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Conserved domains on  [gi|446505028|ref|WP_000582882|]
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MULTISPECIES: protein-glutamate O-methyltransferase CheR [Bacillus]

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
PubMed:  9115443|12504684|23180741|12826405
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];
1-260 1.11e-91

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


:

Pssm-ID: 440963 [Multi-domain]  Cd Length: 272  Bit Score: 271.65  E-value: 1.11e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505028   1 MIIEQDYDHFIASFKQQFNMDIASYKQDRMRRRIDAFISRKGFENYTNFLSKLRADQNLFLNFIDYITINVSEFFRNKER 80
Cdd:COG1352    3 ELSDAEFERLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPEELQALIDALTINVTEFFRDPEH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505028  81 WQTLESKALPKLLEQNSGK--LKVWSAACAAGEEPYTLSLILSKH---LAPFRFEIQATDLDFHILETAKRGQYTERSLK 155
Cdd:COG1352   83 FEALREEVLPELLARRRAGrpLRIWSAGCSTGEEPYSLAMLLAEAggeLAGWRVEILATDISEEALEKARAGIYPERSLR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505028 156 ELPTDLKERHFTKENDLYSLHQNIKQNVSFKQHDLLM-QSFDTNYDLIICRNVMIYFTEEARVKLYEKFSRSLRKGGVLF 234
Cdd:COG1352  163 GLPPEYLSRYFTKEGGRYRIKPELREMVTFAQHNLLDdPPPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSLAPGGYLF 242

                        250       260
                 ....*....|....*....|....*...
gi 446505028 235 VGSTEQILTPERY--NLQRFDTFFYEKI 260
Cdd:COG1352  243 LGHSESLGGLSDLfePVDKKGRFIYRKR 270
 
Name Accession Description Interval E-value
CheR COG1352
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
1-260 1.11e-91

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


Pssm-ID: 440963 [Multi-domain]  Cd Length: 272  Bit Score: 271.65  E-value: 1.11e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505028   1 MIIEQDYDHFIASFKQQFNMDIASYKQDRMRRRIDAFISRKGFENYTNFLSKLRADQNLFLNFIDYITINVSEFFRNKER 80
Cdd:COG1352    3 ELSDAEFERLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPEELQALIDALTINVTEFFRDPEH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505028  81 WQTLESKALPKLLEQNSGK--LKVWSAACAAGEEPYTLSLILSKH---LAPFRFEIQATDLDFHILETAKRGQYTERSLK 155
Cdd:COG1352   83 FEALREEVLPELLARRRAGrpLRIWSAGCSTGEEPYSLAMLLAEAggeLAGWRVEILATDISEEALEKARAGIYPERSLR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505028 156 ELPTDLKERHFTKENDLYSLHQNIKQNVSFKQHDLLM-QSFDTNYDLIICRNVMIYFTEEARVKLYEKFSRSLRKGGVLF 234
Cdd:COG1352  163 GLPPEYLSRYFTKEGGRYRIKPELREMVTFAQHNLLDdPPPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSLAPGGYLF 242

                        250       260
                 ....*....|....*....|....*...
gi 446505028 235 VGSTEQILTPERY--NLQRFDTFFYEKI 260
Cdd:COG1352  243 LGHSESLGGLSDLfePVDKKGRFIYRKR 270
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
 4-241 3.63e-73

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: 224.09  E-value: 3.63e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505028     4 EQDYDHFIASFKQQFNMDIASYKQDRMRRRIDAFISRKGFENYTNFLSKLRADQNLFL--NFIDYITINVSEFFRNKERW 81
Cdd:smart00138   1 DADFRRFCVLIYSRTGIVLTDYKRTLLQSRLSRRLRVLGLKDFSEYLELLTSHRGEEElaELLDLMTTNETRFFRESKHF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505028    82 QTLESKALPKLLE--QNSGKLKVWSAACAAGEEPYTLSLILSKHL---APFRFEIQATDLDFHILETAKRGQYTERSLKE 156
Cdd:smart00138  81 EALEEKVLPLLIAsrRHGRRVRIWSAGCSTGEEPYSLAMLLAETLpkgREPDVKILATDIDLKALEKARAGIYPERELED 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505028   157 LPTDLKERHFTKENDLYSLHQNIKQNVSFKQHDLLMQSF-DTNYDLIICRNVMIYFTEEARVKLYEKFSRSLRKGGVLFV 235
Cdd:smart00138 161 LPKALLARYFKEVEDKYRVKPELKERVRFAKHNLLAESPpLGDFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGGYLFL 240


                   ....*.
gi 446505028   236 GSTEQI 241
Cdd:smart00138 241 GHSESL 246
CheR pfam01739
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ...
 70-241 5.41e-60

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: 187.87  E-value: 5.41e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505028   70 NVSEFFRNKERWQTLESKALPKLLEQNSGK-LKVWSAACAAGEEPYTLSLILSKHL---APFRFEIQATDLDFHILETAK 145
Cdd:pfam01739   1 NETRFFREPAHFEELKKYVLPLLAKAKNGKrVRIWSAGCSSGEEPYSLAMLLKETFpnaARWDFKILATDIDLSVLEKAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505028  146 RGQYTERSLKELPTDLKERHFTK-ENDLYSLHQNIKQNVSFKQHDLL-MQSFDTNYDLIICRNVMIYFTEEARVKLYEKF 223
Cdd:pfam01739  81 AGVYPERELEGLPEELLRRYFEKtAGGGYTVKPEIKSMVLFEYLNLLdEYPPLGDFDVIFCRNVLIYFDEETQRKILNRF 160

                         170
                  ....*....|....*...
gi 446505028  224 SRSLRKGGVLFVGSTEQI 241
Cdd:pfam01739 161 AEKLKPGGYLFLGHSEAL 178
PRK10611 PRK10611
protein-glutamate O-methyltransferase CheR;
22-239 1.30e-32

protein-glutamate O-methyltransferase CheR;


Pssm-ID: 236725 [Multi-domain]  Cd Length: 287  Bit Score: 120.61  E-value: 1.30e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505028  22 IASYKQD----RMRRRIDAFisrkGFENYTNFLSKLRADQNL--FLNFIDYITINVSEFFRnkerwqtlESKALPKLLE- 94
Cdd:PRK10611  42 LADHKREmvynRLVRRLRSL----GLNDFGQYLALLESNQNSaeWQAFINALTTNLTAFFR--------EAHHFPILAEh 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505028  95 --QNSGKLKVWSAACAAGEEPYTLSLILSKHL--APFRFEIQATDLDFHILETAKRGQYTERSLKELPTDLKERHFTKEN 170
Cdd:PRK10611 110 arRRSGEYRVWSAAASTGEEPYSIAMTLADTLgtAPGRWKVFASDIDTEVLEKARSGIYRQEELKTLSPQQLQRYFMRGT 189

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446505028 171 DLYS----LHQNIKQNVSFKQHDLLMQ--SFDTNYDLIICRNVMIYFTEEARVKLYEKFSRSLRKGGVLFVGSTE 239
Cdd:PRK10611 190 GPHEglvrVRQELANYVDFQQLNLLAKqwAVPGPFDAIFCRNVMIYFDKTTQERILRRFVPLLKPDGLLFAGHSE 264
 
Name Accession Description Interval E-value
CheR COG1352
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
1-260 1.11e-91

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


Pssm-ID: 440963 [Multi-domain]  Cd Length: 272  Bit Score: 271.65  E-value: 1.11e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505028   1 MIIEQDYDHFIASFKQQFNMDIASYKQDRMRRRIDAFISRKGFENYTNFLSKLRADQNLFLNFIDYITINVSEFFRNKER 80
Cdd:COG1352    3 ELSDAEFERLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPEELQALIDALTINVTEFFRDPEH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505028  81 WQTLESKALPKLLEQNSGK--LKVWSAACAAGEEPYTLSLILSKH---LAPFRFEIQATDLDFHILETAKRGQYTERSLK 155
Cdd:COG1352   83 FEALREEVLPELLARRRAGrpLRIWSAGCSTGEEPYSLAMLLAEAggeLAGWRVEILATDISEEALEKARAGIYPERSLR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505028 156 ELPTDLKERHFTKENDLYSLHQNIKQNVSFKQHDLLM-QSFDTNYDLIICRNVMIYFTEEARVKLYEKFSRSLRKGGVLF 234
Cdd:COG1352  163 GLPPEYLSRYFTKEGGRYRIKPELREMVTFAQHNLLDdPPPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSLAPGGYLF 242

                        250       260
                 ....*....|....*....|....*...
gi 446505028 235 VGSTEQILTPERY--NLQRFDTFFYEKI 260
Cdd:COG1352  243 LGHSESLGGLSDLfePVDKKGRFIYRKR 270
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
 4-241 3.63e-73

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: 224.09  E-value: 3.63e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505028     4 EQDYDHFIASFKQQFNMDIASYKQDRMRRRIDAFISRKGFENYTNFLSKLRADQNLFL--NFIDYITINVSEFFRNKERW 81
Cdd:smart00138   1 DADFRRFCVLIYSRTGIVLTDYKRTLLQSRLSRRLRVLGLKDFSEYLELLTSHRGEEElaELLDLMTTNETRFFRESKHF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505028    82 QTLESKALPKLLE--QNSGKLKVWSAACAAGEEPYTLSLILSKHL---APFRFEIQATDLDFHILETAKRGQYTERSLKE 156
Cdd:smart00138  81 EALEEKVLPLLIAsrRHGRRVRIWSAGCSTGEEPYSLAMLLAETLpkgREPDVKILATDIDLKALEKARAGIYPERELED 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505028   157 LPTDLKERHFTKENDLYSLHQNIKQNVSFKQHDLLMQSF-DTNYDLIICRNVMIYFTEEARVKLYEKFSRSLRKGGVLFV 235
Cdd:smart00138 161 LPKALLARYFKEVEDKYRVKPELKERVRFAKHNLLAESPpLGDFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGGYLFL 240


                   ....*.
gi 446505028   236 GSTEQI 241
Cdd:smart00138 241 GHSESL 246
CheR pfam01739
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ...
 70-241 5.41e-60

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: 187.87  E-value: 5.41e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505028   70 NVSEFFRNKERWQTLESKALPKLLEQNSGK-LKVWSAACAAGEEPYTLSLILSKHL---APFRFEIQATDLDFHILETAK 145
Cdd:pfam01739   1 NETRFFREPAHFEELKKYVLPLLAKAKNGKrVRIWSAGCSSGEEPYSLAMLLKETFpnaARWDFKILATDIDLSVLEKAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505028  146 RGQYTERSLKELPTDLKERHFTK-ENDLYSLHQNIKQNVSFKQHDLL-MQSFDTNYDLIICRNVMIYFTEEARVKLYEKF 223
Cdd:pfam01739  81 AGVYPERELEGLPEELLRRYFEKtAGGGYTVKPEIKSMVLFEYLNLLdEYPPLGDFDVIFCRNVLIYFDEETQRKILNRF 160

                         170
                  ....*....|....*...
gi 446505028  224 SRSLRKGGVLFVGSTEQI 241
Cdd:pfam01739 161 AEKLKPGGYLFLGHSEAL 178
PRK10611 PRK10611
protein-glutamate O-methyltransferase CheR;
22-239 1.30e-32

protein-glutamate O-methyltransferase CheR;


Pssm-ID: 236725 [Multi-domain]  Cd Length: 287  Bit Score: 120.61  E-value: 1.30e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505028  22 IASYKQD----RMRRRIDAFisrkGFENYTNFLSKLRADQNL--FLNFIDYITINVSEFFRnkerwqtlESKALPKLLE- 94
Cdd:PRK10611  42 LADHKREmvynRLVRRLRSL----GLNDFGQYLALLESNQNSaeWQAFINALTTNLTAFFR--------EAHHFPILAEh 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505028  95 --QNSGKLKVWSAACAAGEEPYTLSLILSKHL--APFRFEIQATDLDFHILETAKRGQYTERSLKELPTDLKERHFTKEN 170
Cdd:PRK10611 110 arRRSGEYRVWSAAASTGEEPYSIAMTLADTLgtAPGRWKVFASDIDTEVLEKARSGIYRQEELKTLSPQQLQRYFMRGT 189

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446505028 171 DLYS----LHQNIKQNVSFKQHDLLMQ--SFDTNYDLIICRNVMIYFTEEARVKLYEKFSRSLRKGGVLFVGSTE 239
Cdd:PRK10611 190 GPHEglvrVRQELANYVDFQQLNLLAKqwAVPGPFDAIFCRNVMIYFDKTTQERILRRFVPLLKPDGLLFAGHSE 264
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 182-231 3.69e-07

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 47.17  E-value: 3.69e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446505028  182 NVSFKQHDLLMQSFDTN-YDLIICRNVMIYFTEEARVKLYEKFSRSLRKGG 231
Cdd:pfam13649  46 NVEFVQGDAEDLPFPDGsFDLVVSSGVLHHLPDPDLEAALREIARVLKPGG 96
CheR_N pfam03705
CheR methyltransferase, all-alpha domain; CheR proteins are part of the chemotaxis signaling ...
 5-57 7.85e-06

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: 42.04  E-value: 7.85e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446505028    5 QDYDHFIASFKQQFNMDIASYKQDRMRRRIDAFISRKGFENYTNFLSKLRADQ 57
Cdd:pfam03705   1 AEFERLLELIYRRTGIDLSDYKRSLLERRLSRRMRALGLDSFSEYLDLLRSDP 53
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 182-235 1.61e-04

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 41.44  E-value: 1.61e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446505028 182 NVSFKQHDLLM--QSFDTNYDLIICRNVMIYFTEEARVKLYEKFSRSLRKGGVLFV 235
Cdd:COG0500   76 NVEFLVADLAEldPLPAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLL 131
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 77-235 7.30e-04

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: 38.46  E-value: 7.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505028  77 NKERWqtleSKALPKLLEQNSGK-LKVWSAACAAGeepytlslILSKHLAPFRFEIQATDLDFHILETAKRgqyterslk 155
Cdd:COG2227    6 ARDFW----DRRLAALLARLLPAgGRVLDVGCGTG--------RLALALARRGADVTGVDISPEALEIARE--------- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505028 156 elptdlkerhftkendlyslhQNIKQNVSFKQHDLL-MQSFDTNYDLIICRNVMIYFTEEARVklYEKFSRSLRKGGVLF 234
Cdd:COG2227   65 ---------------------RAAELNVDFVQGDLEdLPLEDGSFDLVICSEVLEHLPDPAAL--LRELARLLKPGGLLL 121


                 .
gi 446505028 235 V 235
Cdd:COG2227  122 L 122
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 182-235 1.59e-03

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 38.05  E-value: 1.59e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446505028 182 NVSFKQHDLLMQSFDTN-YDLIICRNVMIYFTEEARVklYEKFSRSLRKGGVLFV 235
Cdd:COG2226   70 NVEFVVGDAEDLPFPDGsFDLVISSFVLHHLPDPERA--LAEIARVLKPGGRLVV 122
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 181-237 3.34e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 37.01  E-value: 3.34e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505028  181 QNVSFKQ---HDLLMQSFDTNYDLIICRNVMIYFTEEARVklYEKFSRSLRKGGVLFVGS 237
Cdd:pfam13847  54 DNVEFEQgdiEELPELLEDDKFDVVISNCVLNHIPDPDKV--LQEILRVLKPGGRLIISD 111
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 182-235 9.68e-03

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 35.68  E-value: 9.68e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446505028 182 NVSFKQHDLLMQSFDTNYDLIICRNVMIYFTEEARVKLYEKFSRSLRKGGVLFV 235
Cdd:COG2230  102 RVEVRLADYRDLPADGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLL 155
 
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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