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Conserved domains on  [gi|743517872|ref|WP_039035321|]
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MULTISPECIES: protein-glutamate O-methyltransferase CheR [Shewanella]

Protein Classification

CheR family methyltransferase( domain architecture ID 11442594)

CheR family methyltransferase is a class I SAM-dependent methyltransferase that catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; such as chemotaxis protein methyltransferase that methylates membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0008168|GO:0032259|GO:1904047
SCOP:  3000118

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CheR COG1352
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
10-271 5.51e-110

Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];


:

Pssm-ID: 440963 [Multi-domain]  Cd Length: 272  Bit Score: 319.42  E-value: 5.51e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872  10 PMTAADFGIIRELAYQHTGIVLPERKRHMVYSRLSRRLRLLRLTNFGDYCLKLQRDPLELAPFINALTTNLTAFFRERHH 89
Cdd:COG1352    3 ELSDAEFERLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPEELQALIDALTINVTEFFRDPEH 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872  90 FNFLETELVPYWQQRKQ--RRLRVWSAACSSGEEPYSIAMTLAEHFPAASGWDLKILATDLDTNVLARAEAGVYPLTGLE 167
Cdd:COG1352   83 FEALREEVLPELLARRRagRPLRIWSAGCSTGEEPYSLAMLLAEAGGELAGWRVEILATDISEEALEKARAGIYPERSLR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 168 AIPK-RQHHYLQSRAEEFSISSQIKKLIFFKQLNLLEPWPMQGPFDAIFCRNVLIYFDQSTKQKIVAGFRKLLADDGVLF 246
Cdd:COG1352  163 GLPPeYLSRYFTKEGGRYRIKPELREMVTFAQHNLLDDPPPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSLAPGGYLF 242
                        250       260
                 ....*....|....*....|....*...
gi 743517872 247 IGHSESLTNISREFETVAQ---TTYRLR 271
Cdd:COG1352  243 LGHSESLGGLSDLFEPVDKkgrFIYRKR 270
 
Name Accession Description Interval E-value
CheR COG1352
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
10-271 5.51e-110

Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];


Pssm-ID: 440963 [Multi-domain]  Cd Length: 272  Bit Score: 319.42  E-value: 5.51e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872  10 PMTAADFGIIRELAYQHTGIVLPERKRHMVYSRLSRRLRLLRLTNFGDYCLKLQRDPLELAPFINALTTNLTAFFRERHH 89
Cdd:COG1352    3 ELSDAEFERLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPEELQALIDALTINVTEFFRDPEH 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872  90 FNFLETELVPYWQQRKQ--RRLRVWSAACSSGEEPYSIAMTLAEHFPAASGWDLKILATDLDTNVLARAEAGVYPLTGLE 167
Cdd:COG1352   83 FEALREEVLPELLARRRagRPLRIWSAGCSTGEEPYSLAMLLAEAGGELAGWRVEILATDISEEALEKARAGIYPERSLR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 168 AIPK-RQHHYLQSRAEEFSISSQIKKLIFFKQLNLLEPWPMQGPFDAIFCRNVLIYFDQSTKQKIVAGFRKLLADDGVLF 246
Cdd:COG1352  163 GLPPeYLSRYFTKEGGRYRIKPELREMVTFAQHNLLDDPPPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSLAPGGYLF 242
                        250       260
                 ....*....|....*....|....*...
gi 743517872 247 IGHSESLTNISREFETVAQ---TTYRLR 271
Cdd:COG1352  243 LGHSESLGGLSDLFEPVDKkgrFIYRKR 270
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
13-271 1.14e-96

Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to form gamma-glutamyl methyl ester residues.


Pssm-ID: 214534 [Multi-domain]  Cd Length: 264  Bit Score: 285.33  E-value: 1.14e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872    13 AADFGIIRELAYQHTGIVLPERKRHMVYSRLSRRLRLLRLTNFGDYCLKLQRDPL--ELAPFINALTTNLTAFFRERHHF 90
Cdd:smart00138   1 DADFRRFCVLIYSRTGIVLTDYKRTLLQSRLSRRLRVLGLKDFSEYLELLTSHRGeeELAELLDLMTTNETRFFRESKHF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872    91 NFLETELVPYWQQRKQ--RRLRVWSAACSSGEEPYSIAMTLAEHFPAASGWDLKILATDLDTNVLARAEAGVYPLTGLEA 168
Cdd:smart00138  81 EALEEKVLPLLIASRRhgRRVRIWSAGCSTGEEPYSLAMLLAETLPKGREPDVKILATDIDLKALEKARAGIYPERELED 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872   169 IPK-RQHHYLQSRAEEFSISSQIKKLIFFKQLNLLEPWPMQGPFDAIFCRNVLIYFDQSTKQKIVAGFRKLLADDGVLFI 247
Cdd:smart00138 161 LPKaLLARYFKEVEDKYRVKPELKERVRFAKHNLLAESPPLGDFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGGYLFL 240
                          250       260
                   ....*....|....*....|....
gi 743517872   248 GHSESLTNISREFETVAQTTYRLR 271
Cdd:smart00138 241 GHSESLPGLTDKFEPIEGTVYFYS 264
PRK10611 PRK10611
protein-glutamate O-methyltransferase CheR;
9-270 1.88e-82

protein-glutamate O-methyltransferase CheR;


Pssm-ID: 236725 [Multi-domain]  Cd Length: 287  Bit Score: 250.04  E-value: 1.88e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872   9 FPMTAADFGIIRELAYQHTGIVLPERKRHMVYSRLSRRLRLLRLTNFGDYCLKLQRDP--LELAPFINALTTNLTAFFRE 86
Cdd:PRK10611  20 LALSDAHFRRICQLIYQRAGIVLADHKREMVYNRLVRRLRSLGLNDFGQYLALLESNQnsAEWQAFINALTTNLTAFFRE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872  87 RHHFNFLETElvpywQQRKQRRLRVWSAACSSGEEPYSIAMTLAEHF-PAASGWdlKILATDLDTNVLARAEAGVYPLTG 165
Cdd:PRK10611 100 AHHFPILAEH-----ARRRSGEYRVWSAAASTGEEPYSIAMTLADTLgTAPGRW--KVFASDIDTEVLEKARSGIYRQEE 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 166 LEAIP--KRQHHYLQ---SRAEEFSISSQIKKLIFFKQLNLLEP-WPMQGPFDAIFCRNVLIYFDQSTKQKIVAGFRKLL 239
Cdd:PRK10611 173 LKTLSpqQLQRYFMRgtgPHEGLVRVRQELANYVDFQQLNLLAKqWAVPGPFDAIFCRNVMIYFDKTTQERILRRFVPLL 252
                        250       260       270
                 ....*....|....*....|....*....|.
gi 743517872 240 ADDGVLFIGHSESLTNISREFETVAQTTYRL 270
Cdd:PRK10611 253 KPDGLLFAGHSENFSQLSREFYLRGQTVYGL 283
CheR pfam01739
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ...
79-263 4.50e-79

CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling mechanism in bacteria. CheR methylates the chemotaxis receptor at specific glutamate residues. CheR is an S-adenosylmethionine- dependent methyltransferase - the C-terminal domain (this one) binds SAM.


Pssm-ID: 426403  Cd Length: 190  Bit Score: 237.95  E-value: 4.50e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872   79 NLTAFFRERHHFNFLETELVPYWQQRKQ-RRLRVWSAACSSGEEPYSIAMTLAEHFPAASGWDLKILATDLDTNVLARAE 157
Cdd:pfam01739   1 NETRFFREPAHFEELKKYVLPLLAKAKNgKRVRIWSAGCSSGEEPYSLAMLLKETFPNAARWDFKILATDIDLSVLEKAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872  158 AGVYPLTGLEAIPK--RQHHYLQSRAEEFSISSQIKKLIFFKQLNLLEPWPMQGPFDAIFCRNVLIYFDQSTKQKIVAGF 235
Cdd:pfam01739  81 AGVYPERELEGLPEelLRRYFEKTAGGGYTVKPEIKSMVLFEYLNLLDEYPPLGDFDVIFCRNVLIYFDEETQRKILNRF 160
                         170       180
                  ....*....|....*....|....*...
gi 743517872  236 RKLLADDGVLFIGHSESLTNISREFETV 263
Cdd:pfam01739 161 AEKLKPGGYLFLGHSEALPGNPDKFKKV 188
 
Name Accession Description Interval E-value
CheR COG1352
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
10-271 5.51e-110

Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];


Pssm-ID: 440963 [Multi-domain]  Cd Length: 272  Bit Score: 319.42  E-value: 5.51e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872  10 PMTAADFGIIRELAYQHTGIVLPERKRHMVYSRLSRRLRLLRLTNFGDYCLKLQRDPLELAPFINALTTNLTAFFRERHH 89
Cdd:COG1352    3 ELSDAEFERLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPEELQALIDALTINVTEFFRDPEH 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872  90 FNFLETELVPYWQQRKQ--RRLRVWSAACSSGEEPYSIAMTLAEHFPAASGWDLKILATDLDTNVLARAEAGVYPLTGLE 167
Cdd:COG1352   83 FEALREEVLPELLARRRagRPLRIWSAGCSTGEEPYSLAMLLAEAGGELAGWRVEILATDISEEALEKARAGIYPERSLR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 168 AIPK-RQHHYLQSRAEEFSISSQIKKLIFFKQLNLLEPWPMQGPFDAIFCRNVLIYFDQSTKQKIVAGFRKLLADDGVLF 246
Cdd:COG1352  163 GLPPeYLSRYFTKEGGRYRIKPELREMVTFAQHNLLDDPPPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSLAPGGYLF 242
                        250       260
                 ....*....|....*....|....*...
gi 743517872 247 IGHSESLTNISREFETVAQ---TTYRLR 271
Cdd:COG1352  243 LGHSESLGGLSDLFEPVDKkgrFIYRKR 270
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
13-271 1.14e-96

Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to form gamma-glutamyl methyl ester residues.


Pssm-ID: 214534 [Multi-domain]  Cd Length: 264  Bit Score: 285.33  E-value: 1.14e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872    13 AADFGIIRELAYQHTGIVLPERKRHMVYSRLSRRLRLLRLTNFGDYCLKLQRDPL--ELAPFINALTTNLTAFFRERHHF 90
Cdd:smart00138   1 DADFRRFCVLIYSRTGIVLTDYKRTLLQSRLSRRLRVLGLKDFSEYLELLTSHRGeeELAELLDLMTTNETRFFRESKHF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872    91 NFLETELVPYWQQRKQ--RRLRVWSAACSSGEEPYSIAMTLAEHFPAASGWDLKILATDLDTNVLARAEAGVYPLTGLEA 168
Cdd:smart00138  81 EALEEKVLPLLIASRRhgRRVRIWSAGCSTGEEPYSLAMLLAETLPKGREPDVKILATDIDLKALEKARAGIYPERELED 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872   169 IPK-RQHHYLQSRAEEFSISSQIKKLIFFKQLNLLEPWPMQGPFDAIFCRNVLIYFDQSTKQKIVAGFRKLLADDGVLFI 247
Cdd:smart00138 161 LPKaLLARYFKEVEDKYRVKPELKERVRFAKHNLLAESPPLGDFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGGYLFL 240
                          250       260
                   ....*....|....*....|....
gi 743517872   248 GHSESLTNISREFETVAQTTYRLR 271
Cdd:smart00138 241 GHSESLPGLTDKFEPIEGTVYFYS 264
PRK10611 PRK10611
protein-glutamate O-methyltransferase CheR;
9-270 1.88e-82

protein-glutamate O-methyltransferase CheR;


Pssm-ID: 236725 [Multi-domain]  Cd Length: 287  Bit Score: 250.04  E-value: 1.88e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872   9 FPMTAADFGIIRELAYQHTGIVLPERKRHMVYSRLSRRLRLLRLTNFGDYCLKLQRDP--LELAPFINALTTNLTAFFRE 86
Cdd:PRK10611  20 LALSDAHFRRICQLIYQRAGIVLADHKREMVYNRLVRRLRSLGLNDFGQYLALLESNQnsAEWQAFINALTTNLTAFFRE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872  87 RHHFNFLETElvpywQQRKQRRLRVWSAACSSGEEPYSIAMTLAEHF-PAASGWdlKILATDLDTNVLARAEAGVYPLTG 165
Cdd:PRK10611 100 AHHFPILAEH-----ARRRSGEYRVWSAAASTGEEPYSIAMTLADTLgTAPGRW--KVFASDIDTEVLEKARSGIYRQEE 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 166 LEAIP--KRQHHYLQ---SRAEEFSISSQIKKLIFFKQLNLLEP-WPMQGPFDAIFCRNVLIYFDQSTKQKIVAGFRKLL 239
Cdd:PRK10611 173 LKTLSpqQLQRYFMRgtgPHEGLVRVRQELANYVDFQQLNLLAKqWAVPGPFDAIFCRNVMIYFDKTTQERILRRFVPLL 252
                        250       260       270
                 ....*....|....*....|....*....|.
gi 743517872 240 ADDGVLFIGHSESLTNISREFETVAQTTYRL 270
Cdd:PRK10611 253 KPDGLLFAGHSENFSQLSREFYLRGQTVYGL 283
CheR pfam01739
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ...
79-263 4.50e-79

CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling mechanism in bacteria. CheR methylates the chemotaxis receptor at specific glutamate residues. CheR is an S-adenosylmethionine- dependent methyltransferase - the C-terminal domain (this one) binds SAM.


Pssm-ID: 426403  Cd Length: 190  Bit Score: 237.95  E-value: 4.50e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872   79 NLTAFFRERHHFNFLETELVPYWQQRKQ-RRLRVWSAACSSGEEPYSIAMTLAEHFPAASGWDLKILATDLDTNVLARAE 157
Cdd:pfam01739   1 NETRFFREPAHFEELKKYVLPLLAKAKNgKRVRIWSAGCSSGEEPYSLAMLLKETFPNAARWDFKILATDIDLSVLEKAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872  158 AGVYPLTGLEAIPK--RQHHYLQSRAEEFSISSQIKKLIFFKQLNLLEPWPMQGPFDAIFCRNVLIYFDQSTKQKIVAGF 235
Cdd:pfam01739  81 AGVYPERELEGLPEelLRRYFEKTAGGGYTVKPEIKSMVLFEYLNLLDEYPPLGDFDVIFCRNVLIYFDEETQRKILNRF 160
                         170       180
                  ....*....|....*....|....*...
gi 743517872  236 RKLLADDGVLFIGHSESLTNISREFETV 263
Cdd:pfam01739 161 AEKLKPGGYLFLGHSEALPGNPDKFKKV 188
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
86-247 1.17e-06

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 46.93  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872  86 ERHHFNFLETELVPYWQQRKQRRLRVWSAACSSGEepysiamtLAEHFpAASGWDlkILATDLDTNVLARAEagvypltg 165
Cdd:COG2227    3 DPDARDFWDRRLAALLARLLPAGGRVLDVGCGTGR--------LALAL-ARRGAD--VTGVDISPEALEIAR-------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 166 lEAIPKRQHHYLQSRAEEFSISSqikkliffkqlnllepwpmqGPFDAIFCRNVLIYFDQStkQKIVAGFRKLLADDGVL 245
Cdd:COG2227   64 -ERAAELNVDFVQGDLEDLPLED--------------------GSFDLVICSEVLEHLPDP--AALLRELARLLKPGGLL 120

                 ..
gi 743517872 246 FI 247
Cdd:COG2227  121 LL 122
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
124-245 2.56e-05

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 42.35  E-value: 2.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872  124 SIAMTLAEHFPaasgwDLKILATDLDTNVLARAEAgvypltglEAIPKRQHHYLQSRaeefsissqikklifFKQLNLLE 203
Cdd:pfam08242   9 TLLRALLEALP-----GLEYTGLDISPAALEAARE--------RLAALGLLNAVRVE---------------LFQLDLGE 60
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 743517872  204 PWPmqGPFDAIFCRNVLIYFDQstKQKIVAGFRKLLADDGVL 245
Cdd:pfam08242  61 LDP--GSFDVVVASNVLHHLAD--PRAVLRNIRRLLKPGGVL 98
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
164-247 4.46e-05

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 42.99  E-value: 4.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872 164 TGLEaIPKRQHHYLQSRAEEFSISSQIKklifFKQLNLLEpWPMQGPFDAIFCRNVLIYFDQSTKQKIVAGFRKLLADDG 243
Cdd:COG2230   78 TGVT-LSPEQLEYARERAAEAGLADRVE----VRLADYRD-LPADGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGG 151

                 ....
gi 743517872 244 VLFI 247
Cdd:COG2230  152 RLLL 155
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
194-247 7.82e-05

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 42.60  E-value: 7.82e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 743517872 194 IFFKQLNLLEPWPM-QGPFDAIFCRNVLIYFDQSTKQKIVAGFRKLLADDGVLFI 247
Cdd:COG0500   77 VEFLVADLAELDPLpAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLL 131
CheR_N pfam03705
CheR methyltransferase, all-alpha domain; CheR proteins are part of the chemotaxis signaling ...
14-66 2.98e-04

CheR methyltransferase, all-alpha domain; CheR proteins are part of the chemotaxis signaling mechanism in bacteria. CheR methylates the chemotaxis receptor at specific glutamate residues. CheR is an S-adenosylmethionine- dependent methyltransferase.


Pssm-ID: 461017 [Multi-domain]  Cd Length: 53  Bit Score: 37.80  E-value: 2.98e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 743517872   14 ADFGIIRELAYQHTGIVLPERKRHMVYSRLSRRLRLLRLTNFGDYCLKLQRDP 66
Cdd:pfam03705   1 AEFERLLELIYRRTGIDLSDYKRSLLERRLSRRMRALGLDSFSEYLDLLRSDP 53
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
114-243 1.30e-03

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 37.16  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743517872  114 AACSSGeepySIAMTLAEHFPAasgwdlKILATDLDTNVLARAeagvypltgleaipkrqhhylQSRAEEFSISsqikkl 193
Cdd:pfam13649   4 LGCGTG----RLTLALARRGGA------RVTGVDLSPEMLERA---------------------RERAAEAGLN------ 46
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 743517872  194 IFFKQLNLLEPWPMQGPFDAIFCRNVLIYFDQSTKQKIVAGFRKLLADDG 243
Cdd:pfam13649  47 VEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPDLEAALREIARVLKPGG 96
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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