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Conserved domains on  [gi|110622073|emb|CAJ37351|]
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O-sialoglycoprotein endopeptidase, C-terminal fragment [Methanocella arvoryzae MRE50]

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List of domain hits

Name Accession Description Interval E-value
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
1-196 1.37e-89

serine/threonine protein kinase; Provisional


:

Pssm-ID: 237847  Cd Length: 211  Bit Score: 264.46  E-value: 1.37e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073   1 MAVIRRqGAEAVVELL----PDRVIKTRVPKSYRIRELDERLRRERTRAEAKIISEARRLGIPTPVVY--DVGQFSLEME 74
Cdd:PRK14879   1 MKLIKR-GAEAEIYLGdflgIKAVIKWRIPKRYRHPELDERIRRERTRREARIMSRARKAGVNVPAVYfvDPENFIIVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073  75 LIQGRPLKDVLSP------ELSRKAGVLVGKLHQGGLIHGDLTTSNMIVTDSTIYVIDFGLSYWDGTLEARGVDVHVYYQ 148
Cdd:PRK14879  80 YIEGEPLKDLINSngmeelELSREIGRLVGKLHSAGIIHGDLTTSNMILSGGKIYLIDFGLAEFSKDLEDRAVDLHVLLR 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 110622073 149 TLVSSHENH-EELMEAFAEGYRSSFPG-ANEVLRRVREIEYRGRYKTETP 196
Cdd:PRK14879 160 SLESTHPDWaEELFEAFLEGYREVMGEkAEEVLERVKEIRLRGRYVEERR 209
 
Name Accession Description Interval E-value
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
1-196 1.37e-89

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 264.46  E-value: 1.37e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073   1 MAVIRRqGAEAVVELL----PDRVIKTRVPKSYRIRELDERLRRERTRAEAKIISEARRLGIPTPVVY--DVGQFSLEME 74
Cdd:PRK14879   1 MKLIKR-GAEAEIYLGdflgIKAVIKWRIPKRYRHPELDERIRRERTRREARIMSRARKAGVNVPAVYfvDPENFIIVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073  75 LIQGRPLKDVLSP------ELSRKAGVLVGKLHQGGLIHGDLTTSNMIVTDSTIYVIDFGLSYWDGTLEARGVDVHVYYQ 148
Cdd:PRK14879  80 YIEGEPLKDLINSngmeelELSREIGRLVGKLHSAGIIHGDLTTSNMILSGGKIYLIDFGLAEFSKDLEDRAVDLHVLLR 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 110622073 149 TLVSSHENH-EELMEAFAEGYRSSFPG-ANEVLRRVREIEYRGRYKTETP 196
Cdd:PRK14879 160 SLESTHPDWaEELFEAFLEGYREVMGEkAEEVLERVKEIRLRGRYVEERR 209
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
4-192 1.78e-80

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


Pssm-ID: 274749  Cd Length: 199  Bit Score: 240.57  E-value: 1.78e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073    4 IRRQGAEAVVELL----PDRVIKTRVPKSYRIRELDERLRRERTRAEAKIISEARRLGIPTPVVYDVG--QFSLEMELIQ 77
Cdd:TIGR03724   1 LIAKGAEAIIYLGdflgRKAVIKERVPKSYRHPELDERLRKERTRREARLLSRARKAGVNTPVIYDVDpdNKTIVMEYIE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073   78 GRPLKDVLSP---ELSRKAGVLVGKLHQGGLIHGDLTTSNMIVTDSTIYVIDFGLSYWDGTLEARGVDVHVYYQTLVSSH 154
Cdd:TIGR03724  81 GKPLKDVIEEngdELAREIGRLVGKLHKAGIVHGDLTTSNIIVRDDKVYLIDFGLGKYSDEIEDKAVDLHVLKRSLESTH 160
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 110622073  155 EN-HEELMEAFAEGYRSSFPGANEVLRRVREIEYRGRYK 192
Cdd:TIGR03724 161 PDkAEELFEAFLEGYREVFGEAKDVLERVKEIELRGRYV 199
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
1-194 3.38e-78

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 226168  Cd Length: 204  Bit Score: 234.87  E-value: 3.38e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073   1 MAVIRrQGAEAVVELLP----DRVIKTRVPKSYRIRELDERLRRERTRAEAKIISEARRLGIPTPVVYDVGQFS--LEME 74
Cdd:COG3642    1 MDLIK-QGAEAIIYLTDflglPAVVKERIPKRYRHPELDEKLRRERTRREARILAKAREAGVPVPIVYDVDPDNglIVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073  75 LIQGRPLKDVL---SPELSRKAGVLVGKLHQGGLIHGDLTTSNMIVTDSTIYVIDFGLSYWDGTLEARGVDVHVYYQTLV 151
Cdd:COG3642   80 YIEGELLKDALeeaRPDLLREVGRLVGKLHKAGIVHGDLTTSNIILSGGRIYFIDFGLGEFSDEVEDKAVDLHVLERALE 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 110622073 152 SSHENHEELMEAFAEGYRSSFPGANEVLRRVREIEYRGRYKTE 194
Cdd:COG3642  160 STHEKAEELFAAFLEGYREEFGEAKEVLERLEEIRLRGRYVER 202
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
40-134 3.87e-11

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: 58.75  E-value: 3.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073  40 RERTRAEAKIiseARRL---GIPTpvVYDVGQFS----LEMELIQGRPLKDVLS--PELSRKAGVLVGK--------LHQ 102
Cdd:cd14014   44 RERFLREARA---LARLshpNIVR--VYDVGEDDgrpyIVMEYVEGGSLADLLRerGPLPPREALRILAqiadalaaAHR 118
                         90       100       110
                 ....*....|....*....|....*....|...
gi 110622073 103 GGLIHGDLTTSNMIVT-DSTIYVIDFGLSYWDG 134
Cdd:cd14014  119 AGIVHRDIKPANILLTeDGRVKLTDFGIARALG 151
RIO1 pfam01163
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ...
27-162 1.00e-07

RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria and eukaryotes. Activity of Rio1 is vital in Saccharomyces cerevisiae for the processing of ribosomal RNA, as well as for proper cell cycle progression and chromosome maintenance. The structure of RIO1 has been determined.


Pssm-ID: 279503  Cd Length: 186  Bit Score: 48.39  E-value: 1.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073   27 KSYRIRELDERLR--------RERTRAEAKIISEARRLGIPTPVVYDVGQFSLEMELI--QGRP---LKDVLSPELSRKA 93
Cdd:pfam01163  29 KRYRSGDFRFRDRktswrylvRLWAEKEFRNLKRLYEAGVPVPKPIDLNRHVLVMEFIgkDGVPaprLKDVELPEEAREI 108
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110622073   94 -----GVLVGKLHQGGLIHGDLTTSNMIVTDSTIYVIDFGlsywdgtleargvdvhvyyQTLVSSHENHEELME 162
Cdd:pfam01163 109 ydeiiREMRRLYQEAGLVHGDLSEYNILVHDDKPVIIDVP-------------------QAVETDHPNALEFLE 163
RIO smart00090
RIO-like kinase;
43-130 1.07e-06

RIO-like kinase;


Pssm-ID: 214511  Cd Length: 237  Bit Score: 46.14  E-value: 1.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073    43 TRAEAKIISEARRLGIPTPVVYDVGQFSLEMELIQGRP-----LKDVlSPELSRKAGVL------VGKL-HQGGLIHGDL 110
Cdd:smart00090  97 AEKEFRNLQRLYEAGVPVPKPIAWRRNVLVMEFIGGDGlpaprLKDV-EPEEEEEFELYddileeMRKLyKEGELVHGDL 175
                           90       100
                   ....*....|....*....|
gi 110622073   111 TTSNMIVTDSTIYVIDFGLS 130
Cdd:smart00090 176 SEYNILVHDGKVVIIDVSQS 195
PRK09605 PRK09605
bifunctional UGMP family protein/serine/threonine protein kinase; Validated
4-191 4.14e-84

bifunctional UGMP family protein/serine/threonine protein kinase; Validated


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 260.59  E-value: 4.14e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073   4 IRRQGAEAVVELLP----DRVIKTRVPKSYRIRELDERLRRERTRAEAKIISEARRLGIPTPVVYDV--GQFSLEMELIQ 77
Cdd:PRK09605 340 LIGKGAEADIKKGEylgrDAVIKERVPKGYRHPELDERLRTERTRAEARLLSEARRAGVPTPVIYDVdpEEKTIVMEYIG 419
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073  78 GRPLKDVL--SPELSRKAGVLVGKLHQGGLIHGDLTTSNMIVTDSTIYVIDFGLSYWDGTLEARGVDVHVYYQTLVSSHE 155
Cdd:PRK09605 420 GKDLKDVLegNPELVRKVGEIVAKLHKAGIVHGDLTTSNFIVRDDRLYLIDFGLGKYSDLIEDKAVDLHVLKQSLESTHY 499
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 110622073 156 NHEELMEAFAEGYRSSfPGANEVLRRVREIEYRGRY 191
Cdd:PRK09605 500 DFEELWEAFLEGYRET-EGAEDVLERLKEIEKRGRY 534
RIO2 COG0478
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
38-194 1.51e-06

RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction mechanisms];


Pssm-ID: 223554 [Multi-domain]  Cd Length: 304  Bit Score: 46.16  E-value: 1.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073  38 LRRERTRAEAKIISEARRLGIPTPVVYDVGQFSLEMELIQGRPLKDV-LSPELSRKA--GVL--VGKLHQGGLIHGDLTT 112
Cdd:COG0478  151 VSRLAAEREFEALQRLYPEGVKVPKPIAWNRHAVVMEYIEGVELYRLrLDVENPDEIldKILeeVRKAYRRGIVHGDLSE 230
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073 113 SNMIVT-DSTIYVIDFGlsywdgtleargvdvhvyyQTLVSSHENHEELME--------AFAEGYRSSFPGaNEVLRRVR 183
Cdd:COG0478  231 FNILVTeDGDIVVIDWP-------------------QAVPISHPDAEELLErdveniikYFRRKYGYKVEK-EEELDRVR 290
                        170
                 ....*....|.
gi 110622073 184 EIEYRGRYKTE 194
Cdd:COG0478  291 EASEFGKKEVE 301
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
30-155 1.82e-04

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 39.82  E-value: 1.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073    30 RIRELDERLRRERTRAEAKIISEARRLGIPTpvVYDV----GQFSLEMELIQGRPLKDVL------SPELSRK--AGVLV 97
Cdd:smart00220  31 VIKKKKIKKDRERILREIKILKKLKHPNIVR--LYDVfedeDKLYLVMEYCEGGDLFDLLkkrgrlSEDEARFylRQILS 108
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110622073    98 G--KLHQGGLIHGDLTTSN-MIVTDSTIYVIDFGLsywdgtleARGVDVHVYYQTLVSSHE 155
Cdd:smart00220 109 AleYLHSKGIVHRDLKPENiLLDEDGHVKLADFGL--------ARQLDPGEKLTTFVGTPE 161
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
19-129 2.56e-04

2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the first hydroxylation step in the ubiquinone biosynthetic pathway in bacteria. It is believed that the reaction is 2-polyprenylphenol -> 6-hydroxy-2-polyprenylphenol. This model finds hits primarily in the proteobacteria. The gene is also known as AarF in certain species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273909 [Multi-domain]  Cd Length: 437  Bit Score: 39.59  E-value: 2.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073   19 RVIKTRVPKSYRIR------ELDERLRRERT-RAEAKIISEARR-----LGIPTPVVY--DVGQFSLEMELIQGRPLKDV 84
Cdd:TIGR01982 169 RIVERLSPDSRRLRptevvkEFEKTLRRELDlRREAANASELGEnfkndPGVYVPEVYwdRTSERVLTMEWIDGIPLSDI 248
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 110622073   85 L---SPELSRK------AGVLVGKLHQGGLIHGDLTTSNMIVT-DSTIYVIDFGL 129
Cdd:TIGR01982 249 AaldEAGLDRKalaenlARSFLNQVLRDGFFHADLHPGNIFVLkDGKIIALDFGI 303
Pkinase pfam00069
Protein kinase domain;
20-130 1.18e-03

Protein kinase domain;


Pssm-ID: 278497 [Multi-domain]  Cd Length: 254  Bit Score: 37.19  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073   20 VIKTrVPKSYRIRELDERLRRERtraeaKIIseaRRLGIPTPV-VYDV----GQFSLEMELIQGRPLKDVL------SPE 88
Cdd:pfam00069  28 AVKK-IKKEKIKKKKDKNVLREI-----KIL---KKLNHPNIVrLYDVfedkDHLYLVLEYVEGGSLFDLLsekgafSER 98
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 110622073   89 LSRK--AGVLVG--KLHQGGLIHGDLTTSN-MIVTDSTIYVIDFGLS 130
Cdd:pfam00069  99 EAKFimKQILEGleYLHSNGIVHRDLKPENiLIDEDGNLKITDFGLA 145
 
Name Accession Description Interval E-value
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
1-196 1.37e-89

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 264.46  E-value: 1.37e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073   1 MAVIRRqGAEAVVELL----PDRVIKTRVPKSYRIRELDERLRRERTRAEAKIISEARRLGIPTPVVY--DVGQFSLEME 74
Cdd:PRK14879   1 MKLIKR-GAEAEIYLGdflgIKAVIKWRIPKRYRHPELDERIRRERTRREARIMSRARKAGVNVPAVYfvDPENFIIVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073  75 LIQGRPLKDVLSP------ELSRKAGVLVGKLHQGGLIHGDLTTSNMIVTDSTIYVIDFGLSYWDGTLEARGVDVHVYYQ 148
Cdd:PRK14879  80 YIEGEPLKDLINSngmeelELSREIGRLVGKLHSAGIIHGDLTTSNMILSGGKIYLIDFGLAEFSKDLEDRAVDLHVLLR 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 110622073 149 TLVSSHENH-EELMEAFAEGYRSSFPG-ANEVLRRVREIEYRGRYKTETP 196
Cdd:PRK14879 160 SLESTHPDWaEELFEAFLEGYREVMGEkAEEVLERVKEIRLRGRYVEERR 209
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
4-192 1.78e-80

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


Pssm-ID: 274749  Cd Length: 199  Bit Score: 240.57  E-value: 1.78e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073    4 IRRQGAEAVVELL----PDRVIKTRVPKSYRIRELDERLRRERTRAEAKIISEARRLGIPTPVVYDVG--QFSLEMELIQ 77
Cdd:TIGR03724   1 LIAKGAEAIIYLGdflgRKAVIKERVPKSYRHPELDERLRKERTRREARLLSRARKAGVNTPVIYDVDpdNKTIVMEYIE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073   78 GRPLKDVLSP---ELSRKAGVLVGKLHQGGLIHGDLTTSNMIVTDSTIYVIDFGLSYWDGTLEARGVDVHVYYQTLVSSH 154
Cdd:TIGR03724  81 GKPLKDVIEEngdELAREIGRLVGKLHKAGIVHGDLTTSNIIVRDDKVYLIDFGLGKYSDEIEDKAVDLHVLKRSLESTH 160
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 110622073  155 EN-HEELMEAFAEGYRSSFPGANEVLRRVREIEYRGRYK 192
Cdd:TIGR03724 161 PDkAEELFEAFLEGYREVFGEAKDVLERVKEIELRGRYV 199
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
1-194 3.38e-78

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 226168  Cd Length: 204  Bit Score: 234.87  E-value: 3.38e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073   1 MAVIRrQGAEAVVELLP----DRVIKTRVPKSYRIRELDERLRRERTRAEAKIISEARRLGIPTPVVYDVGQFS--LEME 74
Cdd:COG3642    1 MDLIK-QGAEAIIYLTDflglPAVVKERIPKRYRHPELDEKLRRERTRREARILAKAREAGVPVPIVYDVDPDNglIVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073  75 LIQGRPLKDVL---SPELSRKAGVLVGKLHQGGLIHGDLTTSNMIVTDSTIYVIDFGLSYWDGTLEARGVDVHVYYQTLV 151
Cdd:COG3642   80 YIEGELLKDALeeaRPDLLREVGRLVGKLHKAGIVHGDLTTSNIILSGGRIYFIDFGLGEFSDEVEDKAVDLHVLERALE 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 110622073 152 SSHENHEELMEAFAEGYRSSFPGANEVLRRVREIEYRGRYKTE 194
Cdd:COG3642  160 STHEKAEELFAAFLEGYREEFGEAKEVLERLEEIRLRGRYVER 202
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
40-134 3.87e-11

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: 58.75  E-value: 3.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073  40 RERTRAEAKIiseARRL---GIPTpvVYDVGQFS----LEMELIQGRPLKDVLS--PELSRKAGVLVGK--------LHQ 102
Cdd:cd14014   44 RERFLREARA---LARLshpNIVR--VYDVGEDDgrpyIVMEYVEGGSLADLLRerGPLPPREALRILAqiadalaaAHR 118
                         90       100       110
                 ....*....|....*....|....*....|...
gi 110622073 103 GGLIHGDLTTSNMIVT-DSTIYVIDFGLSYWDG 134
Cdd:cd14014  119 AGIVHRDIKPANILLTeDGRVKLTDFGIARALG 151
RIO2_C cd05144
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ...
57-127 9.94e-09

C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is present in archaea and eukaryotes. It contains an N-terminal winged helix (wHTH) domain and a C-terminal RIO kinase catalytic domain. The wHTH domain is primarily seen in DNA-binding proteins, although some wHTH domains may be involved in RNA recognition. RIO2 is essential for survival and is necessary for rRNA cleavage during 40S ribosomal subunit maturation. RIO kinases are atypical protein serine kinases containing a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. The RIO2 kinase catalytic domain family is part of a larger superfamily, that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270695  Cd Length: 183  Bit Score: 50.97  E-value: 9.94e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110622073  57 GIPTPVVYDVGQFSLEMELIQGRPLKDVlsPELSRKAGVL------VGKLHQGGLIHGDLTTSNMIVTDS-TIYVIDF 127
Cdd:cd05144   79 GFPVPKPIDWNRHAVVMELIDGYPLYQV--RLLEDPEEVLdeilelIVKLAKHGLIHGDFSEFNILVDEDeKITVIDF 154
RIO1 pfam01163
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ...
27-162 1.00e-07

RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria and eukaryotes. Activity of Rio1 is vital in Saccharomyces cerevisiae for the processing of ribosomal RNA, as well as for proper cell cycle progression and chromosome maintenance. The structure of RIO1 has been determined.


Pssm-ID: 279503  Cd Length: 186  Bit Score: 48.39  E-value: 1.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073   27 KSYRIRELDERLR--------RERTRAEAKIISEARRLGIPTPVVYDVGQFSLEMELI--QGRP---LKDVLSPELSRKA 93
Cdd:pfam01163  29 KRYRSGDFRFRDRktswrylvRLWAEKEFRNLKRLYEAGVPVPKPIDLNRHVLVMEFIgkDGVPaprLKDVELPEEAREI 108
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110622073   94 -----GVLVGKLHQGGLIHGDLTTSNMIVTDSTIYVIDFGlsywdgtleargvdvhvyyQTLVSSHENHEELME 162
Cdd:pfam01163 109 ydeiiREMRRLYQEAGLVHGDLSEYNILVHDDKPVIIDVP-------------------QAVETDHPNALEFLE 163
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
27-133 1.04e-07

Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270690  Cd Length: 158  Bit Score: 48.07  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073  27 KSYRIRELDER-LRRERTRAEAKIISEAR-------RLGIPTPVVYDV----GQFSLEMELIQGRPLKDV---LSPE--- 88
Cdd:cd05120   13 KVYLLGDPREYvLKIGPPRLKKDLEKEAAmlqllagKLSLPVPKVYGFgesdGWEYLLMERIEGETLSEVwprLSEEeke 92
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 110622073  89 -LSRKAGVLVGKLHQ---GGLIHGDLTTSNMIV--TDSTIYVIDFGLS-----YWD 133
Cdd:cd05120   93 kIADQLAEILAALHRidsSVLTHGDLHPGNILVkpDGKLSGIIDWEFAgygppAFD 148
RIO1_like cd05145
Catalytic domain of the atypical protein serine kinases, RIO1 and RIO3 kinases and similar ...
43-128 2.00e-07

Catalytic domain of the atypical protein serine kinases, RIO1 and RIO3 kinases and similar proteins; RIO1 is present in archaea, bacteria and eukaryotes. In addition, RIO3 is present in multicellular eukaryotes. Both RIO1 and RIO3 are associated with precursors of 40S ribosomal subunits, just like RIO2. RIO1 is essential for survival and is required for 18S rRNA processing, proper cell cycle progression and chromosome maintenance. Although depletion of either RIO1 and RIO2 results in similar effects, the two kinases are not fully interchangeable. The specific function of RIO3 is unknown. RIO kinases are atypical protein serine kinases containing a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. The RIO kinase catalytic domain family is part of a larger superfamily, that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270696  Cd Length: 189  Bit Score: 47.55  E-value: 2.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073  43 TRAEAKIISEARRLGIPTPVVYDVGQFSLEMELI--QGRP---LKDV-LSPELSRKA-----GVLVGKLHQGGLIHGDLT 111
Cdd:cd05145   65 ARKEFRNLKRLYEAGVRVPEPIAVYRNVLVMEFIgdDGSPaprLKDVeLEEEDAEELyeqvvEQMRRMYCKAGLVHGDLS 144
                         90
                 ....*....|....*..
gi 110622073 112 TSNMIVTDSTIYVIDFG 128
Cdd:cd05145  145 EYNILYYDGKPVIIDVS 161
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
20-130 4.54e-07

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: 47.27  E-value: 4.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073  20 VIKtRVPKSYRIRELDERLRrertraEAKIISEARRLGIPTpvVYDVGQFSLE----MELIQGRPLKDVL-------SPE 88
Cdd:cd00180   22 AVK-VIPKEKLKKLLEELLR------EIEILKKLNHPNIVK--LYDVFETENFlylvMEYCEGGSLKDLLkenkgplSEE 92
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 110622073  89 LSRK--AGVLVG--KLHQGGLIHGDLTTSNMIVTDS-TIYVIDFGLS 130
Cdd:cd00180   93 EALSilRQLLSAleYLHSNGIIHRDLKPENILLDSDgTVKLADFGLA 139
RIO smart00090
RIO-like kinase;
43-130 1.07e-06

RIO-like kinase;


Pssm-ID: 214511  Cd Length: 237  Bit Score: 46.14  E-value: 1.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073    43 TRAEAKIISEARRLGIPTPVVYDVGQFSLEMELIQGRP-----LKDVlSPELSRKAGVL------VGKL-HQGGLIHGDL 110
Cdd:smart00090  97 AEKEFRNLQRLYEAGVPVPKPIAWRRNVLVMEFIGGDGlpaprLKDV-EPEEEEEFELYddileeMRKLyKEGELVHGDL 175
                           90       100
                   ....*....|....*....|
gi 110622073   111 TTSNMIVTDSTIYVIDFGLS 130
Cdd:smart00090 176 SEYNILVHDGKVVIIDVSQS 195
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
44-127 1.26e-06

Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic choline kinases, as well as eukaryotic ethanolamine kinase. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. Bacterial ChoK is also referred to as licA protein. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270700  Cd Length: 152  Bit Score: 44.85  E-value: 1.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073  44 RAEAKIISEARRLGI-PTPVVYDVGQFSLEMELIQGRPL--KDVLSPELSRKAGVLVGKLHQGGLI-----HGDLTTSNM 115
Cdd:cd05151   40 ENEKANSKAAAELGIaPEVIYFDPETGVKITEFIEGATLltNDFSDPENLERIAALLRKLHSSPLEdlvlcHNDLVPGNF 119
                         90
                 ....*....|..
gi 110622073 116 IVTDSTIYVIDF 127
Cdd:cd05151  120 LLDDDRLYLIDW 131
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
7-128 2.41e-06

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870  Cd Length: 136  Bit Score: 43.97  E-value: 2.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073   7 QGAEAVVELLPDrviKTRVPKSY-RIRELDERLRRERTRAEAKIISEARRLGIPTP---VVYDVGQFS-LEMELIQGRPL 81
Cdd:cd13968    3 EGASAKVFWAEG---ECTTIGVAvKIGDDVNNEEGEDLESEMDILRRLKGLELNIPkvlVTEDVDGPNiLLMELVKGGTL 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 110622073  82 KDVLSPELSRKAGV---------LVGKLHQGGLIHGDLTTSNMIVTDS-TIYVIDFG 128
Cdd:cd13968   80 IAYTQEEELDEKDVesimyqlaeCMRLLHSFHLIHRDLNNDNILLSEDgNVKLIDFG 136
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
27-130 3.32e-06

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: 44.84  E-value: 3.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073  27 KSYRIRELDERLRRERTRaEAKIISEARR------LGiptpVVYDVGQFSLEMELIQGRPLKDVL-------SPELSRKA 93
Cdd:cd13999   22 KKLKVEDDNDELLKEFRR-EVSILSKLRHpnivqfIG----ACLSPPPLCIVTEYMPGGSLYDLLhkkkiplSWSLRLKI 96
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 110622073  94 GVLVGK----LHQGGLIHGDLTTSNMIVTDS-TIYVIDFGLS 130
Cdd:cd13999   97 ALDIARgmnyLHSPPIIHRDLKSLNILLDENfTVKIADFGLS 138
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
32-129 9.87e-05

Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and similar proteins; This family is composed of the atypical yeast protein kinase Abc1p, its human homolog ADCK3 (also called CABC1), and similar proteins. Abc1p (also called Coq8p) is required for the biosynthesis of Coenzyme Q (ubiquinone or Q), which is an essential lipid component in respiratory electron and proton transport. It is necessary for the formation of a multi-subunit Q-biosynthetic complex and may also function in the regulation of Q synthesis. Human ADCK3 is able to rescue defects in Q synthesis and the phosphorylation state of Coq proteins in yeast Abc1 (or Coq8) mutants. Mutations in ADCK3 cause progressive cerebellar ataxia and atrophy due to Q10 deficiency. Eukaryotes contain at least two more ABC1/ADCK3-like proteins: in humans, these are the putative atypical protein kinases named ADCK1 and ADCK2. In algae and higher plants, ABC1 kinases have proliferated to more than 15 subfamilies, most of which are located in plastids or mitochondria. Eight of these plant ABC1 kinase subfamilies (ABC1K1-8) are specific for photosynthetic organisms. ABC1 kinases are not related to the ATP-binding cassette (ABC) membrane transporter family.


Pssm-ID: 270691 [Multi-domain]  Cd Length: 247  Bit Score: 40.56  E-value: 9.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073  32 RELDerLRRERTRAE--AKIISEARRLGIPTPVvydvGQFS----LEMELIQGRPLKDVLS--------PELSRKAGVLV 97
Cdd:cd05121  109 EELD--FRREARNAErfRKNLKDSPDVYVPKVY----PELStrrvLVMEYIDGVKLTDLEAlraagidrKELARRLVDAY 182
                         90       100       110
                 ....*....|....*....|....*....|....
gi 110622073  98 GK-LHQGGLIHGDLTTSNMIVT-DSTIYVIDFGL 129
Cdd:cd05121  183 LKqIFEDGFFHADPHPGNILVLpDGRIALLDFGM 216
PRK01723 PRK01723
3-deoxy-D-manno-octulosonic-acid kinase; Reviewed
41-127 1.02e-04

3-deoxy-D-manno-octulosonic-acid kinase; Reviewed


Pssm-ID: 234975  Cd Length: 239  Bit Score: 40.64  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073  41 ERTRA--EAKIISEARRLG--IPTPVVYDVGQFSLE------MELIQG-RPLKDVL-----SPELSRKAGVLVGKLHQGG 104
Cdd:PRK01723  83 ERTRAfaEFRLLAQLYEAGlpVPRPIAARVVRHGLFyradilIERIEGaRDLVALLqeaplSEEQWQAIGQLIARFHDAG 162
                         90       100
                 ....*....|....*....|....
gi 110622073 105 LIHGDLTTSN-MIVTDSTIYVIDF 127
Cdd:PRK01723 163 VYHADLNAHNiLLDPDGKFWLIDF 186
Kdo pfam06293
Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to ...
37-127 1.14e-04

Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to protein kinases pfam00069. This family includes waaP (rfaP) gene product is required for the addition of phosphate to O-4 of the first heptose residue of the lipopolysaccharide (LPS) inner core region. It has previously been shown that WaaP is necessary for resistance to hydrophobic and polycationic antimicrobials in E. coli and that it is required for virulence in invasive strains of S. enterica.


Pssm-ID: 283861  Cd Length: 207  Bit Score: 40.05  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073   37 RLRRERTRAEAKIISEARRLGIPTP-------VVYDVGQ------------FSLEMELIQGRPLKDVLSPELSRKAGVLV 97
Cdd:pfam06293  52 PLGRTRAFREFRLIRRLREAGVPVPkpvaageVKVGGEYradllterlegaQDLADWLADWAVPSGELRRALWEAVGRLI 131
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 110622073   98 GKLHQGGLIHGDLTTSNMIV-----TDSTIYVIDF 127
Cdd:pfam06293 132 AQMHRAGVNHGDLYAHHILLqqegdEGFEAWLIDL 166
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
81-173 1.94e-04

Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a subset of bacteria, which have a Protein Kinase fold. These proteins do not bear any similarity to the GHMP family homoserine kinases present in most bacteria and eukaryotes. Homoserine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to L-homoserine producing L-homoserine phosphate, an intermediate in the production of the amino acids threonine, methionine, and isoleucine. The Type II homoserine kinase subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270702 [Multi-domain]  Cd Length: 300  Bit Score: 39.93  E-value: 1.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073  81 LKDVLSPELSRKAGVLVGKLHQ----------GGLIHGDLTTSNMIVTDSTIY-VIDFGLSYWDgtleARGVDVHVY--Y 147
Cdd:cd05153  147 LKARLDLLAADDRALLEDELARlqalapsdlpRGVIHADLFRDNVLFDGDRLSgIIDFYDACYD----PLLYDLAIAlnD 222
                         90       100
                 ....*....|....*....|....*.
gi 110622073 148 QTLVSSHENHEELMEAFAEGYRSSFP 173
Cdd:cd05153  223 WCFDDDGKLDPERAKALLAGYQSVRP 248
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
100-135 1.98e-04

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


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 39.70  E-value: 1.98e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 110622073 100 LHQGGLIHGDLTTSNMIV-TDSTIYVIDFGLSYWDGT 135
Cdd:cd07850  118 LHSAGIIHRDLKPSNIVVkSDCTLKILDFGLARTAGT 154
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
100-135 2.22e-04

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: 39.53  E-value: 2.22e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 110622073 100 LHQGGLIHGDLTTSNMIVT--DSTIYVIDFGLSYWDGT 135
Cdd:cd05118  117 LHSNGIIHRDLKPENILINleLGQLKLADFGLARSFTS 154
COG2112 COG2112
Predicted Ser/Thr protein kinase [Signal transduction mechanisms];
39-127 3.26e-04

Predicted Ser/Thr protein kinase [Signal transduction mechanisms];


Pssm-ID: 225023  Cd Length: 201  Bit Score: 38.93  E-value: 3.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073  39 RRERTRAEAKIISEARRLGIpTPVVYDVGQFSLEMELIQGRPLKDV---LSPELSRKAGVLVGKLHQGGLIHGDLTT--S 113
Cdd:COG2112   58 PRRNLEKEAKILEILAGEGV-TPEVYFYGEDFIRMEYIDGRPLGKLeigGDRKHLLRVLEKAYKLDRLGIEHGELSRpwK 136
                         90
                 ....*....|....
gi 110622073 114 NMIVTDSTIYVIDF 127
Cdd:COG2112  137 NVLVNDRDVYIIDF 150
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
1-130 3.89e-04

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


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 38.97  E-value: 3.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073   1 MAVIRRQGAEAVVELLPdRVIKTRVPKSYRIRELDERLRRERTRAEAKI--------ISEARRLgIPTPVVY-------D 65
Cdd:cd14077   19 LAKHIRTGEKCAIKIIP-RASNAGLKKEREKRLEKEISRDIRTIREAALssllnhphICRLRDF-LRTPNHYymlfeyvD 96
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110622073  66 VGQFsLEMeLIQGRPLKDVLSPELSRKAGVLVGKLHQGGLIHGDLTTSNMIVTDS-TIYVIDFGLS 130
Cdd:cd14077   97 GGQL-LDY-IISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSgNIKIIDFGLS 160
RIO1_euk cd05147
Catalytic domain of the atypical protein serine kinase, Eukaryotic RIO1 kinase; RIO1 is ...
54-126 4.27e-04

Catalytic domain of the atypical protein serine kinase, Eukaryotic RIO1 kinase; RIO1 is present in archaea, bacteria and eukaryotes. This subfamily is composed of RIO1 proteins from eukaryotes. RIO1 is essential for survival and is required for 18S rRNA processing, proper cell cycle progression and chromosome maintenance. It is associated with precursors of 40S ribosomal subunits, just like RIO2. Although depletion of either RIO1 and RIO2 results in similar effects, the two kinases are not fully interchangeable. RIO kinases are atypical protein serine kinases containing a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. The RIO kinase catalytic domain family is part of a larger superfamily, that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270698  Cd Length: 190  Bit Score: 38.32  E-value: 4.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073  54 RRL---GIPTPVVYDVGQFSLEMELI--QGRP---LKDV-LSPELSRKAGVLVGKL-----HQGGLIHGDLTTSNMIVTD 119
Cdd:cd05147   74 KRLnqaGIPCPEPILLRSHVLVMEFIgkDGWPaprLKDAkLSESKWRELYLQVIKImrrmyQKCRLVHADLSEYNLLYHK 153

                 ....*..
gi 110622073 120 STIYVID 126
Cdd:cd05147  154 GKVYIID 160
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
100-133 4.50e-04

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


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 38.59  E-value: 4.50e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 110622073 100 LHQGGLIHGDLTTSNMIV----TDSTIYVIDFGLS--YWD 133
Cdd:cd14016  112 LHSKGYIHRDIKPENFLMglgkNSNKVYLIDFGLAkkYRD 151
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
62-130 4.84e-04

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


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 38.39  E-value: 4.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073  62 VVYDVGQFSLEMELIQGRPLKDVL--------SPELSRKAGVLVGK--LHQGGLIHGDLTTSNMIVT-DSTIYVIDFGLS 130
Cdd:cd14222   58 VLYKDKRLNLLTEFIEGGTLKDFLraddpfpwQQKVSFAKGIASGMayLHSMSIIHRDLNSHNCLIKlDKTVVVADFGLS 137
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
97-135 4.98e-04

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


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 38.53  E-value: 4.98e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 110622073  97 VGKLHQGGLIHGDLTTSNMIV-TDSTIYVIDFGLSYWDGT 135
Cdd:cd07874  132 IKHLHSAGIIHRDLKPSNIVVkSDCTLKILDFGLARTAGT 171
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
73-131 5.13e-04

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: 38.30  E-value: 5.13e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110622073  73 MELIQGRPLKDV--------LSPELSRK--AGVLVG--KLHQGGLIHGDLTTSNMIVTDS-TIYVIDFGLSY 131
Cdd:cd14008   85 LEYCEGGPVMELdsgdrvppLPEETARKyfRDLVLGleYLHENGIVHRDIKPENLLLTADgTVKISDFGVSE 156
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
62-130 6.72e-04

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


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 38.26  E-value: 6.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073  62 VVYDVGQFSLEMELIQGRPLKDVL----SP-------ELSRKAGVLVGKLHQGGLIHGDLTTSNMIV-TDSTIYVIDFGL 129
Cdd:cd14154   58 VLYKDKKLNLITEYIPGGTLKDVLkdmaRPlpwaqrvRFAKDIASGMAYLHSMNIIHRDLNSHNCLVrEDKTVVVADFGL 137

                 .
gi 110622073 130 S 130
Cdd:cd14154  138 A 138
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
97-135 7.41e-04

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


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 38.10  E-value: 7.41e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 110622073  97 VGKLHQGGLIHGDLTTSNMIV-TDSTIYVIDFGLSYWDGT 135
Cdd:cd07875  139 IKHLHSAGIIHRDLKPSNIVVkSDCTLKILDFGLARTAGT 178
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
73-130 9.30e-04

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: 37.57  E-value: 9.30e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073  73 MELIQGRPLKDVLS------PELSRKA---GVLVG--KLHQGGLIHGDLTTSN-MIVTDSTIYVIDFGLS 130
Cdd:cd05122   76 MEFCSGGSLKDLLKntnktlTEQQIAYvckEVLKGleYLHSHGIIHRDIKAANiLLTSDGEVKLIDFGLS 145
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
63-128 1.21e-03

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: 37.23  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073  63 VYDVGQFS-LEMELIQGRPLKDVLspeLSRK-------AGVL------VGKLHQGGLIHGDLTTSNMIVTD-----STIY 123
Cdd:cd14091   62 VYDDGNSVyLVTELLRGGELLDRI---LRQKffsereaSAVMktltktVEYLHSQGVVHRDLKPSNILYADesgdpESLR 138

                 ....*
gi 110622073 124 VIDFG 128
Cdd:cd14091  139 ICDFG 143
ABC1_ADCK3 cd13970
Activator of bc1 complex (ABC1) kinases, also called aarF domain containing kinase 3; This ...
31-166 1.31e-03

Activator of bc1 complex (ABC1) kinases, also called aarF domain containing kinase 3; This subfamily is composed of the atypical yeast protein kinase Abc1p, its human homolog ADCK3 (also called CABC1), and similar proteins. Abc1p (also called Coq8p) is required for the biosynthesis of Coenzyme Q (ubiquinone or Q), which is an essential lipid component in respiratory electron and proton transport. It is necessary for the formation of a multi-subunit Q-biosynthetic complex and may also function in the regulation of Q synthesis. Human ADCK3 is able to rescue defects in Q synthesis and the phosphorylation state of Coq proteins in yeast Abc1 (or Coq8) mutants. Mutations in ADCK3 cause progressive cerebellar ataxia and atrophy due to Q10 deficiency. In algae and higher plants, ABC1 kinases have proliferated to more than 15 subfamilies, most of which are located in plastids or mitochondria. Subfamily 13 (ABC1K13) of plant ABC1 kinases belongs in this subfamily with yeast Abc1p and human ADCK3. ABC1 kinases are not related to the ATP-binding cassette (ABC) membrane transporter family.


Pssm-ID: 270872  Cd Length: 251  Bit Score: 37.11  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073  31 IRELDERLRRE-RTRAEAKIISEARRL-----GIPTPVVYDvgQFS----LEMELIQGRPLKDV--LSPELSRKAG---- 94
Cdd:cd13970  101 IAELREELLEEcDYEREAANQRRFRELladdpRFVVPEVIP--ELStkrvLTTEFVDGVPLDEAadLSQEERNRIGelll 178
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110622073  95 -VLVGKLHQGGLIHGDLTTSNMIVTDST--IYVIDFGLSywdGTLEARGVDvhVYYQTLVSS-HENHEELMEAFAE 166
Cdd:cd13970  179 rLCLRELFEFGFMQTDPNPGNFLYDPEDgrLGLLDFGAV---REYPPEFVD--GYRRLVRAAlEGDREALLEASVE 249
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
73-130 1.47e-03

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


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 37.24  E-value: 1.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110622073  73 MELiQGRPLKDVL----SPELSRKAGVLVGK--------LHQGGLIHGDLTTSNM-----IVTDSTIYVIDFGLS 130
Cdd:cd14017   75 MTL-LGPNLAELRrsqpRGKFSVSTTLRLGIqilkaiedIHEVGFLHRDVKPSNFaigrgPSDERTVYILDFGLA 148
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
63-130 1.52e-03

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: 37.30  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073  63 VYDVGQFS-LEMELIQGRPLKD-VLSPEL--SRKAGVL-------VGKLHQGGLIHGDLTTSNMIVTDST-----IYVID 126
Cdd:cd14178   65 VYDDGKFVyLVMELMRGGELLDrILRQKCfsEREASAVlctitktVEYLHSQGVVHRDLKPSNILYMDESgnpesIRICD 144

                 ....
gi 110622073 127 FGLS 130
Cdd:cd14178  145 FGFA 148
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
7-132 1.56e-03

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: 36.90  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073   7 QGAEAVVELLPDRVIKTRV---PKSYRIRELDERLRRERTRAeakiISE---ARRLGIPTPV-VYDV-----GQFSLEME 74
Cdd:cd13994    3 KGATSVVRIVTKKNPRSGVlyaVKEYRRRDDESKRKDYVKRL----TSEyiiSSKLHHPNIVkVLDLcqdlhGKWCLVME 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110622073  75 LIQGrplKDVLSpeLSRKAGVL---------------VGKLHQGGLIHGDLTTSNMIVTDS-TIYVIDFGLSYW 132
Cdd:cd13994   79 YCPG---GDLFT--LIEKADSLsleekdcffkqilrgVAYLHSHGIAHRDLKPENILLDEDgVLKLTDFGTAEV 147
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
100-130 1.77e-03

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


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 36.93  E-value: 1.77e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 110622073 100 LHQGGLIHGDLTTSNMIV-TDSTIYVIDFGLS 130
Cdd:cd07876  139 LHSAGIIHRDLKPSNIVVkSDCTLKILDFGLA 170
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
100-131 2.02e-03

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: 36.81  E-value: 2.02e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 110622073 100 LHQGGLIHGDLTTSNMIVTDS-TIYVIDFGLSY 131
Cdd:cd05579  109 LHSHGIIHRDLKPDNILIDANgHLKLTDFGLSK 141
STKc_VRK cd14015
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs ...
100-144 2.16e-03

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


Pssm-ID: 270917 [Multi-domain]  Cd Length: 300  Bit Score: 36.49  E-value: 2.16e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110622073 100 LHQGGLIHGDLTTSNMIV----TDSTIYVIDFGLSY------------------WDGTLEARGVDVH 144
Cdd:cd14015  143 IHENGYVHADIKASNLLLgfgkNKDQVYLVDYGLASrycpngkhkeykedprkaHNGTIEFTSRDAH 209
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
71-130 2.47e-03

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


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 36.20  E-value: 2.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110622073  71 LEMELIQGRPLKDVLSPELS---RKAGVLVGK-------LHQGGLIHGDLTTSNMIV----TDSTIYVIDFGLS 130
Cdd:cd14083   78 LVMELVTGGELFDRIVEKGSyteKDASHLIRQvleavdyLHSLGIVHRDLKPENLLYyspdEDSKIMISDFGLS 151
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
100-130 3.05e-03

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: 36.38  E-value: 3.05e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 110622073 100 LHQGGLIHGDLTTSNMIV-TDSTIYVIDFGLS 130
Cdd:cd07852  123 LHSGGVIHRDLKPSNILLnSDCRVKLADFGLA 154
RIO cd05119
Catalytic domain of the atypical protein serine kinases, RIO kinases; RIO kinases are atypical ...
43-130 3.76e-03

Catalytic domain of the atypical protein serine kinases, RIO kinases; RIO kinases are atypical protein serine kinases present in archaea, bacteria and eukaryotes. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. RIO kinases contain a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. Most organisms contain at least two RIO kinases, RIO1 and RIO2. A third protein, RIO3, is present in multicellular eukaryotes. In yeast, RIO1 and RIO2 are essential for survival. They function as non-ribosomal factors necessary for late 18S rRNA processing. RIO1 is also required for proper cell cycle progression and chromosome maintenance. The biological substrates for RIO kinases are still unknown. The RIO kinase catalytic domain family is part of a larger superfamily, that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270689  Cd Length: 192  Bit Score: 35.77  E-value: 3.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073  43 TRAEAKIISEARRLGIPTPVVYDVGQFSLEMELIQGRPLKDVLSPELSRKAGVL------------VGKL-HQGGLIHGD 109
Cdd:cd05119   67 TEKEFRNLERAKEAGVSVPQPYTYEKNVLL*EFIGEDELPAPTLVELGRELKELdvegifndvvenVKRLyQEAELVHAD 146
                         90       100
                 ....*....|....*....|.
gi 110622073 110 LTTSNMIVTDStIYVIDFGLS 130
Cdd:cd05119  147 LSEYNILYIDK-VYFIDFGQA 166
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
71-130 4.40e-03

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: 35.63  E-value: 4.40e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110622073  71 LEMELIQGRPLKDVLS------PELSRK----AGVLVGKLHQGGLIHGDLTTSNMIVTDST-IYVIDFGLS 130
Cdd:cd05610   81 LVMEYLIGGDVKSLLHiygyfdEEMAVKyiseVALALDYLHRHGIIHRDLKPDNMLISNEGhIKLTDFGLS 151
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
100-144 5.65e-03

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: 35.58  E-value: 5.65e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 110622073 100 LHQGGLIHGDLTTSNMIV-TDSTIYVIDFGLsywdgtleARGVDVH 144
Cdd:cd07834  119 LHSAGVIHRDLKPSNILVnSNCDLKICDFGL--------ARGVDPD 156
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
97-138 6.81e-03

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases. The KSR2 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: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 34.98  E-value: 6.81e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 110622073  97 VGKLHQGGLIHGDLTTSNMIVTDSTIYVIDFGLSYWDGTLEA 138
Cdd:cd14153  110 MGYLHAKGILHKDLKSKNVFYDNGKVVITDFGLFTISGVLQA 151
PRK10359 PRK10359
lipopolysaccharide core biosynthesis protein; Provisional
74-126 7.95e-03

lipopolysaccharide core biosynthesis protein; Provisional


Pssm-ID: 182407  Cd Length: 232  Bit Score: 34.73  E-value: 7.95e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 110622073  74 ELIQGRPLKDVL--SPELSRKAGVLVGKLHQGGLIHGDLTTSNMIVTDSTIYVID 126
Cdd:PRK10359 123 EYIEGVELNDMPeiSEDVKAKIKASIESLHQHGMVSGDPHKGNFIVSKNGLRIID 177
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
97-130 8.28e-03

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: 35.01  E-value: 8.28e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 110622073  97 VGKLHQGGLIHGDLTTSNMIVtDST--IYVIDFGLS 130
Cdd:cd05600  124 ISSLHQLGYIHRDLKPENFLI-DSSghIKLTDFGLA 158
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
30-129 8.66e-03

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


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 34.85  E-value: 8.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073  30 RIRELDERLRRERTRAEAKIISEARRLGIptpVVY----------------DVGQFSLEMELIQGRPLKDVLSPEL---S 90
Cdd:cd14048   38 RIRLPNNELAREKVLREVRALAKLDHPGI---VRYfnawlerppegwqekmDEVYLYIQMQLCRKENLKDWMNRRCtmeS 114
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 110622073  91 RKAGVL----------VGKLHQGGLIHGDLTTSNMIVT-DSTIYVIDFGL 129
Cdd:cd14048  115 RELFVClnifkqiasaVEYLHSKGLIHRDLKPSNVFFSlDDVVKVGDFGL 164
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
71-130 8.90e-03

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: 34.87  E-value: 8.90e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110622073  71 LEMELIQGRPLKDVLSPELS---RKAGVLVGK-------LHQGGLIHGDLTTSNMI----VTDSTIYVIDFGLS 130
Cdd:cd14169   78 LAMELVTGGELFDRIIERGSyteKDASQLIGQvlqavkyLHQLGIVHRDLKPENLLyatpFEDSKIMISDFGLS 151
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
97-130 9.31e-03

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


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 34.76  E-value: 9.31e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 110622073  97 VGKLHQGGLIHGDLTTSNMIVtDST--IYVIDFGLS 130
Cdd:cd05611  110 VEDLHQRGIIHRDIKPENLLI-DQTghLKLTDFGLS 144
PRK09605 PRK09605
bifunctional UGMP family protein/serine/threonine protein kinase; Validated
4-191 4.14e-84

bifunctional UGMP family protein/serine/threonine protein kinase; Validated


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 260.59  E-value: 4.14e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073   4 IRRQGAEAVVELLP----DRVIKTRVPKSYRIRELDERLRRERTRAEAKIISEARRLGIPTPVVYDV--GQFSLEMELIQ 77
Cdd:PRK09605 340 LIGKGAEADIKKGEylgrDAVIKERVPKGYRHPELDERLRTERTRAEARLLSEARRAGVPTPVIYDVdpEEKTIVMEYIG 419
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073  78 GRPLKDVL--SPELSRKAGVLVGKLHQGGLIHGDLTTSNMIVTDSTIYVIDFGLSYWDGTLEARGVDVHVYYQTLVSSHE 155
Cdd:PRK09605 420 GKDLKDVLegNPELVRKVGEIVAKLHKAGIVHGDLTTSNFIVRDDRLYLIDFGLGKYSDLIEDKAVDLHVLKQSLESTHY 499
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 110622073 156 NHEELMEAFAEGYRSSfPGANEVLRRVREIEYRGRY 191
Cdd:PRK09605 500 DFEELWEAFLEGYRET-EGAEDVLERLKEIEKRGRY 534
RIO2 COG0478
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
38-194 1.51e-06

RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction mechanisms];


Pssm-ID: 223554 [Multi-domain]  Cd Length: 304  Bit Score: 46.16  E-value: 1.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073  38 LRRERTRAEAKIISEARRLGIPTPVVYDVGQFSLEMELIQGRPLKDV-LSPELSRKA--GVL--VGKLHQGGLIHGDLTT 112
Cdd:COG0478  151 VSRLAAEREFEALQRLYPEGVKVPKPIAWNRHAVVMEYIEGVELYRLrLDVENPDEIldKILeeVRKAYRRGIVHGDLSE 230
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073 113 SNMIVT-DSTIYVIDFGlsywdgtleargvdvhvyyQTLVSSHENHEELME--------AFAEGYRSSFPGaNEVLRRVR 183
Cdd:COG0478  231 FNILVTeDGDIVVIDWP-------------------QAVPISHPDAEELLErdveniikYFRRKYGYKVEK-EEELDRVR 290
                        170
                 ....*....|.
gi 110622073 184 EIEYRGRYKTE 194
Cdd:COG0478  291 EASEFGKKEVE 301
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
7-130 6.43e-06

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 44.35  E-value: 6.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073   7 QGAEAVVELLPDR---VIKTRVPKSYRIRELDERLRRErtraeakiISEARRLGIPTPVV--YDVGQ----FSLEMELIQ 77
Cdd:COG0515   10 EGSFGEVYLARDRklvALKVLAKKLESKSKEVERFLRE--------IQILASLNHPPNIVklYDFFQdegsLYLVMEYVD 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110622073  78 GRPLKDVLSPELSRKAGVL-------------VGKLHQGGLIHGDLTTSNMIVT--DSTIYVIDFGLS 130
Cdd:COG0515   82 GGSLEDLLKKIGRKGPLSEsealfilaqilsaLEYLHSKGIIHRDIKPENILLDrdGRVVKLIDFGLA 149
RIO1 COG1718
Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms];
7-128 8.87e-06

Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms];


Pssm-ID: 224632 [Multi-domain]  Cd Length: 268  Bit Score: 43.85  E-value: 8.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073   7 QGAEAVVELLPDRVIKTRVPKSYRI-----------RELDERLRRER----------TRAEAKIISEARRLGIPTPVVYD 65
Cdd:COG1718   58 TGKEANVYLAETGDGRYVAVKIYRTstsefkrirryIQGDPRFRNSRsnrrklvfawARKEFRNLKRAYEAGVRVPEPIA 137
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110622073  66 VGQFSLEMELI--QGRP---LKDV-LSPELSRKAGVLVGK-----LHQGGLIHGDLTTSNMIVTDSTIYVIDFG 128
Cdd:COG1718  138 FRNNVLVMEFIgdDGLPaprLKDVpLELEEAEGLYEDVVEymrrlYKEAGLVHGDLSEYNILVHDGEPYIIDVS 211
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
30-155 1.82e-04

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 39.82  E-value: 1.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073    30 RIRELDERLRRERTRAEAKIISEARRLGIPTpvVYDV----GQFSLEMELIQGRPLKDVL------SPELSRK--AGVLV 97
Cdd:smart00220  31 VIKKKKIKKDRERILREIKILKKLKHPNIVR--LYDVfedeDKLYLVMEYCEGGDLFDLLkkrgrlSEDEARFylRQILS 108
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110622073    98 G--KLHQGGLIHGDLTTSN-MIVTDSTIYVIDFGLsywdgtleARGVDVHVYYQTLVSSHE 155
Cdd:smart00220 109 AleYLHSKGIVHRDLKPENiLLDEDGHVKLADFGL--------ARQLDPGEKLTTFVGTPE 161
UbiB TIGR01982
2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the ...
19-129 2.56e-04

2-polyprenylphenol 6-hydroxylase; This model represents the enzyme (UbiB) which catalyzes the first hydroxylation step in the ubiquinone biosynthetic pathway in bacteria. It is believed that the reaction is 2-polyprenylphenol -> 6-hydroxy-2-polyprenylphenol. This model finds hits primarily in the proteobacteria. The gene is also known as AarF in certain species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273909 [Multi-domain]  Cd Length: 437  Bit Score: 39.59  E-value: 2.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073   19 RVIKTRVPKSYRIR------ELDERLRRERT-RAEAKIISEARR-----LGIPTPVVY--DVGQFSLEMELIQGRPLKDV 84
Cdd:TIGR01982 169 RIVERLSPDSRRLRptevvkEFEKTLRRELDlRREAANASELGEnfkndPGVYVPEVYwdRTSERVLTMEWIDGIPLSDI 248
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 110622073   85 L---SPELSRK------AGVLVGKLHQGGLIHGDLTTSNMIVT-DSTIYVIDFGL 129
Cdd:TIGR01982 249 AaldEAGLDRKalaenlARSFLNQVLRDGFFHADLHPGNIFVLkDGKIIALDFGI 303
Pkinase pfam00069
Protein kinase domain;
20-130 1.18e-03

Protein kinase domain;


Pssm-ID: 278497 [Multi-domain]  Cd Length: 254  Bit Score: 37.19  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073   20 VIKTrVPKSYRIRELDERLRRERtraeaKIIseaRRLGIPTPV-VYDV----GQFSLEMELIQGRPLKDVL------SPE 88
Cdd:pfam00069  28 AVKK-IKKEKIKKKKDKNVLREI-----KIL---KKLNHPNIVrLYDVfedkDHLYLVLEYVEGGSLFDLLsekgafSER 98
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 110622073   89 LSRK--AGVLVG--KLHQGGLIHGDLTTSN-MIVTDSTIYVIDFGLS 130
Cdd:pfam00069  99 EAKFimKQILEGleYLHSNGIVHRDLKPENiLIDEDGNLKITDFGLA 145
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
105-189 5.26e-03

Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal transduction mechanisms];


Pssm-ID: 225213 [Multi-domain]  Cd Length: 331  Bit Score: 35.39  E-value: 5.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110622073 105 LIHGDLTTSNMIVTDST--IYVIDFGlsywDGTLEARGVDVHVyyqTLVSSHENHEE---LMEAFAEGYRSSFP------ 173
Cdd:COG2334  199 IIHGDLHPDNVLFDDDTdvSGFIDFD----DAGYGWFIYDLAI---ALNAWNGDEADpraAIAAFLEGYEEVRPltaael 271
                         90
                 ....*....|....*.
gi 110622073 174 GANEVLRRVREIEYRG 189
Cdd:COG2334  272 ELLPDLRRLRALRLWA 287
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.15
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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