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Conserved domains on  [gi|446505031|ref|WP_000582885|]
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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 8.23e-91

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


:

Pssm-ID: 440963 [Multi-domain]  Cd Length: 272  Bit Score: 269.34  E-value: 8.23e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505031   1 MIIEQDYDHFIASFKQQFNMDIASYKQDRMRRRIDAFISRKGFENYTSFLSNLRTDQKLFLSFIDYITINVSEFFRNKER 80
Cdd:COG1352    3 ELSDAEFERLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPEELQALIDALTINVTEFFRDPEH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505031  81 WQTLESKALPKLLEQN--NGKLKVWSAACAAGEEPYTLSLILSKH---LAPYRFEIQATDLDFHILETAKRGQYTERSLK 155
Cdd:COG1352   83 FEALREEVLPELLARRraGRPLRIWSAGCSTGEEPYSLAMLLAEAggeLAGWRVEILATDISEEALEKARAGIYPERSLR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505031 156 ELPADLKERHFTKENDIYSLHQNIKQNVTFKQHDLLM-QSFDTNYDLIICRNVMIYFTEEARVKLYEKFSRALRKGGVLF 234
Cdd:COG1352  163 GLPPEYLSRYFTKEGGRYRIKPELREMVTFAQHNLLDdPPPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSLAPGGYLF 242

                        250       260
                 ....*....|....*....|....*...
gi 446505031 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 8.23e-91

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


Pssm-ID: 440963 [Multi-domain]  Cd Length: 272  Bit Score: 269.34  E-value: 8.23e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505031   1 MIIEQDYDHFIASFKQQFNMDIASYKQDRMRRRIDAFISRKGFENYTSFLSNLRTDQKLFLSFIDYITINVSEFFRNKER 80
Cdd:COG1352    3 ELSDAEFERLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPEELQALIDALTINVTEFFRDPEH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505031  81 WQTLESKALPKLLEQN--NGKLKVWSAACAAGEEPYTLSLILSKH---LAPYRFEIQATDLDFHILETAKRGQYTERSLK 155
Cdd:COG1352   83 FEALREEVLPELLARRraGRPLRIWSAGCSTGEEPYSLAMLLAEAggeLAGWRVEILATDISEEALEKARAGIYPERSLR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505031 156 ELPADLKERHFTKENDIYSLHQNIKQNVTFKQHDLLM-QSFDTNYDLIICRNVMIYFTEEARVKLYEKFSRALRKGGVLF 234
Cdd:COG1352  163 GLPPEYLSRYFTKEGGRYRIKPELREMVTFAQHNLLDdPPPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSLAPGGYLF 242

                        250       260
                 ....*....|....*....|....*...
gi 446505031 235 VGSTEQILTPERY--NLQRFDTFFYEKI 260
Cdd:COG1352  243 LGHSESLGGLSDLfePVDKKGRFIYRKR 270
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
 4-241 1.99e-74

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: 227.55  E-value: 1.99e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505031     4 EQDYDHFIASFKQQFNMDIASYKQDRMRRRIDAFISRKGFENYTSFLSNLRTDQKLFL--SFIDYITINVSEFFRNKERW 81
Cdd:smart00138   1 DADFRRFCVLIYSRTGIVLTDYKRTLLQSRLSRRLRVLGLKDFSEYLELLTSHRGEEElaELLDLMTTNETRFFRESKHF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505031    82 QTLESKALPKLLE--QNNGKLKVWSAACAAGEEPYTLSLILSKHL---APYRFEIQATDLDFHILETAKRGQYTERSLKE 156
Cdd:smart00138  81 EALEEKVLPLLIAsrRHGRRVRIWSAGCSTGEEPYSLAMLLAETLpkgREPDVKILATDIDLKALEKARAGIYPERELED 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505031   157 LPADLKERHFTKENDIYSLHQNIKQNVTFKQHDLLMQSF-DTNYDLIICRNVMIYFTEEARVKLYEKFSRALRKGGVLFV 235
Cdd:smart00138 161 LPKALLARYFKEVEDKYRVKPELKERVRFAKHNLLAESPpLGDFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGGYLFL 240


                   ....*.
gi 446505031   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 1.24e-61

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: 192.11  E-value: 1.24e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505031   70 NVSEFFRNKERWQTLESKALPKLLEQNNGK-LKVWSAACAAGEEPYTLSLILSKHL---APYRFEIQATDLDFHILETAK 145
Cdd:pfam01739   1 NETRFFREPAHFEELKKYVLPLLAKAKNGKrVRIWSAGCSSGEEPYSLAMLLKETFpnaARWDFKILATDIDLSVLEKAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505031  146 RGQYTERSLKELPADLKERHFTK-ENDIYSLHQNIKQNVTFKQHDLL-MQSFDTNYDLIICRNVMIYFTEEARVKLYEKF 223
Cdd:pfam01739  81 AGVYPERELEGLPEELLRRYFEKtAGGGYTVKPEIKSMVLFEYLNLLdEYPPLGDFDVIFCRNVLIYFDEETQRKILNRF 160

                         170
                  ....*....|....*...
gi 446505031  224 SRALRKGGVLFVGSTEQI 241
Cdd:pfam01739 161 AEKLKPGGYLFLGHSEAL 178
PRK10611 PRK10611
protein-glutamate O-methyltransferase CheR;
22-239 1.26e-32

protein-glutamate O-methyltransferase CheR;


Pssm-ID: 236725 [Multi-domain]  Cd Length: 287  Bit Score: 120.61  E-value: 1.26e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505031  22 IASYKQD----RMRRRIDAFisrkGFENYTSFLSNLRTDQ--KLFLSFIDYITINVSEFFRnkerwqtlESKALPKLLE- 94
Cdd:PRK10611  42 LADHKREmvynRLVRRLRSL----GLNDFGQYLALLESNQnsAEWQAFINALTTNLTAFFR--------EAHHFPILAEh 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505031  95 --QNNGKLKVWSAACAAGEEPYTLSLILSKHL--APYRFEIQATDLDFHILETAKRGQYTERSLKELPADLKERHFTKEN 170
Cdd:PRK10611 110 arRRSGEYRVWSAAASTGEEPYSIAMTLADTLgtAPGRWKVFASDIDTEVLEKARSGIYRQEELKTLSPQQLQRYFMRGT 189

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446505031 171 DIYS----LHQNIKQNVTFKQHDLLMQ--SFDTNYDLIICRNVMIYFTEEARVKLYEKFSRALRKGGVLFVGSTE 239
Cdd:PRK10611 190 GPHEglvrVRQELANYVDFQQLNLLAKqwAVPGPFDAIFCRNVMIYFDKTTQERILRRFVPLLKPDGLLFAGHSE 264
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 181-235 2.93e-03

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 36.64  E-value: 2.93e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446505031 181 QNVTFKQHDLLMQSF--DTNYDLIICRNVMIYFtEEARVKLYEKFSRALRKGGVLFV 235
Cdd:cd02440   47 DNVEVLKGDAEELPPeaDESFDVIISDPPLHHL-VEDLARFLEEARRLLKPGGVLVL 102
 
Name Accession Description Interval E-value
CheR COG1352
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
1-260 8.23e-91

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


Pssm-ID: 440963 [Multi-domain]  Cd Length: 272  Bit Score: 269.34  E-value: 8.23e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505031   1 MIIEQDYDHFIASFKQQFNMDIASYKQDRMRRRIDAFISRKGFENYTSFLSNLRTDQKLFLSFIDYITINVSEFFRNKER 80
Cdd:COG1352    3 ELSDAEFERLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPEELQALIDALTINVTEFFRDPEH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505031  81 WQTLESKALPKLLEQN--NGKLKVWSAACAAGEEPYTLSLILSKH---LAPYRFEIQATDLDFHILETAKRGQYTERSLK 155
Cdd:COG1352   83 FEALREEVLPELLARRraGRPLRIWSAGCSTGEEPYSLAMLLAEAggeLAGWRVEILATDISEEALEKARAGIYPERSLR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505031 156 ELPADLKERHFTKENDIYSLHQNIKQNVTFKQHDLLM-QSFDTNYDLIICRNVMIYFTEEARVKLYEKFSRALRKGGVLF 234
Cdd:COG1352  163 GLPPEYLSRYFTKEGGRYRIKPELREMVTFAQHNLLDdPPPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSLAPGGYLF 242

                        250       260
                 ....*....|....*....|....*...
gi 446505031 235 VGSTEQILTPERY--NLQRFDTFFYEKI 260
Cdd:COG1352  243 LGHSESLGGLSDLfePVDKKGRFIYRKR 270
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
 4-241 1.99e-74

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: 227.55  E-value: 1.99e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505031     4 EQDYDHFIASFKQQFNMDIASYKQDRMRRRIDAFISRKGFENYTSFLSNLRTDQKLFL--SFIDYITINVSEFFRNKERW 81
Cdd:smart00138   1 DADFRRFCVLIYSRTGIVLTDYKRTLLQSRLSRRLRVLGLKDFSEYLELLTSHRGEEElaELLDLMTTNETRFFRESKHF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505031    82 QTLESKALPKLLE--QNNGKLKVWSAACAAGEEPYTLSLILSKHL---APYRFEIQATDLDFHILETAKRGQYTERSLKE 156
Cdd:smart00138  81 EALEEKVLPLLIAsrRHGRRVRIWSAGCSTGEEPYSLAMLLAETLpkgREPDVKILATDIDLKALEKARAGIYPERELED 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505031   157 LPADLKERHFTKENDIYSLHQNIKQNVTFKQHDLLMQSF-DTNYDLIICRNVMIYFTEEARVKLYEKFSRALRKGGVLFV 235
Cdd:smart00138 161 LPKALLARYFKEVEDKYRVKPELKERVRFAKHNLLAESPpLGDFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGGYLFL 240


                   ....*.
gi 446505031   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 1.24e-61

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: 192.11  E-value: 1.24e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505031   70 NVSEFFRNKERWQTLESKALPKLLEQNNGK-LKVWSAACAAGEEPYTLSLILSKHL---APYRFEIQATDLDFHILETAK 145
Cdd:pfam01739   1 NETRFFREPAHFEELKKYVLPLLAKAKNGKrVRIWSAGCSSGEEPYSLAMLLKETFpnaARWDFKILATDIDLSVLEKAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505031  146 RGQYTERSLKELPADLKERHFTK-ENDIYSLHQNIKQNVTFKQHDLL-MQSFDTNYDLIICRNVMIYFTEEARVKLYEKF 223
Cdd:pfam01739  81 AGVYPERELEGLPEELLRRYFEKtAGGGYTVKPEIKSMVLFEYLNLLdEYPPLGDFDVIFCRNVLIYFDEETQRKILNRF 160

                         170
                  ....*....|....*...
gi 446505031  224 SRALRKGGVLFVGSTEQI 241
Cdd:pfam01739 161 AEKLKPGGYLFLGHSEAL 178
PRK10611 PRK10611
protein-glutamate O-methyltransferase CheR;
22-239 1.26e-32

protein-glutamate O-methyltransferase CheR;


Pssm-ID: 236725 [Multi-domain]  Cd Length: 287  Bit Score: 120.61  E-value: 1.26e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505031  22 IASYKQD----RMRRRIDAFisrkGFENYTSFLSNLRTDQ--KLFLSFIDYITINVSEFFRnkerwqtlESKALPKLLE- 94
Cdd:PRK10611  42 LADHKREmvynRLVRRLRSL----GLNDFGQYLALLESNQnsAEWQAFINALTTNLTAFFR--------EAHHFPILAEh 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505031  95 --QNNGKLKVWSAACAAGEEPYTLSLILSKHL--APYRFEIQATDLDFHILETAKRGQYTERSLKELPADLKERHFTKEN 170
Cdd:PRK10611 110 arRRSGEYRVWSAAASTGEEPYSIAMTLADTLgtAPGRWKVFASDIDTEVLEKARSGIYRQEELKTLSPQQLQRYFMRGT 189

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446505031 171 DIYS----LHQNIKQNVTFKQHDLLMQ--SFDTNYDLIICRNVMIYFTEEARVKLYEKFSRALRKGGVLFVGSTE 239
Cdd:PRK10611 190 GPHEglvrVRQELANYVDFQQLNLLAKqwAVPGPFDAIFCRNVMIYFDKTTQERILRRFVPLLKPDGLLFAGHSE 264
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 182-231 9.18e-08

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 48.71  E-value: 9.18e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446505031  182 NVTFKQHDLLMQSFDTN-YDLIICRNVMIYFTEEARVKLYEKFSRALRKGG 231
Cdd:pfam13649  46 NVEFVQGDAEDLPFPDGsFDLVVSSGVLHHLPDPDLEAALREIARVLKPGG 96
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
182-235 6.86e-06

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 43.66  E-value: 6.86e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446505031 182 NVTFKQHDLLMQSFDTNYDLIICRNVMIYFTEeaRVKLYEKFSRALRKGGVLFV 235
Cdd:COG4106   47 NVRFVVADLRDLDPPEPFDLVVSNAALHWLPD--HAALLARLAAALAPGGVLAV 98
CheR_N pfam03705
CheR methyltransferase, all-alpha domain; CheR proteins are part of the chemotaxis signaling ...
 5-57 7.11e-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: 42.42  E-value: 7.11e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446505031    5 QDYDHFIASFKQQFNMDIASYKQDRMRRRIDAFISRKGFENYTSFLSNLRTDQ 57
Cdd:pfam03705   1 AEFERLLELIYRRTGIDLSDYKRSLLERRLSRRMRALGLDSFSEYLDLLRSDP 53
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 182-235 9.34e-06

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 45.29  E-value: 9.34e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446505031 182 NVTFKQHDLLM--QSFDTNYDLIICRNVMIYFTEEARVKLYEKFSRALRKGGVLFV 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 9.66e-05

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: 41.16  E-value: 9.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505031  77 NKERWqtleSKALPKLLEQNNGK-LKVWSAACAAGeepytlslILSKHLAPYRFEIQATDLDFHILETAKRgqyterslk 155
Cdd:COG2227    6 ARDFW----DRRLAALLARLLPAgGRVLDVGCGTG--------RLALALARRGADVTGVDISPEALEIARE--------- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505031 156 elpadlkerhftkendiyslhQNIKQNVTFKQHDLL-MQSFDTNYDLIICRNVMIYFTEEARVklYEKFSRALRKGGVLF 234
Cdd:COG2227   65 ---------------------RAAELNVDFVQGDLEdLPLEDGSFDLVICSEVLEHLPDPAAL--LRELARLLKPGGLLL 121


                 .
gi 446505031 235 V 235
Cdd:COG2227  122 L 122
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 182-235 2.68e-04

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: 39.98  E-value: 2.68e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446505031 182 NVTFKQHDLLMQSFDTN-YDLIICRNVMIYFTEEARVklYEKFSRALRKGGVLFV 235
Cdd:COG2226   70 NVEFVVGDAEDLPFPDGsFDLVISSFVLHHLPDPERA--LAEIARVLKPGGRLVV 122
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 182-235 1.35e-03

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 38.37  E-value: 1.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446505031 182 NVTFKQHDLLMQSFDTNYDLIICRNVMIYFTEEARVKLYEKFSRALRKGGVLFV 235
Cdd:COG2230  102 RVEVRLADYRDLPADGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLL 155
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 181-237 1.80e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 37.78  E-value: 1.80e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446505031  181 QNVTFKQ---HDLLMQSFDTNYDLIICRNVMIYFTEEARVklYEKFSRALRKGGVLFVGS 237
Cdd:pfam13847  54 DNVEFEQgdiEELPELLEDDKFDVVISNCVLNHIPDPDKV--LQEILRVLKPGGRLIISD 111
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 181-235 2.93e-03

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 36.64  E-value: 2.93e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446505031 181 QNVTFKQHDLLMQSF--DTNYDLIICRNVMIYFtEEARVKLYEKFSRALRKGGVLFV 235
Cdd:cd02440   47 DNVEVLKGDAEELPPeaDESFDVIISDPPLHHL-VEDLARFLEEARRLLKPGGVLVL 102
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
183-247 8.79e-03

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 36.13  E-value: 8.79e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446505031 183 VTFKQHDLL-MQSFDTNYDLIICRNVMIYFteEARVKLYEKFSRALRKGGvLFVGSTEQILTPERY 247
Cdd:COG4976   91 DRLLVADLAdLAEPDGRFDLIVAADVLTYL--GDLAAVFAGVARALKPGG-LFIFSVEDADGSGRY 153
 
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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