGS 232
Cdd:cd14108   158 KYgTPEFVAPE--------------IVNQSPV----SKVTDIWPVGVIAYLCLTGISPFVGENDRTTL-----MNIRNYN 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1704602876 233 FEFPEEEWSQISEMAKDVVRKLLkVKPEERLTIEGVLDHPWL 274
Cdd:cd14108   215 VAFEESMFKDLCREAKGFIIKVL-VSDRLRPDAEETLEHPWF 255
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
28-272 1.19e-09

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: 58.88  E-value: 1.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKIL-LDRPKARNEVRLHMmcathpNIVQIIEV----FANSVQFPHESspRARLLIVM 102
Cdd:cd05630     8 LGKGGFGEVCACQVRATGKMYACKKLeKKRIKKRKGEAMAL------NEKQILEKvnsrFVVSLAYAYET--KDALCLVL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 103 EMMEGGEL-FHRISQ-HRHFTEKQA---------------------------SQVTKQDAPVKLCDFGFA-KIDQGDLMT 152
Cdd:cd05630    80 TLMNGGDLkFHIYHMgQAGFPEARAvfyaaeiccgledlhrerivyrdlkpeNILLDDHGHIRISDLGLAvHVPEGQTIK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 153 PQF-TPYYVAPQVLEAQRrhqkeksgiiptsptpYTYnkSCDLWSLGVIIYVMLCGYPPFysKHHSRTIPKDMRRKIMTg 231
Cdd:cd05630   160 GRVgTVGYMAPEVVKNER----------------YTF--SPDWWALGCLLYEMIAGQSPF--QQRKKKIKREEVERLVK- 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1704602876 232 sfEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEG-----VLDHP 272
Cdd:cd05630   219 --EVPEEYSEKFSPQARSLCSMLLCKDPAERLGCRGggareVKEHP 262
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
18-310 1.47e-09

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: 59.30  E-value: 1.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  18 EEYSInwTQKLGAGISGPVRVCVKKSTQERFALK--------ILLDRPKARnEVRL--HMmcaTHPNIVQIIEVFANSVQ 87
Cdd:cd07855     5 DRYEP--IETIGSGAYGVVCSAIDTKSGQKVAIKkipnafdvVTTAKRTLR-ELKIlrHF---KHDNIIAIRDILRPKVP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  88 FPHESSprarLLIVMEMMEGgELFHRISQHRHFTE---------------------------KQASQVTKQDAPVKLCDF 140
Cdd:cd07855    79 YADFKD----VYVVLDLMES-DLHHIIHSDQPLTLehiryflyqllrglkyihsanvihrdlKPSNLLVNENCELKIGDF 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 141 GFAK------IDQGDLMTPQF-TPYYVAPQVLEAQRRhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYS 213
Cdd:cd07855   154 GMARglctspEEHKYFMTEYVaTRWYRAPELMLSLPE-----------------YTQAIDMWSVGCIFAEMLGRRQLFPG 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 214 KHHS------------------RTIPKDMRRKIMTGSFEFPEEEWSQI----SEMAKDVVRKLLKVKPEERLTIEGVLDH 271
Cdd:cd07855   217 KNYVhqlqliltvlgtpsqaviNAIGADRVRRYIQNLPNKQPVPWETLypkaDQQALDLLSQMLRFDPSERITVAEALQH 296
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1704602876 272 PWLNSTEALDN--VLPSAqLMMDKAVVAGIQQAHAEQLANM 310
Cdd:cd07855   297 PFLAKYHDPDDepDCAPP-FDFDFDAEALTREALKEAIVNE 336
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
27-285 1.91e-09

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: 58.50  E-value: 1.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  27 KLGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLH----MMCATHPNIVQIIevfaNSVQFPHEssprarLLIVM 102
Cdd:cd06657    27 KIGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRRELLFNevviMRDYQHENVVEMY----NSYLVGDE------LWVVM 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 103 EMMEGGELFHrISQHRHFTEKQASQVT---------------------------KQDAPVKLCDFGFAKIDQGDLMTPQF 155
Cdd:cd06657    97 EFLEGGALTD-IVTHTRMNEEQIAAVClavlkalsvlhaqgvihrdiksdsillTHDGRVKLSDFGFCAQVSKEVPRRKS 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 156 ---TPYYVAPQVLeaqrrhqkeksgiiptSPTPYtyNKSCDLWSLGVIIYVMLCGYPPFYSKhhsrtiPKDMRRKIMTGS 232
Cdd:cd06657   176 lvgTPYWMAPELI----------------SRLPY--GPEVDIWSLGIMVIEMVDGEPPYFNE------PPLKAMKMIRDN 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1704602876 233 FEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEALDNVLP 285
Cdd:cd06657   232 LPPKLKNLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPSCIVP 284
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
28-272 2.19e-09

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: 58.38  E-value: 2.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKiLLDRPKARNEVRLHMMCATHPNIVQIIEVFANSVQFPHESspRARLLIVMEMMEG 107
Cdd:cd05607    10 LGKGGFGEVCAVQVKNTGQMYACK-KLDKKRLKKKSGEKMALLEKEILEKVNSPFIVSLAYAFET--KTHLCLVMSLMNG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 108 GEL-FH------------RI----SQ------HRH-----FTEKQASQVTKQD-APVKLCDFGFA-KIDQGDLMTPQF-T 156
Cdd:cd05607    87 GDLkYHiynvgergiemeRVifysAQitcgilHLHslkivYRDMKPENVLLDDnGNCRLSDLGLAvEVKEGKPITQRAgT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 157 PYYVAPQVLeaqrrhqKEKSgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFySKHHSRTIPKDMRRKIMTGSFEFp 236
Cdd:cd05607   167 NGYMAPEIL-------KEES-----------YSYPVDWFAMGCSIYEMVAGRTPF-RDHKEKVSKEELKRRTLEDEVKF- 226
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1704602876 237 eeEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHP 272
Cdd:cd05607   227 --EHQNFTEEAKDICRLFLAKKPENRLGSRTNDDDP 260
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
17-274 2.39e-09

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: 58.08  E-value: 2.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  17 LEEYSINW--TQKLGAGISGPVRVCVKKSTQERFALKIL-----LDRpKARNEVRLHMMCATHPNIVQIIEVFANSVQFP 89
Cdd:cd06639    17 LADPSDTWdiIETIGKGTYGKVYKVTNKKDGSLAAVKILdpisdVDE-EIEAEYNILRSLPNHPNVVKFYGMFYKADQYV 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  90 HessprARLLIVMEMMEGGELFHRIS-------------------------QHRHFTE------KQASQVTKQDAPVKLC 138
Cdd:cd06639    96 G-----GQLWLVLELCNGGSVTELVKgllkcgqrldeamisyilygallglQHLHNNRiihrdvKGNNILLTTEGGVKLV 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 139 DFGF-AKIDQGDLM--TPQFTPYYVAPQVLEAQRRHQkeksgiiptsptpYTYNKSCDLWSLGVIIYVMLCGYPPFYSKH 215
Cdd:cd06639   171 DFGVsAQLTSARLRrnTSVGTPFWMAPEVIACEQQYD-------------YSYDARCDVWSLGITAIELADGDPPLFDMH 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1704602876 216 HSRTIPKDMRRKIMTgsFEFPeEEWSQisEMAKDVVRKLLKvKPEERLTIEGVLDHPWL 274
Cdd:cd06639   238 PVKALFKIPRNPPPT--LLNP-EKWCR--GFSHFISQCLIK-DFEKRPSVTHLLEHPFI 290
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
27-273 2.54e-09

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: 58.05  E-value: 2.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  27 KLGAGISGPVRVCVKKSTQERFALKIL------LDRPKARNEVRLHMMCATHPNIVQIIEVfansvqfpHESSPRARLLI 100
Cdd:cd07831     6 KIGEGTFSEVLKAQSRKTGKYYAIKCMkkhfksLEQVNNLREIQALRRLSPHPNILRLIEV--------LFDRKTGRLAL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 101 VMEMMEGgELFHRISQHRH-FTEKQASQVTKQ--------------------------DAPVKLCDFGFAK-IDQgdlmT 152
Cdd:cd07831    78 VFELMDM-NLYELIKGRKRpLPEKRVKNYMYQllksldhmhrngifhrdikpenilikDDILKLADFGSCRgIYS----K 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 153 PQFTPY-----YVAPQVLEaqrrhqkeksgiiptspTPYTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPK----- 222
Cdd:cd07831   153 PPYTEYistrwYRAPECLL-----------------TDGYYGPKMDIWAVGCVFFEILSLFPLFPGTNELDQIAKihdvl 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1704602876 223 --------DMRRKIMTGSFEFPEEEWSQI-------SEMAKDVVRKLLKVKPEERLTIEGVLDHPW 273
Cdd:cd07831   216 gtpdaevlKKFRKSRHMNYNFPSKKGTGLrkllpnaSAEGLDLLKKLLAYDPDERITAKQALRHPY 281
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
92-276 3.72e-09

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: 57.25  E-value: 3.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  92 SSPRARLLIvMEMMEGGELFHRiSQHRHFTEKQASQVTKQDAPVKLCDFGFA---KIDQGDLMTPQFTPYYVAPQVLeAQ 168
Cdd:cd14187   105 TEPEARYYL-RQIILGCQYLHR-NRVIHRDLKLGNLFLNDDMEVKIGDFGLAtkvEYDGERKKTLCGTPNYIAPEVL-SK 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 169 RRHQKEksgiiptsptpytynksCDLWSLGVIIYVMLCGYPPFYSkhhsrTIPKDMRRKIMTGSFEFPEeewsQISEMAK 248
Cdd:cd14187   182 KGHSFE-----------------VDIWSIGCIMYTLLVGKPPFET-----SCLKETYLRIKKNEYSIPK----HINPVAA 235
                         170       180
                  ....*....|....*....|....*...
gi 1704602876 249 DVVRKLLKVKPEERLTIEGVLDHPWLNS 276
Cdd:cd14187   236 SLIQKMLQTDPTARPTINELLNDEFFTS 263
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
28-274 3.76e-09

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


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 58.07  E-value: 3.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKiLLDRP--------KARNEVRL--HMmcaTHPNIVQIIEVFAnsvqfPHESSPRAR 97
Cdd:cd07851    23 VGSGAYGQVCSAFDTKTGRKVAIK-KLSRPfqsaihakRTYRELRLlkHM---KHENVIGLLDVFT-----PASSLEDFQ 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  98 -LLIVMEMMeGGELfHRISQHRHFTEKQ----ASQVTK-----------------------QDAPVKLCDFGFAKIDQGD 149
Cdd:cd07851    94 dVYLVTHLM-GADL-NNIVKCQKLSDDHiqflVYQILRglkyihsagiihrdlkpsnlavnEDCELKILDFGLARHTDDE 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 150 LMTPQFTPYYVAPQVLeAQRRHqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSrtipkDMRRKIM 229
Cdd:cd07851   172 MTGYVATRWYRAPEIM-LNWMH----------------YNQTVDIWSVGCIMAELLTGKTLFPGSDHI-----DQLKRIM 229
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1704602876 230 --TGSfefPEEEWSQ--ISEMAKDVVR--------------------------KLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd07851   230 nlVGT---PDEELLKkiSSESARNYIQslpqmpkkdfkevfsganplaidlleKMLVLDPDKRITAAEALAHPYL 301
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
27-274 4.43e-09

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: 58.12  E-value: 4.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  27 KLGAGISGPVRVCVKKSTQERFALKILLDRP-KARNEVRlHMM-------CATHPNIVQIIEVF--ANSVQFPHESSP-- 94
Cdd:cd05600    18 QVGQGGYGSVFLARKKDTGEICALKIMKKKVlFKLNEVN-HVLterdiltTTNSPWLVKLLYAFqdPENVYLAMEYVPgg 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  95 ---------------RARLLIvMEMMEGGELFHRISQ-HRHFteKQASQVTKQDAPVKLCDFGFA--------------- 143
Cdd:cd05600    97 dfrtllnnsgilseeHARFYI-AEMFAAISSLHQLGYiHRDL--KPENFLIDSSGHIKLTDFGLAsgtlspkkiesmkir 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 144 ----KIDQGDLMTPQFT---------------------PYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLG 198
Cdd:cd05600   174 leevKNTAFLELTAKERrniyramrkedqnyansvvgsPDYMAPEVLRGEG------------------YDLTVDYWSLG 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 199 VIIYVMLCGYPPFYS----------KHHSRTipkdMRRKIMTG---SFEFPEEEWSQISEMAKDvvrkllkvkPEERL-T 264
Cdd:cd05600   236 CILFECLVGFPPFSGstpnetwanlYHWKKT----LQRPVYTDpdlEFNLSDEAWDLITKLITD---------PQDRLqS 302
                         330
                  ....*....|
gi 1704602876 265 IEGVLDHPWL 274
Cdd:cd05600   303 PEQIKNHPFF 312
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
27-274 5.16e-09

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: 57.36  E-value: 5.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  27 KLGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLH----MMCATHPNIVQIIevfaNSVQFPHEssprarLLIVM 102
Cdd:cd06658    29 KIGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRRELLFNevviMRDYHHENVVDMY----NSYLVGDE------LWVVM 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 103 EMMEGGELFHRISQHR--------------------------HFTEKQASQVTKQDAPVKLCDFGFAKIDQGDLMTPQF- 155
Cdd:cd06658    99 EFLEGGALTDIVTHTRmneeqiatvclsvlralsylhnqgviHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRKSl 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 156 --TPYYVAPQVLeaqrrhqkeksgiiptSPTPYtyNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTipkdMRRkiMTGSF 233
Cdd:cd06658   179 vgTPYWMAPEVI----------------SRLPY--GTEVDIWSLGIMVIEMIDGEPPYFNEPPLQA----MRR--IRDNL 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1704602876 234 EFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd06658   235 PPRVKDSHKVSSVLRGFLDLMLVREPSQRATAQELLQHPFL 275
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
60-272 5.21e-09

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: 57.05  E-value: 5.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  60 RNEVRLhMMCATHPNIVQIIEVFANSVQFPhessprarllIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ-------- 131
Cdd:cd06630    51 REEIRM-MARLNHPNIVRMLGATQHKSHFN----------IFVEWMAGGSVASLLSKYGAFSENVIINYTLQilrglayl 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 132 -----------------DAP---VKLCDFGFA-----KIDQGDLMTPQF--TPYYVAPQVLEAQrrhqkeksgiiptspt 184
Cdd:cd06630   120 hdnqiihrdlkganllvDSTgqrLRIADFGAAarlasKGTGAGEFQGQLlgTIAFMAPEVLRGE---------------- 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 185 pyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDMRRKIMTGSFEFPEeewsQISEMAKDVVRKLLKVKPEERLT 264
Cdd:cd06630   184 --QYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIFKIASATTPPPIPE----HLSPGLRDVTLRCLELQPEDRPP 257

                  ....*...
gi 1704602876 265 IEGVLDHP 272
Cdd:cd06630   258 ARELLKHP 265
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
26-206 7.04e-09

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: 56.28  E-value: 7.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKILLDRP----------KARNEVRLhMMCATHPNIVQIIEVFANSVQFphesspr 95
Cdd:cd08222     6 RKLGSGNFGTVYLVSDLKATADEELKVLKEISvgelqpdetvDANREAKL-LSKLDHPAIVKFHDSFVEKESF------- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  96 arlLIVMEMMEGGELFHRISQHRH----FTEKQ--------------------------ASQVTKQDAPVKLCDFGFAKI 145
Cdd:cd08222    78 ---CIVTEYCEGGDLDDKISEYKKsgttIDENQildwfiqlllavqymherrilhrdlkAKNIFLKNNVIKVGDFGISRI 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1704602876 146 DQG--DLMTpQF--TPYYVAPQVLeaqrRHQkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLC 206
Cdd:cd08222   155 LMGtsDLAT-TFtgTPYYMSPEVL----KHE--------------GYNSKSDIWSLGCILYEMCC 200
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
128-274 8.69e-09

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: 56.12  E-value: 8.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 128 VTKQDAPVKLCDFGFAKIDQgDLMTPQF--TPYYVAPQVLEAQRRHqkeksgiiptsptpytyNKSCDLWSLGVIIYVML 205
Cdd:cd14102   138 VDLRTGELKLIDFGSGALLK-DTVYTDFdgTRVYSPPEWIRYHRYH-----------------GRSATVWSLGVLLYDMV 199
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1704602876 206 CGYPPFyskhhsrtipkDMRRKIMTGSFEFPEeewsQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14102   200 CGDIPF-----------EQDEEILRGRLYFRR----RVSPECQQLIKWCLSLRPSDRPTLEQIFDHPWM 253
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
26-274 1.02e-08

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: 56.43  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPV----------RVCVKKsTQERFALKILLDRPKARNEVRLHMmcaTHPNIVQIIEVFAnsvqfphesSPR 95
Cdd:cd07856    16 QPVGMGAFGLVcsardqltgqNVAVKK-IMKPFSTPVLAKRTYRELKLLKHL---RHENIISLSDIFI---------SPL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  96 ARLLIVMEMMegGELFHRISQHRHFtEKQASQ----------------------------VTKQDAPVKLCDFGFAKIDQ 147
Cdd:cd07856    83 EDIYFVTELL--GTDLHRLLTSRPL-EKQFIQyflyqilrglkyvhsagvihrdlkpsniLVNENCDLKICDFGLARIQD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 148 GDLMTPQFTPYYVAPQVLEAQRRhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSR--------- 218
Cdd:cd07856   160 PQMTGYVSTRYYRAPEIMLTWQK-----------------YDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNqfsiitell 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1704602876 219 -TIPKDMRRKIMT-GSFEF----PEEEWSQISEM-------AKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd07856   223 gTPPDDVINTICSeNTLRFvqslPKRERVPFSEKfknadpdAIDLLEKMLVFDPKKRISAAEALAHPYL 291
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
26-289 1.15e-08

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


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 56.59  E-value: 1.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKiLLDRP--------KARNEVRLhMMCATHPNIVQIIEVFAnsvqfPHESSPRAR 97
Cdd:cd07875    30 KPIGSGAQGIVCAAYDAILERNVAIK-KLSRPfqnqthakRAYRELVL-MKCVNHKNIIGLLNVFT-----PQKSLEEFQ 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  98 -LLIVMEMMEGG-------ELFH-RIS----------QHRHFTE------KQASQVTKQDAPVKLCDFGFAKIDQGD-LM 151
Cdd:cd07875   103 dVYIVMELMDANlcqviqmELDHeRMSyllyqmlcgiKHLHSAGiihrdlKPSNIVVKSDCTLKILDFGLARTAGTSfMM 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 152 TPQF-TPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHH----SRTIPK---- 222
Cdd:cd07875   183 TPYVvTRYYRAPEVILGM------------------GYKENVDIWSVGCIMGEMIKGGVLFPGTDHidqwNKVIEQlgtp 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 223 ----------------DMRRKIMTGSFE--FPEEEWSQISE-------MAKDVVRKLLKVKPEERLTIEGVLDHPWLN-- 275
Cdd:cd07875   245 cpefmkklqptvrtyvENRPKYAGYSFEklFPDVLFPADSEhnklkasQARDLLSKMLVIDASKRISVDEALQHPYINvw 324
                         330
                  ....*....|....*...
gi 1704602876 276 ----STEALDNVLPSAQL 289
Cdd:cd07875   325 ydpsEAEAPPPKIPDKQL 342
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
26-271 1.15e-08

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


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 55.81  E-value: 1.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKILLDRPK-----ARNEVRLHMMCaTHPNIVQIIEVF--------------ANSV 86
Cdd:cd06646    15 QRVGSGTYGDVYKARNLHTGELAAVKIIKLEPGddfslIQQEIFMVKEC-KHCNIVAYFGSYlsreklwicmeycgGGSL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  87 Q-FPHESSPRARLLIVM---EMMEG-GELFHRISQHRHFteKQASQVTKQDAPVKLCDFGFA-KIDQGDLMTPQF--TPY 158
Cdd:cd06646    94 QdIYHVTGPLSELQIAYvcrETLQGlAYLHSKGKMHRDI--KGANILLTDNGDVKLADFGVAaKITATIAKRKSFigTPY 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 159 YVAPQVLEAqrrhqkEKSGiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIpkdmrrKIMTGS-FEFPE 237
Cdd:cd06646   172 WMAPEVAAV------EKNG---------GYNQLCDIWAVGITAIELAELQPPMFDLHPMRAL------FLMSKSnFQPPK 230
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1704602876 238 -EEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDH 271
Cdd:cd06646   231 lKDKTKWSSTFHNFVKISLTKNPKKRPTAERLLTH 265
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
135-274 1.32e-08

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: 55.63  E-value: 1.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 135 VKLCDFGFAKIDQgDLMTPQF--TPYYVAPQVLEAQRRHQkeksgiiptspTPYTynkscdLWSLGVIIYVMLCGyppfy 212
Cdd:cd14101   148 IKLIDFGSGATLK-DSMYTDFdgTRVYSPPEWILYHQYHA-----------LPAT------VWSLGILLYDMVCG----- 204
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1704602876 213 skhhsrTIPKDMRRKIMTGSFEFPeeewSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14101   205 ------DIPFERDTDILKAKPSFN----KRVSNDCRSLIRSCLAYNPSDRPSLEQILLHPWM 256
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
25-275 1.61e-08

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


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 55.87  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  25 TQKLGAGISGPV------------RVCVKKSTQErFALKILLDRpkARNEVRLHMMCATHPNIVQIIEVfanSVQFPhes 92
Cdd:cd07857     5 IKELGQGAYGIVcsarnaetseeeTVAIKKITNV-FSKKILAKR--ALRELKLLRHFRGHKNITCLYDM---DIVFP--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  93 SPRARLLIVMEMME---------GGEL--FHR---ISQ--------------HRHFteKQASQVTKQDAPVKLCDFGFAK 144
Cdd:cd07857    76 GNFNELYLYEELMEadlhqiirsGQPLtdAHFqsfIYQilcglkyihsanvlHRDL--KPGNLLVNADCELKICDFGLAR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 145 -IDQGDLMTPQF------TPYYVAPQVLEAQRRhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSK--- 214
Cdd:cd07857   154 gFSENPGENAGFmteyvaTRWYRAPEIMLSFQS-----------------YTKAIDVWSVGCILAELLGRKPVFKGKdyv 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 215 HHSRTI-------PKDMRRKIMTG-------SFEFPEE---EWSQI--SEMAKDVVRKLLKVKPEERLTIEGVLDHPWLN 275
Cdd:cd07857   217 DQLNQIlqvlgtpDEETLSRIGSPkaqnyirSLPNIPKkpfESIFPnaNPLALDLLEKLLAFDPTKRISVEEALEHPYLA 296
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
25-274 1.69e-08

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


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 55.40  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  25 TQKLGAGISGPVRVCVKKSTQERFALKIL-----LDRpKARNEVRLHMMCATHPNIVQIIEVFansvqFPHESSPRARLL 99
Cdd:cd06638    23 IETIGKGTYGKVFKVLNKKNGSKAAVKILdpihdIDE-EIEAEYNILKALSDHPNVVKFYGMY-----YKKDVKNGDQLW 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMEGGELF----------HRIS---------------QHRHFTE------KQASQVTKQDAPVKLCDFGF-AKIDQ 147
Cdd:cd06638    97 LVLELCNGGSVTdlvkgflkrgERMEepiiayilhealmglQHLHVNKtihrdvKGNNILLTTEGGVKLVDFGVsAQLTS 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 148 GDLM--TPQFTPYYVAPQVLEAQRRHQKeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDMR 225
Cdd:cd06638   177 TRLRrnTSVGTPFWMAPEVIACEQQLDS-------------TYDARCDVWSLGITAIELGDGDPPLADLHPMRALFKIPR 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1704602876 226 RKIMTgsFEFPeEEWSqiSEMaKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd06638   244 NPPPT--LHQP-ELWS--NEF-NDFIRKCLTKDYEKRPTVSDLLQHVFI 286
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
28-278 1.88e-08

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: 55.04  E-value: 1.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALK-ILLDRPKARN-----EVRLHMMCaTHPNIVQIIEVFANSvqfphessprARLLIV 101
Cdd:cd06605     9 LGEGNGGVVSKVRHRPSGQIMAVKvIRLEIDEALQkqilrELDVLHKC-NSPYIVGFYGAFYSE----------GDISIC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 102 MEMMEGGE--------------------------LFHRISQHR--HFTEKQASQVTKQDAPVKLCDFG--------FAKI 145
Cdd:cd06605    78 MEYMDGGSldkilkevgriperilgkiavavvkgLIYLHEKHKiiHRDVKPSNILVNSRGQVKLCDFGvsgqlvdsLAKT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 146 DQGdlmtpqfTPYYVAPQVLeaqrrhqkeksgiiptSPTPYTyNKScDLWSLGVIIYVMLCG---YPPFYSKhhSRTIPK 222
Cdd:cd06605   158 FVG-------TRSYMAPERI----------------SGGKYT-VKS-DIWSLGLSLVELATGrfpYPPPNAK--PSMMIF 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1704602876 223 DMRRKIMTG-SFEFPEEEWsqiSEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTE 278
Cdd:cd06605   211 ELLSYIVDEpPPLLPSGKF---SPDFQDFVSQCLQKDPTERPSYKELMEHPFIKRYE 264
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
135-274 2.68e-08

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


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 55.39  E-value: 2.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 135 VKLCDFGFAKI-----DQGDLMTPQF-TPYYVAPQVLEAQRrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGY 208
Cdd:cd07849   145 LKICDFGLARIadpehDHTGFLTEYVaTRWYRAPEIMLNSK-----------------GYTKAIDIWSVGCILAEMLSNR 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 209 PPFYSKHHS------------------RTIpKDMRRKIMTGSFEF-PEEEWSQI----SEMAKDVVRKLLKVKPEERLTI 265
Cdd:cd07849   208 PLFPGKDYLhqlnlilgilgtpsqedlNCI-ISLKARNYIKSLPFkPKVPWNKLfpnaDPKALDLLDKMLTFNPHKRITV 286

                  ....*....
gi 1704602876 266 EGVLDHPWL 274
Cdd:cd07849   287 EEALAHPYL 295
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
27-273 2.80e-08

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: 54.69  E-value: 2.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  27 KLGAGISGPVRVCVKKSTQERFALKILLD-------RPKARNEVRLHMMCaTHPNIVQIIEVFANsvqfphesspRARLL 99
Cdd:cd07847     8 KIGEGSYGVVFKCRNRETGQIVAIKKFVEseddpviKKIALREIRMLKQL-KHPNLVNLIEVFRR----------KRKLH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMEGgELFHRISQH-----RHFTEKQASQV------------------------TKQDApVKLCDFGFAKI--DQG 148
Cdd:cd07847    77 LVFEYCDH-TVLNELEKNprgvpEHLIKKIIWQTlqavnfchkhncihrdvkpeniliTKQGQ-IKLCDFGFARIltGPG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 149 DLMTPQF-TPYYVAPQVLEAQRRhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYP------------------ 209
Cdd:cd07847   155 DDYTDYVaTRWYRAPELLVGDTQ-----------------YGPPVDVWAIGCVFAELLTGQPlwpgksdvdqlylirktl 217
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1704602876 210 -PFYSKH----------HSRTIPKDMRRKIMtgsfefpEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPW 273
Cdd:cd07847   218 gDLIPRHqqifstnqffKGLSIPEPETREPL-------ESKFPNISSPALSFLKGCLQMDPTERLSCEELLEHPY 285
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
15-262 3.33e-08

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 55.90  E-value: 3.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876   15 SILEEYSInwTQKLGAGISGPVRVCVKKSTQERFALKI-----LLDRPKARNEVRLHMMCA-THPNIVQIIEVFANSVQf 88
Cdd:PTZ00266    10 SRLNEYEV--IKKIGNGRFGEVFLVKHKRTQEFFCWKAisyrgLKEREKSQLVIEVNVMRElKHKNIVRYIDRFLNKAN- 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876   89 phessprARLLIVMEMMEGGEL----------FHRISQH----------------------------------------- 117
Cdd:PTZ00266    87 -------QKLYILMEFCDAGDLsrniqkcykmFGKIEEHaivditrqllhalaychnlkdgpngervlhrdlkpqnifls 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  118 ---RHFTEKQASQVTKQDAPV-KLCDFGFAKIDQGDLMTPQF--TPYYVAPQVLEAQRRhqkeksgiiptsptpyTYNKS 191
Cdd:PTZ00266   160 tgiRHIGKITAQANNLNGRPIaKIGDFGLSKNIGIESMAHSCvgTPYYWSPELLLHETK----------------SYDDK 223
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1704602876  192 CDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDMRRKimtgsfefPEEEWSQISEMAKDVVRKLLKVKPEER 262
Cdd:PTZ00266   224 SDMWALGCIIYELCSGKTPFHKANNFSQLISELKRG--------PDLPIKGKSKELNILIKNLLNLSAKER 286
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
27-288 3.66e-08

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: 54.65  E-value: 3.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  27 KLGAGISGPVRVCVKKSTQERFALKILldRPKARNEVRLHM----MCAT--HPNIVQIIEVFANS------VQFPHESSP 94
Cdd:cd06644    19 ELGDGAFGKVYKAKNKETGALAAAKVI--ETKSEEELEDYMveieILATcnHPYIVKLLGAFYWDgklwimIEFCPGGAV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  95 RARLL-------------IVMEMMEGGELFHRISQ-HRHFteKQASQVTKQDAPVKLCDFGfakIDQGDLMTPQF----- 155
Cdd:cd06644    97 DAIMLeldrgltepqiqvICRQMLEALQYLHSMKIiHRDL--KAGNVLLTLDGDIKLADFG---VSAKNVKTLQRrdsfi 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 156 -TPYYVAPQVLEAQrrhqkeksgiiPTSPTPYTYNksCDLWSLGVIIYVMLCGYPPfyskHHSRTipkDMRRKIMTGSFE 234
Cdd:cd06644   172 gTPYWMAPEVVMCE-----------TMKDTPYDYK--ADIWSLGITLIEMAQIEPP----HHELN---PMRVLLKIAKSE 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1704602876 235 FPE-EEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPW---LNSTEALDNVLPSAQ 288
Cdd:cd06644   232 PPTlSQPSKWSMEFRDFLKTALDKHPETRPSAAQLLEHPFvssVTSNRPLRELVAEAK 289
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
98-274 4.50e-08

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: 53.97  E-value: 4.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  98 LLIVMEMMEGGELFHRISQHRH--FTEKQ--------ASQV--------------------TKQDApVKLCDFGFAKI-D 146
Cdd:cd08221    74 LFIEMEYCNGGNLHDKIAQQKNqlFPEEVvlwylyqiVSAVshihkagilhrdiktlniflTKADL-VKLGDFGISKVlD 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 147 QGDLMTPQF--TPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCgyppfYSKHHSRTIPKDM 224
Cdd:cd08221   153 SESSMAESIvgTPYYMSPELVQGVK------------------YNFKSDIWAVGCVLYELLT-----LKRTFDATNPLRL 209
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1704602876 225 RRKIMTGSFefpEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd08221   210 AVKIVQGEY---EDIDEQYSEEIIQLVHDCLHQDPEDRPTAEELLERPLL 256
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
26-274 4.66e-08

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


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 54.28  E-value: 4.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKILLDRPK-----ARNEVRLHMMCaTHPNIVQIIEVF--------------ANSV 86
Cdd:cd06645    17 QRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGedfavVQQEIIMMKDC-KHSNIVAYFGSYlrrdklwicmefcgGGSL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  87 Q-FPHESSPRARLLIVM---EMMEGGELFHRISQ-HRHFteKQASQVTKQDAPVKLCDFGF-AKIDQGDLMTPQF--TPY 158
Cdd:cd06645    96 QdIYHVTGPLSESQIAYvsrETLQGLYYLHSKGKmHRDI--KGANILLTDNGHVKLADFGVsAQITATIAKRKSFigTPY 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 159 YVAPQVLEAQRrhqkeKSGiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIpkdmrrKIMT-GSFEFPE 237
Cdd:cd06645   174 WMAPEVAAVER-----KGG----------YNQLCDIWAVGITAIELAELQPPMFDLHPMRAL------FLMTkSNFQPPK 232
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1704602876 238 -EEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd06645   233 lKDKMKWSNSFHHFVKMALTKNPKKRPTAEKLLQHPFV 270
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
26-274 6.40e-08

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: 53.59  E-value: 6.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKIL-------LDRPKARNEVRLhMMCATHPNIVQIIEVFANSVQFphessprarL 98
Cdd:cd08223     6 RVIGKGSYGEVWLVRHKRDRKQYVIKKLnlknaskRERKAAEQEAKL-LSKLKHPNIVSYKESFEGEDGF---------L 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  99 LIVMEMMEGGELFHRISQ-------------------------------HRHFtEKQASQVTKQDApVKLCDFGFAKI-- 145
Cdd:cd08223    76 YIVMGFCEGGDLYTRLKEqkgvlleerqvvewfvqiamalqymhernilHRDL-KTQNIFLTKSNI-IKVGDLGIARVle 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 146 DQGDLMTPQF-TPYYVAPQVLeaqrrhqkeksgiiptSPTPYTYnKScDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDM 224
Cdd:cd08223   154 SSSDMATTLIgTPYYMSPELF----------------SNKPYNH-KS-DVWALGCCVYEMATLKHAFNAKDMNSLVYKIL 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1704602876 225 RRKIMtgsfEFPeeewSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd08223   216 EGKLP----PMP----KQYSPELGELIKAMLHQDPEKRPSVKRILRQPYI 257
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
28-274 7.46e-08

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: 53.82  E-value: 7.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKIL-LDRPKARNEVRLHMmcathpNIVQIIEV----FANSVQFPHESspRARLLIVM 102
Cdd:cd05632    10 LGKGGFGEVCACQVRATGKMYACKRLeKKRIKKRKGESMAL------NEKQILEKvnsqFVVNLAYAYET--KDALCLVL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 103 EMMEGGEL-FHRISQ------------------------HRHFTE----KQASQVTKQDAPVKLCDFGFA-KIDQGDLMT 152
Cdd:cd05632    82 TIMNGGDLkFHIYNMgnpgfeeeralfyaaeilcgledlHRENTVyrdlKPENILLDDYGHIRISDLGLAvKIPEGESIR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 153 PQF-TPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHsRTIPKDMRRKIMtg 231
Cdd:cd05632   162 GRVgTVGYMAPEVLNNQR------------------YTLSPDYWGLGCLIYEMIEGQSPFRGRKE-KVKREEVDRRVL-- 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1704602876 232 sfEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIE-----GVLDHPWL 274
Cdd:cd05632   221 --ETEEVYSAKFSEEAKSICKMLLTKDPKQRLGCQeegagEVKRHPFF 266
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
28-272 9.98e-08

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: 53.35  E-value: 9.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKIL-LDRPKARNEVRLHMMcaTHPNIVQIIEVFANSVQFPHESspRARLLIVMEMME 106
Cdd:cd05608     9 LGKGGFGEVSACQMRATGKLYACKKLnKKRLKKRKGYEGAMV--EKRILAKVHSRFIVSLAYAFQT--KTDLCLVMTIMN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 107 GGELFHRI----SQHRHFTEKQASQVTKQ---------------------------DAPVKLCDFGFA-KIDQGDLMTPQ 154
Cdd:cd05608    85 GGDLRYHIynvdEENPGFQEPRACFYTAQiisglehlhqrriiyrdlkpenvllddDGNVRISDLGLAvELKDGQTKTKG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 155 F--TPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHsRTIPKDMRRKIMTGS 232
Cdd:cd05608   165 YagTPGFMAPELLLGEE------------------YDYSVDYFTLGVTLYEMIAARGPFRARGE-KVENKELKQRILNDS 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1704602876 233 FEFPEeewsQISEMAKDVVRKLLKVKPEERL-----TIEGVLDHP 272
Cdd:cd05608   226 VTYSE----KFSPASKSICEALLAKDPEKRLgfrdgNCDGLRTHP 266
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
26-272 1.00e-07

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: 52.70  E-value: 1.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKILLDR---PKAR----NEVRLHMMCATHPNIVQIIEVFANsvqfphesspRARL 98
Cdd:cd14050     7 SKLGEGSFGEVFKVRSREDGKLYAVKRSRSRfrgEKDRkrklEEVERHEKLGEHPNCVRFIKAWEE----------KGIL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  99 LIVMEMMEGG-----ELFHRISQHR---------------------HFTEKQASQVTKQDAPVKLCDFGF-AKIDQGDLM 151
Cdd:cd14050    77 YIQTELCDTSlqqycEETHSLPESEvwnilldllkglkhlhdhgliHLDIKPANIFLSKDGVCKLGDFGLvVELDKEDIH 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 152 TPQ-FTPYYVAPQVLEAqrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCgyppfyskhhSRTIPK--DMRRKI 228
Cdd:cd14050   157 DAQeGDPRYMAPELLQG-------------------SFTKAADIFSLGITILELAC----------NLELPSggDGWHQL 207
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1704602876 229 MTGsfEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHP 272
Cdd:cd14050   208 RQG--YLPEEFTAGLSPELRSIIKLMMDPDPERRPTAEDLLALP 249
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
27-273 1.19e-07

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


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 52.81  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  27 KLGAGISGPVRVCVKKSTQERFALKILLDRPK-------ARNEVRLhMMCATHPNIVQIIEVFANsvqfphesspRARLL 99
Cdd:cd07846     8 LVGEGSYGMVMKCRHKETGQIVAIKKFLESEDdkmvkkiAMREIKM-LKQLRHENLVNLIEVFRR----------KKRWY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMM-----------EGGELFHRISQ------------HR----HFTEKQASQVTKQDAPVKLCDFGFAKI--DQGDL 150
Cdd:cd07846    77 LVFEFVdhtvlddlekyPNGLDESRVRKylfqilrgidfcHShniiHRDIKPENILVSQSGVVKLCDFGFARTlaAPGEV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 151 MTPQF-TPYYVAPQVLEAQRRhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSK------HH-----SR 218
Cdd:cd07846   157 YTDYVaTRWYRAPELLVGDTK-----------------YGKAVDVWAVGCLVTEMLTGEPLFPGDsdidqlYHiikclGN 219
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1704602876 219 TIPKdmRRKIMTGSFEFP-------------EEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPW 273
Cdd:cd07846   220 LIPR--HQELFQKNPLFAgvrlpevkeveplERRYPKLSGVVIDLAKKCLHIDPDKRPSCSELLHHEF 285
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
57-270 1.21e-07

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


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 52.66  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  57 PKARN----EVRLhMMCATHPNIVQIIEVFANSvqfphessprARLLIVMEMMEGGELF----HRISQHRHFTEKQA--- 125
Cdd:cd08224    41 AKARQdclkEIDL-LQQLNHPNIIKYLASFIEN----------NELNIVLELADAGDLSrlikHFKKQKRLIPERTIwky 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 126 -SQVTK-----------------------QDAPVKLCDFGFakidqGDLMTPQF--------TPYYVAPQVLEAQrrhqk 173
Cdd:cd08224   110 fVQLCSalehmhskrimhrdikpanvfitANGVVKLGDLGL-----GRFFSSKTtaahslvgTPYYMSPERIREQ----- 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 174 eksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTipkDMRRKIMTGSFE-FPEEEWSQisEMaKDVVR 252
Cdd:cd08224   180 -------------GYDFKSDIWSLGCLLYEMAALQSPFYGEKMNLY---SLCKKIEKCEYPpLPADLYSQ--EL-RDLVA 240
                         250
                  ....*....|....*...
gi 1704602876 253 KLLKVKPEERLTIEGVLD 270
Cdd:cd08224   241 ACIQPDPEKRPDISYVLD 258
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
28-270 1.27e-07

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 53.50  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLHMMCATHPNIVQIIE-------------VFANSVQ------- 87
Cdd:PTZ00036   74 IGNGSFGVVYEAICIDTSEKVAIKKVLQDPQYKNRELLIMKNLNHINIIFLKDyyytecfkkneknIFLNVVMefipqtv 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  88 ---FPHESSPRARLLIVMEMMEGGELFHRISQ-HRHFT-----EKQASQVTKQDAPVKLCDFGFAKidqgDLMTPQFTPY 158
Cdd:PTZ00036  154 hkyMKHYARNNHALPLFLVKLYSYQLCRALAYiHSKFIchrdlKPQNLLIDPNTHTLKLCDFGSAK----NLLAGQRSVS 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 159 YVAPQVLEAQRrhqkeksgiIPTSPTPYTYNksCDLWSLGVIIYVMLCGYPPFYSKHH----SRTI-----PKDMRRKIM 229
Cdd:PTZ00036  230 YICSRFYRAPE---------LMLGATNYTTH--IDLWSLGCIIAEMILGYPIFSGQSSvdqlVRIIqvlgtPTEDQLKEM 298
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1704602876 230 TGSF---EFPEEEWSQIS--------EMAKDVVRKLLKVKPEERLT-IEGVLD 270
Cdd:PTZ00036  299 NPNYadiKFPDVKPKDLKkvfpkgtpDDAINFISQFLKYEPLKRLNpIEALAD 351
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
156-278 2.15e-07

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: 52.74  E-value: 2.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 156 TPYYVAPQVLEaqrrhqkeKSGiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHhsrtiPKDMRRKIMTGSFEF 235
Cdd:cd05625   211 TPNYIAPEVLL--------RTG----------YTQLCDWWSVGVILFEMLVGQPPFLAQT-----PLETQMKVINWQTSL 267
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1704602876 236 PEEEWSQISEMAKDVVRKLLKvKPEERLTIEGVLD---HPWLNSTE 278
Cdd:cd05625   268 HIPPQAKLSPEASDLIIKLCR-GPEDRLGKNGADEikaHPFFKTID 312
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
27-211 2.43e-07

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: 51.89  E-value: 2.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  27 KLGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLH-----MMCATHPNIVQIIEVfANSVQfphESSPRARLLIV 101
Cdd:cd14038     1 RLGTGGFGNVLRWINQETGEQVAIKQCRQELSPKNRERWCleiqiMKRLNHPNVVAARDV-PEGLQ---KLAPNDLPLLA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 102 MEMMEGGELFHRISQ--------------------------------HRHFT-EKQASQVTKQDAPVKLCDFGFAK-IDQ 147
Cdd:cd14038    77 MEYCQGGDLRKYLNQfenccglregailtllsdissalrylhenriiHRDLKpENIVLQQGEQRLIHKIIDLGYAKeLDQ 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1704602876 148 GDLMTpQF--TPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPF 211
Cdd:cd14038   157 GSLCT-SFvgTLQYLAPELLEQQK------------------YTVTVDYWSFGTLAFECITGFRPF 203
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
61-293 2.64e-07

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


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 52.35  E-value: 2.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  61 NEVRL--HMMCATHPNIVQIIEVFANSVQFphessprarllIVMEMMEGGELFHRISQ-HRHFteKQASQVTKQDAPVKL 137
Cdd:cd07877    95 NDVYLvtHLMGADLNNIVKCQKLTDDHVQF-----------LIYQILRGLKYIHSADIiHRDL--KPSNLAVNEDCELKI 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 138 CDFGFAKIDQGDLMTPQFTPYYVAPQVLeAQRRHqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHS 217
Cdd:cd07877   162 LDFGLARHTDDEMTGYVATRWYRAPEIM-LNWMH----------------YNQTVDIWSVGCIMAELLTGRTLFPGTDHI 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 218 ------------------RTIPKDMRRKIMTGSFEFPEEEWSQI----SEMAKDVVRKLLKVKPEERLTIEGVLDHPWLN 275
Cdd:cd07877   225 dqlklilrlvgtpgaellKKISSESARNYIQSLTQMPKMNFANVfigaNPLAVDLLEKMLVLDSDKRITAAQALAHAYFA 304
                         250       260
                  ....*....|....*....|....*..
gi 1704602876 276 S---------TEALDNVLPSAQLMMDK 293
Cdd:cd07877   305 QyhdpddepvADPYDQSFESRDLLIDE 331
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
28-274 3.04e-07

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: 51.38  E-value: 3.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALK-ILLDRPKARNEVR-LHMMCATHPNIVQIIEV-FANSVQFPHESSPRARLLIVMEM 104
Cdd:cd06628     8 IGSGSFGSVYLGMNASSGELMAVKqVELPSVSAENKDRkKSMLDALQREIALLRELqHENIVQYLGSSSDANHLNIFLEY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 105 MEGGELFHRISQHRHFTE---------------------------KQASQVTKQDAPVKLCDFGFAK-IDQGDLMTP--- 153
Cdd:cd06628    88 VPGGSVATLLNNYGAFEEslvrnfvrqilkglnylhnrgiihrdiKGANILVDNKGGIKISDFGISKkLEANSLSTKnng 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 154 -----QFTPYYVAPQVLeaqrrhqKEKSgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKdmrrki 228
Cdd:cd06628   168 arpslQGSVFWMAPEVV-------KQTS-----------YTRKADIWSLGCLVVEMLTGTHPFPDCTQMQAIFK------ 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1704602876 229 mTGSFEFPEEEwSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd06628   224 -IGENASPTIP-SNISSEARDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
26-274 3.67e-07

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


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 51.70  E-value: 3.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALK-ILLDRPK----ARNEVRLhMMCATHPNIVQIIEVFANSVQFPHES----SPRA 96
Cdd:cd07854    11 RPLGCGSNGLVFSAVDSDCDKRVAVKkIVLTDPQsvkhALREIKI-IRRLDHDNIVKVYEVLGPSGSDLTEDvgslTELN 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  97 RLLIVMEMMEGGelFHRISQHRHFTEKQASQVTKQ----------------------------DAPVKLCDFGFAKI--- 145
Cdd:cd07854    90 SVYIVQEYMETD--LANVLEQGPLSEEHARLFMYQllrglkyihsanvlhrdlkpanvfinteDLVLKIGDFGLARIvdp 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 146 ---DQGDLMTPQFTPYYVAPQVLeaqrrhqkeksgiipTSPTPYTynKSCDLWSLGVIIYVMLCGYPPFYSKH------- 215
Cdd:cd07854   168 hysHKGYLSEGLVTKWYRSPRLL---------------LSPNNYT--KAIDMWAAGCIFAEMLTGKPLFAGAHeleqmql 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 216 -------------------------HSRTIPKDMRRKIMTGsfefpeeewsqISEMAKDVVRKLLKVKPEERLTIEGVLD 270
Cdd:cd07854   231 ilesvpvvreedrnellnvipsfvrNDGGEPRRPLRDLLPG-----------VNPEALDFLEQILTFNPMDRLTAEEALM 299

                  ....
gi 1704602876 271 HPWL 274
Cdd:cd07854   300 HPYM 303
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
26-275 3.73e-07

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


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 52.01  E-value: 3.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALKiLLDRP--------KARNEVRLhMMCATHPNIVQIIEVFAnsvqfPHESSPRAR 97
Cdd:cd07874    23 KPIGSGAQGIVCAAYDAVLDRNVAIK-KLSRPfqnqthakRAYRELVL-MKCVNHKNIISLLNVFT-----PQKSLEEFQ 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  98 -LLIVMEMMEGG-------ELFH-RIS----------QHRHFTE------KQASQVTKQDAPVKLCDFGFAKIDQGD-LM 151
Cdd:cd07874    96 dVYLVMELMDANlcqviqmELDHeRMSyllyqmlcgiKHLHSAGiihrdlKPSNIVVKSDCTLKILDFGLARTAGTSfMM 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 152 TPQ-FTPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVML---------------------CGYP 209
Cdd:cd07874   176 TPYvVTRYYRAPEVILGM------------------GYKENVDIWSVGCIMGEMVrhkilfpgrdyidqwnkvieqLGTP 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1704602876 210 -PFYSKHHSRTIPKDMRRKIMTGSFEFP----------EEEWSQI-SEMAKDVVRKLLKVKPEERLTIEGVLDHPWLN 275
Cdd:cd07874   238 cPEFMKKLQPTVRNYVENRPKYAGLTFPklfpdslfpaDSEHNKLkASQARDLLSKMLVIDPAKRISVDEALQHPYIN 315
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
135-274 4.32e-07

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: 51.12  E-value: 4.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 135 VKLCDFGFAKIDQgDLMTPQF--TPYYVAPQVLEAQRRHqkeksgiiptsptpytyNKSCDLWSLGVIIYVMLCGYPPFy 212
Cdd:cd14100   146 LKLIDFGSGALLK-DTVYTDFdgTRVYSPPEWIRFHRYH-----------------GRSAAVWSLGILLYDMVCGDIPF- 206
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1704602876 213 skhhsrtipkDMRRKIMTGSFEFPEeewsQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14100   207 ----------EHDEEIIRGQVFFRQ----RVSSECQHLIKWCLALRPSDRPSFEDIQNHPWM 254
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
26-264 4.61e-07

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: 51.01  E-value: 4.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876   26 QKLGAGISGPVRVCV----KKSTQERFALKILLDRPKA------RNEVRLhMMCATHPNIVQIIEVfansvqfpheSSPR 95
Cdd:smart00221   5 KKLGEGAFGEVYKGTlkgkGDGKEVEVAVKTLKEDASEqqieefLREARI-MRKLDHPNIVKLLGV----------CTEE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876   96 ARLLIVMEMMEGGELFHRISQHRH--FTEKQ----ASQVTK-----------------------QDAPVKLCDFGFAK-I 145
Cdd:smart00221  74 EPLMIVMEYMPGGDLLDYLRKNRPkeLSLSDllsfALQIARgmeylesknfihrdlaarnclvgENLVVKISDFGLSRdL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  146 DQGDLMTPQFT--PY-YVAPQVLeaqrrhqkeKSGIiptsptpytYNKSCDLWSLGVIIYVML-CGYPPFYSKHhsrtiP 221
Cdd:smart00221 154 YDDDYYKVKGGklPIrWMAPESL---------KEGK---------FTSKSDVWSFGVLLWEIFtLGEEPYPGMS-----N 210
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1704602876  222 KDMRRKIMTGSFEFPEEEWSqiSEMAKdVVRKLLKVKPEERLT 264
Cdd:smart00221 211 AEVLEYLKKGYRLPKPPNCP--PELYK-LMLQCWAEDPEDRPT 250
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
156-271 5.67e-07

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 50.78  E-value: 5.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 156 TPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSkhhsrTIPKDMRRKIMTGSFEF 235
Cdd:cd14188   164 TPNYLSPEVLNKQ------------------GHGCESDIWALGCVMYTMLLGRPPFET-----TNLKETYRCIREARYSL 220
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1704602876 236 PeeewSQISEMAKDVVRKLLKVKPEERLTIEGVLDH 271
Cdd:cd14188   221 P----SSLLAPAKHLIASMLSKNPEDRPSLDEIIRH 252
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
96-211 6.16e-07

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: 50.88  E-value: 6.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  96 ARLLIVMEMMEGGELFHRISQHRHFTEKQA---------------------------SQVTKQDAPVKLCDFGFAK--ID 146
Cdd:cd05588    69 SRLFFVIEFVNGGDLMFHMQRQRRLPEEHArfysaeislalnflhekgiiyrdlkldNVLLDSEGHIKLTDYGMCKegLR 148
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1704602876 147 QGDLmTPQF--TPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPF 211
Cdd:cd05588   149 PGDT-TSTFcgTPNYIAPEILRGE------------------DYGFSVDWWALGVLMFEMLAGRSPF 196
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
135-274 6.17e-07

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: 50.51  E-value: 6.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 135 VKLCDFGFAK--------IDQGDLM-TPQFTPYYVAPQVLEaqrrhqkeKSGiiptsptpytYNKSCDLWSLGVIIYVML 205
Cdd:cd06631   142 IKLIDFGCAKrlcinlssGSQSQLLkSMRGTPYWMAPEVIN--------ETG----------HGRKSDIWSIGCTVFEMA 203
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1704602876 206 CGYPP----------FYSKHHSRTIPkdmrrkimtgsfEFPEeewsQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd06631   204 TGKPPwadmnpmaaiFAIGSGRKPVP------------RLPD----KFSPEARDFVHACLTRDQDERPSAEQLLKHPFI 266
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
26-273 8.69e-07

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


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 50.45  E-value: 8.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  26 QKLGAGISGPVRVCVKKSTQERFALK-ILLDRPK------ARNEVRLhMMCATHPNIVQIIEVFANSVQfpHESSPRARL 98
Cdd:cd07865    18 AKIGQGTFGEVFKARHRKTGQIVALKkVLMENEKegfpitALREIKI-LQLLKHENVVNLIEICRTKAT--PYNRYKGSI 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  99 LIVMEMMEG---------------GELFHRISQ--------HR----HFTEKQASQVTKQDAPVKLCDFGFA------KI 145
Cdd:cd07865    95 YLVFEFCEHdlagllsnknvkftlSEIKKVMKMllnglyyiHRnkilHRDMKAANILITKDGVLKLADFGLArafslaKN 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 146 DQGDLMTPQF-TPYYVAPQVLEAQRRhqkeksgiiptsptpytYNKSCDLWSLGVIIYVM-------------------- 204
Cdd:cd07865   175 SQPNRYTNRVvTLWYRPPELLLGERD-----------------YGPPIDMWGAGCIMAEMwtrspimqgnteqhqltlis 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 205 -LCG------YP-----PFYSKhhsRTIPKDMRRKImtgsfefPEEEWSQISEM-AKDVVRKLLKVKPEERLTIEGVLDH 271
Cdd:cd07865   238 qLCGsitpevWPgvdklELFKK---MELPQGQKRKV-------KERLKPYVKDPyALDLIDKLLVLDPAKRIDADTALNH 307

                  ..
gi 1704602876 272 PW 273
Cdd:cd07865   308 DF 309
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
72-273 1.00e-06

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 50.26  E-value: 1.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  72 HPNIVQIIEVFansvqfPHESSprarLLIVMEMMEG--------GELFHRISQ---------------HRHFTE----KQ 124
Cdd:cd07841    61 HPNIIGLLDVF------GHKSN----INLVFEFMETdlekvikdKSIVLTPADiksymlmtlrgleylHSNWILhrdlKP 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 125 ASQVTKQDAPVKLCDFGFAKI--DQGDLMTPQ-FTPYYVAPQVLEAQRrhqkeksgiiptsptpyTYNKSCDLWSLGVII 201
Cdd:cd07841   131 NNLLIASDGVLKLADFGLARSfgSPNRKMTHQvVTRWYRAPELLFGAR-----------------HYGVGVDMWSVGCIF 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 202 YVMLCGYPPFYSkhhsrTIPKDMRRKIMT--GSFEfpEEEW------------------------SQISEMAKDVVRKLL 255
Cdd:cd07841   194 AELLLRVPFLPG-----DSDIDQLGKIFEalGTPT--EENWpgvtslpdyvefkpfpptplkqifPAASDDALDLLQRLL 266
                         250
                  ....*....|....*...
gi 1704602876 256 KVKPEERLTIEGVLDHPW 273
Cdd:cd07841   267 TLNPNKRITARQALEHPY 284
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
27-273 1.07e-06

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


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 50.06  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  27 KLGAGISGPVRVCVKKSTQERFALK-ILLDRPK------ARNEVRLHMMCaTHPNIVQIIEVFA----NSVQFPHESSPR 95
Cdd:cd07845    14 RIGEGTYGIVYRARDTTSGEIVALKkVRMDNERdgipisSLREITLLLNL-RHPNIVELKEVVVgkhlDSIFLVMEYCEQ 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  96 --ARLL--------------IVMEMMEGGELFH-RISQHRHFteKQASQVTKQDAPVKLCDFGFAKI--DQGDLMTPQF- 155
Cdd:cd07845    93 dlASLLdnmptpfsesqvkcLMLQLLRGLQYLHeNFIIHRDL--KVSNLLLTDKGCLKIADFGLARTygLPAKPMTPKVv 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 156 TPYYVAPQVLEAQRrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHH--------------SRTIP 221
Cdd:cd07845   171 TLWYRAPELLLGCT-----------------TYTTAIDMWAVGCILAELLAHKPLLPGKSEieqldliiqllgtpNESIW 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1704602876 222 KDMRRKIMTGSFEFPEEEWSQ-------ISEMAKDVVRKLLKVKPEERLTIEGVLDHPW 273
Cdd:cd07845   234 PGFSDLPLVGKFTLPKQPYNNlkhkfpwLSEAGLRLLNFLLMYDPKKRATAEEALESSY 292
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
96-263 1.25e-06

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: 50.40  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  96 ARLLIVMEMMEGGELFHRISQHRHFTEKQA---------------------------SQVTKQDAPVKLCDFGFAK--ID 146
Cdd:cd05617    89 SRLFLVIEYVNGGDLMFHMQRQRKLPEEHArfyaaeicialnflhergiiyrdlkldNVLLDADGHIKLTDYGMCKegLG 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 147 QGDlMTPQF--TPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPF--YSKHHSRTIPK 222
Cdd:cd05617   169 PGD-TTSTFcgTPNYIAPEILRGEE------------------YGFSVDWWALGVLMFEMMAGRSPFdiITDNPDMNTED 229
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1704602876 223 DMRRKIMTGSFEFPEeewsQISEMAKDVVRKLLKVKPEERL 263
Cdd:cd05617   230 YLFQVILEKPIRIPR----FLSVKASHVLKGFLNKDPKERL 266
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
137-274 1.29e-06

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: 49.53  E-value: 1.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 137 LCDFGFAkidQGDLMTPQF------TPYYVAPQVLeaqRRHQKEKSGIiptsptpytynkscDLWSLGVIIYVMLCG-YP 209
Cdd:cd14019   143 LVDFGLA---QREEDRPEQrapragTRGFRAPEVL---FKCPHQTTAI--------------DIWSAGVILLSILSGrFP 202
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1704602876 210 PFYSKHhsrtiPKDMRRKIMT--GSFEfpeeewsqisemAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14019   203 FFFSSD-----DIDALAEIATifGSDE------------AYDLLDKLLELDPSKRITAEEALKHPFF 252
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
156-283 1.42e-06

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: 50.01  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 156 TPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKhhsrtIPKDMRRKIMT--GSF 233
Cdd:cd05626   211 TPNYIAPEVLLRK------------------GYTQLCDWWSVGVILFEMLVGQPPFLAP-----TPTETQLKVINweNTL 267
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1704602876 234 EFPEEewSQISEMAKDVVRKLLkVKPEERLTIEGVLD---HPWLNSTEALDNV 283
Cdd:cd05626   268 HIPPQ--VKLSPEAVDLITKLC-CSAEERLGRNGADDikaHPFFSEVDFSSDI 317
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
192-271 1.70e-06

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


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 49.22  E-value: 1.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 192 CDLWSLGVIIYVMLCGYPPF---YSKHHSrtipkdMRRKIMTGSFEFPEEewSQISEMAKDVVRKLLKVKPEERLTIEGV 268
Cdd:cd13986   202 TDIWSLGCTLYALMYGESPFeriFQKGDS------LALAVLSGNYSFPDN--SRYSEELHQLVKSMLVVNPAERPSIDDL 273

                  ...
gi 1704602876 269 LDH 271
Cdd:cd13986   274 LSR 276
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
25-270 2.21e-06

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: 48.92  E-value: 2.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  25 TQKLGAGISGPVRVCVKKStqERFALKILLDRPK---ARNEVR--LHMMCATHPNIVQIIEVFAnsvqfpheSSPRARL- 98
Cdd:cd13979     8 QEPLGSGGFGSVYKATYKG--ETVAVKIVRRRRKnraSRQSFWaeLNAARLRHENIVRVLAAET--------GTDFASLg 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  99 LIVMEMMEGGELFHRI--------SQHR--------------------HFTEKQAS-QVTKQDAPvKLCDFG-----FAK 144
Cdd:cd13979    78 LIIMEYCGNGTLQQLIyegseplpLAHRilisldiaralrfchshgivHLDVKPANiLISEQGVC-KLCDFGcsvklGEG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 145 IDQGDLMTPQF-TPYYVAPQVLEAQRrhqkeksgiiptsPTPytynKScDLWSLGVIIYVMLCGYPPFYSKHHS---RTI 220
Cdd:cd13979   157 NEVGTPRSHIGgTYTYRAPELLKGER-------------VTP----KA-DIYSFGITLWQMLTRELPYAGLRQHvlyAVV 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1704602876 221 PKDMrRKIMTGSFEFPEEEWsqisemAKDVVRKLLKVKPEERLTIEGVLD 270
Cdd:cd13979   219 AKDL-RPDLSGLEDSEFGQR------LRSLISRCWSAQPAERPNADESLL 261
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
12-263 2.98e-06

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: 49.26  E-value: 2.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  12 KETSILEEYSINWTQKLGAGISGPVRVCVKKSTQERFALKILL--------DRPKARNEVRLHMMCATHPNIVQIIEVFA 83
Cdd:cd05618    12 KASSSLGLQDFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKkelvnddeDIDWVQTEKHVFEQASNHPFLVGLHSCFQ 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  84 NsvqfphesspRARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ---------------------------DAPVK 136
Cdd:cd05618    92 T----------ESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEislalnylhergiiyrdlkldnvlldsEGHIK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 137 LCDFGFAK--IDQGDlMTPQF--TPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPF- 211
Cdd:cd05618   162 LTDYGMCKegLRPGD-TTSTFcgTPNYIAPEILRGE------------------DYGFSVDWWALGVLMFEMMAGRSPFd 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1704602876 212 ---YSKHHSRTIPKDMRRKIMTGSFEFPEeewsQISEMAKDVVRKLLKVKPEERL 263
Cdd:cd05618   223 ivgSSDNPDQNTEDYLFQVILEKQIRIPR----SLSVKAASVLKSFLNKDPKERL 273
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
131-274 3.15e-06

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: 48.46  E-value: 3.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 131 QDAPVKLCDFGF-AKIDQ--GDLMTPQFTPYYVAPQVLEAQRRhqkeksgiiPTSptpyTYNKSCDLWSLGVIIYVMLCG 207
Cdd:cd06636   156 ENAEVKLVDFGVsAQLDRtvGRRNTFIGTPYWMAPEVIACDEN---------PDA----TYDYRSDIWSLGITAIEMAEG 222
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1704602876 208 YPPFYSKHHSRT---IPKDMRRKIMTgsfefpeEEWSQ--ISEMAKDVVRKLLKVKPEERLtiegvLDHPWL 274
Cdd:cd06636   223 APPLCDMHPMRAlflIPRNPPPKLKS-------KKWSKkfIDFIEGCLVKNYLSRPSTEQL-----LKHPFI 282
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
72-274 3.94e-06

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


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 48.42  E-value: 3.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  72 HPNIVQIIEVFANS---------VQFPH---------ESSPRARLLI-----VMEMMEGGELFHRISQHRHFTEKQASQV 128
Cdd:cd07863    61 HPNIVRLMDVCATSrtdretkvtLVFEHvdqdlrtylDKVPPPGLPAetikdLMRQFLRGLDFLHANCIVHRDLKPENIL 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 129 TKQDAPVKLCDFGFAKIDQGDL-MTP-QFTPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLC 206
Cdd:cd07863   141 VTSGGQVKLADFGLARIYSCQMaLTPvVVTLWYRAPEVLLQS------------------TYATPVDMWSVGCIFAEMFR 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 207 GYPPFYSKHHSrtipkDMRRKIMTGSFEFPEEEW-----------------------SQISEMAKDVVRKLLKVKPEERL 263
Cdd:cd07863   203 RKPLFCGNSEA-----DQLGKIFDLIGLPPEDDWprdvtlprgafsprgprpvqsvvPEIEESGAQLLLEMLTFNPHKRI 277
                         250
                  ....*....|.
gi 1704602876 264 TIEGVLDHPWL 274
Cdd:cd07863   278 SAFRALQHPFF 288
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
28-274 4.00e-06

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


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 48.17  E-value: 4.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILLDRPKAR-----NEVRLHMMCaTHPNIVQIIEVFANSVQFphessprarlLIVM 102
Cdd:cd06624    16 LGKGTFGVVYAARDLSTQVRIAIKEIPERDSREvqplhEEIALHSRL-SHKNIVQYLGSVSEDGFF----------KIFM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 103 EMMEGGELFHRISQH-----------RHFTeKQ---------ASQVTKQD------------APVKLCDFGFAKIDQG-D 149
Cdd:cd06624    85 EQVPGGSLSALLRSKwgplkdnentiGYYT-KQileglkylhDNKIVHRDikgdnvlvntysGVVKISDFGTSKRLAGiN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 150 LMTPQF--TPYYVAPQVLEAQRRhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHsrtiPKDMRRK 227
Cdd:cd06624   164 PCTETFtgTLQYMAPEVIDKGQR----------------GYGPPADIWSLGCTIIEMATGKPPFIELGE----PQAAMFK 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1704602876 228 ImtGSF----EFPEEewsqISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd06624   224 V--GMFkihpEIPES----LSEEAKSFILRCFEPDPDKRATASDLLQDPFL 268
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
135-274 4.70e-06

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: 47.92  E-value: 4.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 135 VKLCDFGFAkidqGDLM-----TPQFTPYYVAPQVLeaqrrhqkeKSGIIPTSPTpytYNKSCDLWSLGVIIYVMLCG-- 207
Cdd:cd06622   142 VKLCDFGVS----GNLVaslakTNIGCQSYMAPERI---------KSGGPNQNPT---YTVQSDVWSLGLSILEMALGry 205
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1704602876 208 -YPP-FYSKHHSRTipkdmrRKIMTGSfefPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd06622   206 pYPPeTYANIFAQL------SAIVDGD---PPTLPSGYSDDAQDFVAKCLNKIPNRRPTYAQLLEHPWL 265
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
100-274 7.09e-06

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: 47.79  E-value: 7.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMEGGELFHrisQHR--HFTEKQASQVTKQDAPVKLCDFGF-AKIDQ--GDLMTPQFTPYYVAPQVLEAQRRhqke 174
Cdd:cd06637   116 ICREILRGLSHLH---QHKviHRDIKGQNVLLTENAEVKLVDFGVsAQLDRtvGRRNTFIGTPYWMAPEVIACDEN---- 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 175 ksgiiPTSptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRT---IPKDMRRKIMTgsfefpeEEWSQiseMAKDVV 251
Cdd:cd06637   189 -----PDA----TYDFKSDLWSLGITAIEMAEGAPPLCDMHPMRAlflIPRNPAPRLKS-------KKWSK---KFQSFI 249
                         170       180
                  ....*....|....*....|...
gi 1704602876 252 RKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd06637   250 ESCLVKNHSQRPSTEQLMKHPFI 272
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
135-272 8.14e-06

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: 47.57  E-value: 8.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 135 VKLCDFGFAKIDQG------DLMTpqfTPYYVAPQVLEAQRRHQ--KEKSGIIPTSPTPYTYNKSC-------------- 192
Cdd:cd05610   143 IKLTDFGLSKVTLNrelnmmDILT---TPSMAKPKNDYSRTPGQvlSLISSLGFNTPTPYRTPKSVrrgaarvegerilg 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 193 -------------------DLWSLGVIIYVMLCGYPPFYSKhhsrtIPKDMRRKIMTGSFEFPEEEwSQISEMAKDVVRK 253
Cdd:cd05610   220 tpdylapelllgkphgpavDWWALGVCLFEFLTGIPPFNDE-----TPQQVFQNILNRDIPWPEGE-EELSVNAQNAIEI 293
                         170
                  ....*....|....*....
gi 1704602876 254 LLKVKPEERLTIEGVLDHP 272
Cdd:cd05610   294 LLTMDPTKRAGLKELKQHP 312
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
43-272 8.18e-06

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


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 47.50  E-value: 8.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  43 STQERFALKILLDRPKARN-EVRLhMMCATHPNIVQIIEVFansvQFPHESSPRARLLIVMEMMEggELFHRIsqHRHFT 121
Cdd:cd14137    27 ETGEVVAIKKVLQDKRYKNrELQI-MRRLKHPNIVKLKYFF----YSSGEKKDEVYLNLVMEYMP--ETLYRV--IRHYS 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 122 EKQ-----------ASQ------------------------VTKQDAPVKLCDFGFAK-IDQGDLMTP-QFTPYYVAPQ- 163
Cdd:cd14137    98 KNKqtipiiyvklySYQlfrglaylhslgichrdikpqnllVDPETGVLKLCDFGSAKrLVPGEPNVSyICSRYYRAPEl 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 164 VLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFyskhHSRTiPKDMRRKIMT--GSfefPEEEws 241
Cdd:cd14137   178 IFGAT------------------DYTTAIDIWSAGCVLAELLLGQPLF----PGES-SVDQLVEIIKvlGT---PTRE-- 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1704602876 242 QISEM----------------------------AKDVVRKLLKVKPEERLTIEGVLDHP 272
Cdd:cd14137   230 QIKAMnpnytefkfpqikphpwekvfpkrtppdAIDLLSKILVYNPSKRLTALEALAHP 288
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
28-274 9.97e-06

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: 47.35  E-value: 9.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKiLLDRP--------KARNEVRL--HMmcaTHPNIVQIIEVFA-------------- 83
Cdd:cd07878    23 VGSGAYGSVCSAYDTRLRQKVAVK-KLSRPfqsliharRTYRELRLlkHM---KHENVIGLLDVFTpatsienfnevylv 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  84 ---------NSVQFPHESSPRARLLIvMEMMEGGELFHRISQ-HRHFteKQASQVTKQDAPVKLCDFGFAKIDQGDLMTP 153
Cdd:cd07878    99 tnlmgadlnNIVKCQKLSDEHVQFLI-YQLLRGLKYIHSAGIiHRDL--KPSNVAVNEDCELRILDFGLARQADDEMTGY 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 154 QFTPYYVAPQVLeAQRRHqkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPPF----YSKHHSR----------- 218
Cdd:cd07878   176 VATRWYRAPEIM-LNWMH----------------YNQTVDIWSVGCIMAELLKGKALFpgndYIDQLKRimevvgtpspe 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1704602876 219 ---TIPKDMRRKIMTGSFEFPEEEWSQI----SEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd07878   239 vlkKISSEHARKYIQSLPHMPQQDLKKIfrgaNPLAIDLLEKMLVLDSDKRISASEALAHPYF 301
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
100-274 1.25e-05

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: 46.59  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMEGGELFHRiSQHRHFTEKQASQVTKQDAPVKLCDFGFAkidqGDLMTPQF-------TPYYVAPQVLEAQrrhq 172
Cdd:cd06642   106 ILREILKGLDYLHS-ERKIHRDIKAANVLLSEQGDVKLADFGVA----GQLTDTQIkrntfvgTPFWMAPEVIKQS---- 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 173 keksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRT---IPKDMrrkimtgsfefPEEEWSQISEMAKD 249
Cdd:cd06642   177 --------------AYDFKADIWSLGITAIELAKGEPPNSDLHPMRVlflIPKNS-----------PPTLEGQHSKPFKE 231
                         170       180
                  ....*....|....*....|....*
gi 1704602876 250 VVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd06642   232 FVEACLNKDPRFRPTAKELLKHKFI 256
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
22-273 1.39e-05

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: 46.61  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  22 INWTQK--LGAGISGPVRVCVKKSTQERFALKILL---DRPKARNEVRLhMMCAthpniVQIIEVFANSVQFPHESSPRA 96
Cdd:cd06651     7 INWRRGklLGQGAFGRVYLCYDVDTGRELAAKQVQfdpESPETSKEVSA-LECE-----IQLLKNLQHERIVQYYGCLRD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  97 R----LLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQ---------------------------DAPVKLCDFGFAKI 145
Cdd:cd06651    81 RaektLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQilegmsylhsnmivhrdikganilrdsAGNVKLGDFGASKR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 146 DQGDLMTPQF------TPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRT 219
Cdd:cd06651   161 LQTICMSGTGirsvtgTPYWMSPEVISGE------------------GYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAA 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1704602876 220 IpkdmrRKIMTGSFEFPEEewSQISEMAKDVVRKLLkVKPEERLTIEGVLDHPW 273
Cdd:cd06651   223 I-----FKIATQPTNPQLP--SHISEHARDFLGCIF-VEARHRPSAEELLRHPF 268
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
22-231 1.50e-05

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


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 46.34  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  22 INWTQKLGAGISGPVRVCV----KKSTQERFALKILldRPKARNEVR------LHMMCAT-HPNIVQIIEVfansvqfph 90
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTlkgeGENTKIKVAVKTL--KEGADEEERedfleeASIMKKLdHPNIVKLLGV--------- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  91 eSSPRARLLIVMEMMEGGELFHRISQHR-HFTEKQASQVTKQDAP---------------------------VKLCDFGF 142
Cdd:pfam07714  70 -CTQGEPLYIVTEYMPGGDLLDFLRKHKrKLTLKDLLSMALQIAKgmeylesknfvhrdlaarnclvsenlvVKISDFGL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 143 AK-IDQGDLMTPQ---FTPY-YVAPQVLEAQRrhqkeksgiiptsptpYTYnKScDLWSLGVIIYVMLC-GYPPFYSKHh 216
Cdd:pfam07714 149 SRdIYDDDYYRKRgggKLPIkWMAPESLKDGK----------------FTS-KS-DVWSFGVLLWEIFTlGEQPYPGMS- 209
                         250
                  ....*....|....*
gi 1704602876 217 srtiPKDMRRKIMTG 231
Cdd:pfam07714 210 ----NEEVLEFLEDG 220
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
60-211 1.63e-05

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: 46.23  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  60 RNEVRLHMMCAtHPNIVQIIEVfanSVQFPHessprarLLIVMEMMEGGELFHRISQHR---HFTEKQASQVTK------ 130
Cdd:cd14061    41 RQEARLFWMLR-HPNIIALRGV---CLQPPN-------LCLVMEYARGGALNRVLAGRKippHVLVDWAIQIARgmnylh 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 131 QDAPV----------------------------KLCDFGFAK-IDQGDLMTPQFTPYYVAPQVLEAQrrhqkeksgiipt 181
Cdd:cd14061   110 NEAPVpiihrdlkssnilileaienedlenktlKITDFGLAReWHKTTRMSAAGTYAWMAPEVIKSS------------- 176
                         170       180       190
                  ....*....|....*....|....*....|
gi 1704602876 182 sptpyTYNKSCDLWSLGVIIYVMLCGYPPF 211
Cdd:cd14061   177 -----TFSKASDVWSYGVLLWELLTGEVPY 201
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
59-274 1.83e-05

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: 46.20  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  59 ARNEVRLHMMCaTHPNIVQIIEVFANSVQfphesspraRLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQD------ 132
Cdd:cd14040    57 ACREYRIHKEL-DHPRIVKLYDYFSLDTD---------TFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIvnalry 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 133 --------------------------APVKLCDFGFAKIDQGDL-------MTPQF--TPYYVAPQVLeaqrrhqkeksg 177
Cdd:cd14040   127 lneikppiihydlkpgnillvdgtacGEIKITDFGLSKIMDDDSygvdgmdLTSQGagTYWYLPPECF------------ 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 178 IIPTSPtPYTYNKsCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDmRRKIMTGSFEFPEEewSQISEMAKDVVRKLLKV 257
Cdd:cd14040   195 VVGKEP-PKISNK-VDVWSVGVIFFQCLYGRKPFGHNQSQQDILQE-NTILKATEVQFPVK--PVVSNEAKAFIRRCLAY 269
                         250
                  ....*....|....*..
gi 1704602876 258 KPEERLTIEGVLDHPWL 274
Cdd:cd14040   270 RKEDRFDVHQLASDPYL 286
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
128-274 1.86e-05

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: 45.99  E-value: 1.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 128 VTKQDAPVKLCDFGFA-KIDQGDLMTPQFTPYYVAPQVleaqrrHQKEkSGIIPTSptpytynkscDLWSLGVIIYVMLC 206
Cdd:cd14112   133 QSVRSWQVKLVDFGRAqKVSKLGKVPVDGDTDWASPEF------HNPE-TPITVQS----------DIWGLGVLTFCLLS 195
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1704602876 207 GYPPFYSKHHSRTipkDMRRKIMTGSFEfPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14112   196 GFHPFTSEYDDEE---ETKENVIFVKCR-PNLIFVEATQEALRFATWALKKSPTRRMRTDEALEHRWL 259
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
97-288 2.03e-05

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


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 46.31  E-value: 2.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  97 RLLIVMEMMEGGELFHRisqhrhfTEKQASQVTKQDAPVKLCDFGFAKIDQGDLMTPQFTPYYVAPQVLEAqrrhqKEKS 176
Cdd:cd07859   111 QLLRALKYIHTANVFHR-------DLKPKNILANADCKLKICDFGLARVAFNDTPTAIFWTDYVATRWYRA-----PELC 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 177 GIIPTSPTPytynkSCDLWSLGVIIYVMLCGYPPFYSKH--HSRTIPKDM-----------------RRKIMTGSFEFP- 236
Cdd:cd07859   179 GSFFSKYTP-----AIDIWSIGCIFAEVLTGKPLFPGKNvvHQLDLITDLlgtpspetisrvrnekaRRYLSSMRKKQPv 253
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1704602876 237 --EEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEALDNVlPSAQ 288
Cdd:cd07859   254 pfSQKFPNADPLALRLLERLLAFDPKDRPTAEEALADPYFKGLAKVERE-PSAQ 306
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
59-274 3.71e-05

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: 45.44  E-value: 3.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  59 ARNEVRLHMMCaTHPNIVQIIEVFansvqfpheSSPRARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQD------ 132
Cdd:cd14041    57 ACREYRIHKEL-DHPRIVKLYDYF---------SLDTDSFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIvnalky 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 133 --------------------------APVKLCDFGFAKIDQGD--------LMTPQF--TPYYVAPQVLeaqrrhqkeks 176
Cdd:cd14041   127 lneikppiihydlkpgnillvngtacGEIKITDFGLSKIMDDDsynsvdgmELTSQGagTYWYLPPECF----------- 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 177 gIIPTSPtPYTYNKsCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDmRRKIMTGSFEFPEEewSQISEMAKDVVRKLLK 256
Cdd:cd14041   196 -VVGKEP-PKISNK-VDVWSVGVIFYQCLYGRKPFGHNQSQQDILQE-NTILKATEVQFPPK--PVVTPEAKAFIRRCLA 269
                         250
                  ....*....|....*...
gi 1704602876 257 VKPEERLTIEGVLDHPWL 274
Cdd:cd14041   270 YRKEDRIDVQQLACDPYL 287
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
118-274 4.28e-05

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


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 45.39  E-value: 4.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 118 RHFTEKQASQVTKQDAPVKLCDFGFAKIDQGDLMTPQFTPYYVAPQVLeaqrrhqkeksgiiptspTPYTYNKSCDLWSL 197
Cdd:cd14215   157 TYNLEKKRDERSVKSTAIRVVDFGSATFDHEHHSTIVSTRHYRAPEVI------------------LELGWSQPCDVWSI 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 198 GVIIYVMLCGYPPFYSkHHSRT-----------IPKDMRRKIMTGSFEFPEE-EWSQISEMAK----------------- 248
Cdd:cd14215   219 GCIIFEYYVGFTLFQT-HDNREhlammerilgpIPSRMIRKTRKQKYFYHGRlDWDENTSAGRyvrenckplrryltsea 297
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1704602876 249 -------DVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd14215   298 eehhqlfDLIESMLEYEPSKRLTLAAALKHPFF 330
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
136-262 5.52e-05

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


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 44.91  E-value: 5.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 136 KLCDFGFAK-IDQGDLMTpQF--TPYYVAPQVLEAQrrhqkeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFY 212
Cdd:cd14039   142 KIIDLGYAKdLDQGSLCT-SFvgTLQYLAPELFENK------------------SYTVTVDYWSFGTMVFECIAGFRPFL 202
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1704602876 213 S-----KHHSRTIPKD----MRRKIMTGSFEF------PEEEWSQISEMAKDVVRKLLKVKPEER 262
Cdd:cd14039   203 HnlqpfTWHEKIKKKDpkhiFAVEEMNGEVRFsthlpqPNNLCSLIVEPMEGWLQLMLNWDPVQR 267
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
22-274 7.24e-05

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: 44.48  E-value: 7.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  22 INWTQKLGAGISGPVRVCVKKSTQERFALK-ILLD-----RPKARNEVRLHMMCAThPNIVQIIEVFansvqFPHEsspr 95
Cdd:cd06619     3 IQYQEILGHGNGGTVYKAYHLLTRRILAVKvIPLDitvelQKQIMSELEILYKCDS-PYIIGFYGAF-----FVEN---- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  96 aRLLIVMEMMEGGEL--FHRISQH---------------------RHFTEKQASQVTKQDAPVKLCDFGFAKidqgdLMT 152
Cdd:cd06619    73 -RISICTEFMDGGSLdvYRKIPEHvlgriavavvkgltylwslkiLHRDVKPSNMLVNTRGQVKLCDFGVST-----QLV 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 153 PQFTPYYVAPQVLEAQRRHQKEKSGIIptsptpytynksCDLWSLGVIIYVMLCG---YPPFYsKHHSRTIPKDMRRKIM 229
Cdd:cd06619   147 NSIAKTYVGTNAYMAPERISGEQYGIH------------SDVWSLGISFMELALGrfpYPQIQ-KNQGSLMPLQLLQCIV 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1704602876 230 TGsfEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd06619   214 DE--DPPVLPVGQFSEKFVHFITQCMRKQPKERPAPENLMDHPFI 256
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
28-254 1.16e-04

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: 43.88  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  28 LGAGISGPVRVCVKKSTQERFALKILlDRPK---------ARNEVRLHMMCATH--PNIVQIIEVFansvqfpheSSPRa 96
Cdd:cd14223     8 IGRGGFGEVYGCRKADTGKMYAMKCL-DKKRikmkqgetlALNERIMLSLVSTGdcPFIVCMSYAF---------HTPD- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  97 RLLIVMEMMEGGELFHRISQHRHFTE---------------------------KQASQVTKQDAPVKLCDFGFA-KIDQG 148
Cdd:cd14223    77 KLSFILDLMNGGDLHYHLSQHGVFSEaemrfyaaeiilglehmhsrfvvyrdlKPANILLDEFGHVRISDLGLAcDFSKK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 149 DLMTPQFTPYYVAPQVLEaqrrhqkekSGIiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFysKHHSRTIPKDMRRKI 228
Cdd:cd14223   157 KPHASVGTHGYMAPEVLQ---------KGV--------AYDSSADWFSLGCMLFKLLRGHSPF--RQHKTKDKHEIDRMT 217
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1704602876 229 MTGSFEFPEE---EWSQISE--MAKDVVRKL 254
Cdd:cd14223   218 LTMAVELPDSfspELRSLLEglLQRDVNRRL 248
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
135-274 2.17e-04

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


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 43.19  E-value: 2.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 135 VKLCDFGFAKI---DQGDLMTPQ-FTPYYVAPQVLEAQRRhqkeksgiiptsptpytYNKSCDLWSLGVIIYVML----- 205
Cdd:cd07853   142 LKICDFGLARVeepDESKHMTQEvVTQYYRAPEILMGSRH-----------------YTSAVDIWSVGCIFAELLgrril 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 206 ----------------CGYPPFYSKHHSRTIPKD--MRRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEG 267
Cdd:cd07853   205 fqaqspiqqldlitdlLGTPSLEAMRSACEGARAhiLRGPHKPPSLPVLYTLSSQATHEAVHLLCRMLVFDPDKRISAAD 284

                  ....*..
gi 1704602876 268 VLDHPWL 274
Cdd:cd07853   285 ALAHPYL 291
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
100-274 2.78e-04

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


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 42.75  E-value: 2.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMEGGELFHRiSQHRHFTEKQASQVTKQDAPVKLCDFGFAkidqGDLMTPQF-------TPYYVAPQVLEAQrrhq 172
Cdd:cd06641   106 ILREILKGLDYLHS-EKKIHRDIKAANVLLSEHGEVKLADFGVA----GQLTDTQIkrn*fvgTPFWMAPEVIKQS---- 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 173 keksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRT---IPKDmRRKIMTGSFefpeeewsqiSEMAKD 249
Cdd:cd06641   177 --------------AYDSKADIWSLGITAIELARGEPPHSELHPMKVlflIPKN-NPPTLEGNY----------SKPLKE 231
                         170       180
                  ....*....|....*....|....*
gi 1704602876 250 VVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd06641   232 FVEACLNKEPSFRPTAKELLKHKFI 256
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
100-274 5.00e-04

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


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 41.96  E-value: 5.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 100 IVMEMMEGGELFHRiSQHRHFTEKQASQVTKQDAPVKLCDFGFAkidqGDLMTPQF-------TPYYVAPQVLEAQrrhq 172
Cdd:cd06640   106 MLKEILKGLDYLHS-EKKIHRDIKAANVLLSEQGDVKLADFGVA----GQLTDTQIkrntfvgTPFWMAPEVIQQS---- 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 173 keksgiiptsptpyTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRT---IPKDmRRKIMTGSFefpeeewsqiSEMAKD 249
Cdd:cd06640   177 --------------AYDSKADIWSLGITAIELAKGEPPNSDMHPMRVlflIPKN-NPPTLVGDF----------SKPFKE 231
                         170       180
                  ....*....|....*....|....*
gi 1704602876 250 VVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd06640   232 FIDACLNKDPSFRPTAKELLKHKFI 256
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
54-269 5.12e-04

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 41.55  E-value: 5.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  54 LDRPKARNEVRLHMMCATHPNIVQIIEVFANSVQFPHESSPR---ARLLIVMEMMEGGELFHRisqhrhfTEKQASQVTK 130
Cdd:cd08228    68 LDSFIEDNELNIVLELADAGDLSQMIKYFKKQKRLIPERTVWkyfVQLCSAVEHMHSRRVMHR-------DIKPANVFIT 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 131 QDAPVKLCDFGFAKIDQGDLMTPQF---TPYYVAPQvleaqRRHQKeksgiiptsptpyTYNKSCDLWSLGVIIYVMLCG 207
Cdd:cd08228   141 ATGVVKLGDLGLGRFFSSKTTAAHSlvgTPYYMSPE-----RIHEN-------------GYNFKSDIWSLGCLLYEMAAL 202
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1704602876 208 YPPFYSKHHSRTipkDMRRKIMtgSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVL 269
Cdd:cd08228   203 QSPFYGDKMNLF---SLCQKIE--QCDYPPLPTEHYSEKLRELVSMCIYPDPDQRPDIGYVH 259
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
136-276 8.47e-04

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: 41.15  E-value: 8.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 136 KLCDFGFA-KIDQGdlmTPQFTPYyvapqvleaqrrHQKEKSGIIPTSPTP------YTYNKSC----DLWSLGVIIYVM 204
Cdd:cd14011   155 KLAGFDFCiSSEQA---TDQFPYF------------REYDPNLPPLAQPNLnylapeYILSKTCdpasDMFSLGVLIYAI 219
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1704602876 205 LC-GYPPFYSKHHsRTIPKDMRRKIMTGSFefpeEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNS 276
Cdd:cd14011   220 YNkGKPLFDCVNN-LLSYKKNSNQLRQLSL----SLLEKVPEELRDHVKTLLNVTPEVRPDAEQLSKIPFFDD 287
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
135-271 1.04e-03

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: 40.82  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 135 VKLCDFGFAK---------------------IDQGDLMTPQFTPYYVAPQVLeaqrrhqkeksgiiptSPTPYTYNKSCD 193
Cdd:cd14046   143 VKIGDFGLATsnklnvelatqdinkstsaalGSSGDLTGNVGTALYVAPEVQ----------------SGTKSTYNEKVD 206
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1704602876 194 LWSLGVIIYVMLcgYPPFYSKHHSRTIpkdmrRKIMTGSFEFPEE-EWSQISEMAKdVVRKLLKVKPEERLTIEGVLDH 271
Cdd:cd14046   207 MYSLGIIFFEMC--YPFSTGMERVQIL-----TALRSVSIEFPPDfDDNKHSKQAK-LIRWLLNHDPAKRPSAQELLKS 277
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
135-274 1.23e-03

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


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 40.78  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 135 VKLCDFGFAKIdqgdlMTPQF----TPYYVAPQVLEAQRRHQkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPP 210
Cdd:cd06634   154 VKLGDFGSASI-----MAPANsfvgTPYWMAPEVILAMDEGQ---------------YDGKVDVWSLGITCIELAERKPP 213
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1704602876 211 FYSKHHsrtipkdMRRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWL 274
Cdd:cd06634   214 LFNMNA-------MSALYHIAQNESPALQSGHWSEYFRNFVDSCLQKIPQDRPTSDVLLKHRFL 270
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
18-202 2.18e-03

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


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 39.88  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  18 EEYSINWTQKLGAGISGPVRVC----VKKSTQERFALKILL-DRPKARNEVR--LHMMCATHPNIVqiieVFANSVQFph 90
Cdd:cd05081     2 EERHLKYISQLGKGNFGSVELCrydpLGDNTGALVAVKQLQhSGPDQQRDFQreIQILKALHSDFI----VKYRGVSY-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  91 eSSPRARLLIVMEMMEGGELFHRISQHRHFTEKQ-----ASQVTK-----------------------QDAPVKLCDFGF 142
Cdd:cd05081    76 -GPGRRSLRLVMEYLPSGCLRDFLQRHRARLDASrlllySSQICKgmeylgsrrcvhrdlaarnilveSEAHVKIADFGL 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1704602876 143 AKIdqgdlmTPQFTPYYVApqvleaqrrHQKEKSGII---PTSPTPYTYNKSCDLWSLGVIIY 202
Cdd:cd05081   155 AKL------LPLDKDYYVV---------REPGQSPIFwyaPESLSDNIFSRQSDVWSFGVVLY 202
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
72-274 2.36e-03

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: 39.52  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  72 HPNIVQIIEVFansvqfphESSPRARLLIVMEMMEGGELFHRISQHRHFTEK----QASQVTK-------QDAP------ 134
Cdd:cd13983    59 HPNIIKFYDSW--------ESKSKKEVIFITELMTSGTLKQYLKRFKRLKLKviksWCRQILEglnylhtRDPPiihrdl 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 135 -------------VKLCDFGFAKIDQGD-----LMTPQFTpyyvAPQVLEAQrrhqkeksgiiptsptpytYNKSCDLWS 196
Cdd:cd13983   131 kcdnifingntgeVKIGDLGLATLLRQSfaksvIGTPEFM----APEMYEEH-------------------YDEKVDIYA 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 197 LGVIIYVMLCG-YPpfYSKHhsrTIPKDMRRKIMTGsfeFPEEEWSQI-SEMAKDVVRKLLKvKPEERLTIEGVLDHPWL 274
Cdd:cd13983   188 FGMCLLEMATGeYP--YSEC---TNAAQIYKKVTSG---IKPESLSKVkDPELKDFIEKCLK-PPDERPSARELLEHPFF 258
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
117-221 2.45e-03

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


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 39.56  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 117 HRHFTEKQAsqVTKQDAPVKLCDFGFAK-IDQGDLMTPQFTPYYVAPQVLEAqrrhqkeksgiIPTSPTpytynksCDLW 195
Cdd:cd14060   110 HRDLKSRNV--VIAADGVLKICDFGASRfHSHTTHMSLVGTFPWMAPEVIQS-----------LPVSET-------CDTY 169
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1704602876 196 SLGVIIYVMLCGYPPF------------YSKHHSRTIP 221
Cdd:cd14060   170 SYGVVLWEMLTREVPFkgleglqvawlvVEKNERPTIP 207
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
67-270 4.19e-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: 38.97  E-value: 4.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876  67 MMCATHPNIVQIIEVfansvqfpheSSPRARLLIVMEMMEGGELFHRISQHRHFTEKQ-----ASQVTK----------- 130
Cdd:cd05059    53 MMKLSHPKLVQLYGV----------CTKQRPIFIVTEYMANGCLLNYLRERRGKFQTEqllemCKDVCEameylesngfi 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 131 ------------QDAPVKLCDFGFAKIDQGDLMT----PQFTPYYVAPQVLEAQRrhqkeksgiiptsptpytYNKSCDL 194
Cdd:cd05059   123 hrdlaarnclvgEQNVVKVSDFGLARYVLDDEYTssvgTKFPVKWSPPEVFMYSK------------------FSSKSDV 184
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1704602876 195 WSLGVIIY-VMLCGYPPFYSKHHSRTIpkdmrRKIMTGsfeFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLD 270
Cdd:cd05059   185 WSFGVLMWeVFSEGKMPYERFSNSEVV-----EHISQG---YRLYRPHLAPTEVYTIMYSCWHEKPEERPTFKILLS 253
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
135-271 4.53e-03

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


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 38.88  E-value: 4.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1704602876 135 VKLCDFGFAKIdqgdlMTPQF----TPYYVAPQVLEAQRRHQkeksgiiptsptpytYNKSCDLWSLGVIIYVMLCGYPP 210
Cdd:cd06635   164 VKLADFGSASI-----ASPANsfvgTPYWMAPEVILAMDEGQ---------------YDGKVDVWSLGITCIELAERKPP 223
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1704602876 211 FYSKHHsrtipkdMRRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDH 271
Cdd:cd06635   224 LFNMNA-------MSALYHIAQNESPTLQSNEWSDYFRNFVDSCLQKIPQDRPTSEELLKH 277
 
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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