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Conserved domains on  [gi|1308674808|gb|PKM46777|]
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chemotaxis protein CheR [Firmicutes bacterium HGW-Firmicutes-8]

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];
2-258 2.17e-98

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


:

Pssm-ID: 440963 [Multi-domain]  Cd Length: 272  Bit Score: 288.60  E-value: 2.17e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808   2 PDAYEKFLQDLRRRKGLDLTGYKRPQMERRINSLMRSLKVEGYDTYLDLMEKEIQHWLKFLDTLTINVSEFYRNPNQWEL 81
Cdd:COG1352     6 DAEFERLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPEELQALIDALTINVTEFFRDPEHFEA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808  82 LESKIIPELITK---TPFLKLWSAGCSTGEEPYSLAML---MINRFHKVSFTLTASDIDDEVINKAKAGVYNDKAVANLP 155
Cdd:COG1352    86 LREEVLPELLARrraGRPLRIWSAGCSTGEEPYSLAMLlaeAGGELAGWRVEILATDISEEALEKARAGIYPERSLRGLP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808 156 KQFLSLNFTQQGTNFVISEDVKRRVKYVKRNLLRDP-FDRSYDLILCRNVVIYFTEESKAELYRKFHDALRIGGILFTGS 234
Cdd:COG1352   166 PEYLSRYFTKEGGRYRIKPELREMVTFAQHNLLDDPpPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSLAPGGYLFLGH 245

                         250       260
                  ....*....|....*....|....*..
gi 1308674808 235 TEQIFQPREiGF---NLASSFFYRREG 258
Cdd:COG1352   246 SESLGGLSD-LFepvDKKGRFIYRKRA 271
 
Name Accession Description Interval E-value
CheR COG1352
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
2-258 2.17e-98

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


Pssm-ID: 440963 [Multi-domain]  Cd Length: 272  Bit Score: 288.60  E-value: 2.17e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808   2 PDAYEKFLQDLRRRKGLDLTGYKRPQMERRINSLMRSLKVEGYDTYLDLMEKEIQHWLKFLDTLTINVSEFYRNPNQWEL 81
Cdd:COG1352     6 DAEFERLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPEELQALIDALTINVTEFFRDPEHFEA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808  82 LESKIIPELITK---TPFLKLWSAGCSTGEEPYSLAML---MINRFHKVSFTLTASDIDDEVINKAKAGVYNDKAVANLP 155
Cdd:COG1352    86 LREEVLPELLARrraGRPLRIWSAGCSTGEEPYSLAMLlaeAGGELAGWRVEILATDISEEALEKARAGIYPERSLRGLP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808 156 KQFLSLNFTQQGTNFVISEDVKRRVKYVKRNLLRDP-FDRSYDLILCRNVVIYFTEESKAELYRKFHDALRIGGILFTGS 234
Cdd:COG1352   166 PEYLSRYFTKEGGRYRIKPELREMVTFAQHNLLDDPpPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSLAPGGYLFLGH 245

                         250       260
                  ....*....|....*....|....*..
gi 1308674808 235 TEQIFQPREiGF---NLASSFFYRREG 258
Cdd:COG1352   246 SESLGGLSD-LFepvDKKGRFIYRKRA 271
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
 2-241 9.00e-78

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: 236.03  E-value: 9.00e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808    2 PDAYEKFLQDLRRRKGLDLTGYKRPQMERRINSLMRSLKVEGYDTYLDLMEKE--IQHWLKFLDTLTINVSEFYRNPNQW 79
Cdd:smart00138   1 DADFRRFCVLIYSRTGIVLTDYKRTLLQSRLSRRLRVLGLKDFSEYLELLTSHrgEEELAELLDLMTTNETRFFRESKHF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808   80 ELLESKIIPELITKTPF---LKLWSAGCSTGEEPYSLAMLMINRFHKV---SFTLTASDIDDEVINKAKAGVYNDKAVAN 153
Cdd:smart00138  81 EALEEKVLPLLIASRRHgrrVRIWSAGCSTGEEPYSLAMLLAETLPKGrepDVKILATDIDLKALEKARAGIYPERELED 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808  154 LPKQFLSLNFTQQGTNFVISEDVKRRVKYVKRNLLRD-PFDRSYDLILCRNVVIYFTEESKAELYRKFHDALRIGGILFT 232
Cdd:smart00138 161 LPKALLARYFKEVEDKYRVKPELKERVRFAKHNLLAEsPPLGDFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGGYLFL 240


                   ....*....
gi 1308674808  233 GSTEQIFQP 241
Cdd:smart00138 241 GHSESLPGL 249
CheR pfam01739
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ...
 68-240 2.82e-55

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: 175.93  E-value: 2.82e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808  68 NVSEFYRNPNQWELLESKIIPELITKTPF--LKLWSAGCSTGEEPYSLAMLMINRFHKV---SFTLTASDIDDEVINKAK 142
Cdd:pfam01739   1 NETRFFREPAHFEELKKYVLPLLAKAKNGkrVRIWSAGCSSGEEPYSLAMLLKETFPNAarwDFKILATDIDLSVLEKAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808 143 AGVYNDKAVANLPKQFLSLNFTQQ-GTNFVISEDVKRRVKYVKRNLL-RDPFDRSYDLILCRNVVIYFTEESKAELYRKF 220
Cdd:pfam01739  81 AGVYPERELEGLPEELLRRYFEKTaGGGYTVKPEIKSMVLFEYLNLLdEYPPLGDFDVIFCRNVLIYFDEETQRKILNRF 160

                         170       180
                  ....*....|....*....|
gi 1308674808 221 HDALRIGGILFTGSTEQIFQ 240
Cdd:pfam01739 161 AEKLKPGGYLFLGHSEALPG 180
PRK10611 PRK10611
protein-glutamate O-methyltransferase CheR;
1-240 3.73e-33

protein-glutamate O-methyltransferase CheR;


Pssm-ID: 236725 [Multi-domain]  Cd Length: 287  Bit Score: 121.77  E-value: 3.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808   1 MPDA-YEKFLQDLRRRKGLDLTGYKRPQMERRINSLMRSLKVEGYDTYLDLMEKEIQ--HWLKFLDTLTINVSEFYRNPN 77
Cdd:PRK10611   22 LSDAhFRRICQLIYQRAGIVLADHKREMVYNRLVRRLRSLGLNDFGQYLALLESNQNsaEWQAFINALTTNLTAFFREAH 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808  78 QWELLESkiipELITKTPFLKLWSAGCSTGEEPYSLAMLMI----NRFHKvsFTLTASDIDDEVINKAKAGVYNDKAVAN 153
Cdd:PRK10611  102 HFPILAE----HARRRSGEYRVWSAAASTGEEPYSIAMTLAdtlgTAPGR--WKVFASDIDTEVLEKARSGIYRQEELKT 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808 154 LPKQFLSLNF-----TQQGTNFVISEdVKRRVKYVKRNLLRD--PFDRSYDLILCRNVVIYFTEESKAELYRKFHDALRI 226
Cdd:PRK10611  176 LSPQQLQRYFmrgtgPHEGLVRVRQE-LANYVDFQQLNLLAKqwAVPGPFDAIFCRNVMIYFDKTTQERILRRFVPLLKP 254

                         250
                  ....*....|....
gi 1308674808 227 GGILFTGSTEQIFQ 240
Cdd:PRK10611  255 DGLLFAGHSENFSQ 268
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 98-232 4.60e-06

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: 44.34  E-value: 4.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808  98 KLWSAGCSTGeepYSLAMLMINRFHKVsftlTASDIDDEVINKAKAGVYNDKAVanlpkqflslnftqqgtnfvisedvk 177
Cdd:cd02440     1 RVLDLGCGTG---ALALALASGPGARV----TGVDISPVALELARKAAAALLAD-------------------------- 47

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1308674808 178 rRVKYVKRNLLRDPF--DRSYDLILCrNVVIYFTEESKAELYRKFHDALRIGGILFT 232
Cdd:cd02440    48 -NVEVLKGDAEELPPeaDESFDVIIS-DPPLHHLVEDLARFLEEARRLLKPGGVLVL 102
 
Name Accession Description Interval E-value
CheR COG1352
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
2-258 2.17e-98

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


Pssm-ID: 440963 [Multi-domain]  Cd Length: 272  Bit Score: 288.60  E-value: 2.17e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808   2 PDAYEKFLQDLRRRKGLDLTGYKRPQMERRINSLMRSLKVEGYDTYLDLMEKEIQHWLKFLDTLTINVSEFYRNPNQWEL 81
Cdd:COG1352     6 DAEFERLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPEELQALIDALTINVTEFFRDPEHFEA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808  82 LESKIIPELITK---TPFLKLWSAGCSTGEEPYSLAML---MINRFHKVSFTLTASDIDDEVINKAKAGVYNDKAVANLP 155
Cdd:COG1352    86 LREEVLPELLARrraGRPLRIWSAGCSTGEEPYSLAMLlaeAGGELAGWRVEILATDISEEALEKARAGIYPERSLRGLP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808 156 KQFLSLNFTQQGTNFVISEDVKRRVKYVKRNLLRDP-FDRSYDLILCRNVVIYFTEESKAELYRKFHDALRIGGILFTGS 234
Cdd:COG1352   166 PEYLSRYFTKEGGRYRIKPELREMVTFAQHNLLDDPpPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSLAPGGYLFLGH 245

                         250       260
                  ....*....|....*....|....*..
gi 1308674808 235 TEQIFQPREiGF---NLASSFFYRREG 258
Cdd:COG1352   246 SESLGGLSD-LFepvDKKGRFIYRKRA 271
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
 2-241 9.00e-78

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: 236.03  E-value: 9.00e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808    2 PDAYEKFLQDLRRRKGLDLTGYKRPQMERRINSLMRSLKVEGYDTYLDLMEKE--IQHWLKFLDTLTINVSEFYRNPNQW 79
Cdd:smart00138   1 DADFRRFCVLIYSRTGIVLTDYKRTLLQSRLSRRLRVLGLKDFSEYLELLTSHrgEEELAELLDLMTTNETRFFRESKHF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808   80 ELLESKIIPELITKTPF---LKLWSAGCSTGEEPYSLAMLMINRFHKV---SFTLTASDIDDEVINKAKAGVYNDKAVAN 153
Cdd:smart00138  81 EALEEKVLPLLIASRRHgrrVRIWSAGCSTGEEPYSLAMLLAETLPKGrepDVKILATDIDLKALEKARAGIYPERELED 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808  154 LPKQFLSLNFTQQGTNFVISEDVKRRVKYVKRNLLRD-PFDRSYDLILCRNVVIYFTEESKAELYRKFHDALRIGGILFT 232
Cdd:smart00138 161 LPKALLARYFKEVEDKYRVKPELKERVRFAKHNLLAEsPPLGDFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGGYLFL 240


                   ....*....
gi 1308674808  233 GSTEQIFQP 241
Cdd:smart00138 241 GHSESLPGL 249
CheR pfam01739
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ...
 68-240 2.82e-55

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: 175.93  E-value: 2.82e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808  68 NVSEFYRNPNQWELLESKIIPELITKTPF--LKLWSAGCSTGEEPYSLAMLMINRFHKV---SFTLTASDIDDEVINKAK 142
Cdd:pfam01739   1 NETRFFREPAHFEELKKYVLPLLAKAKNGkrVRIWSAGCSSGEEPYSLAMLLKETFPNAarwDFKILATDIDLSVLEKAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808 143 AGVYNDKAVANLPKQFLSLNFTQQ-GTNFVISEDVKRRVKYVKRNLL-RDPFDRSYDLILCRNVVIYFTEESKAELYRKF 220
Cdd:pfam01739  81 AGVYPERELEGLPEELLRRYFEKTaGGGYTVKPEIKSMVLFEYLNLLdEYPPLGDFDVIFCRNVLIYFDEETQRKILNRF 160

                         170       180
                  ....*....|....*....|
gi 1308674808 221 HDALRIGGILFTGSTEQIFQ 240
Cdd:pfam01739 161 AEKLKPGGYLFLGHSEALPG 180
PRK10611 PRK10611
protein-glutamate O-methyltransferase CheR;
1-240 3.73e-33

protein-glutamate O-methyltransferase CheR;


Pssm-ID: 236725 [Multi-domain]  Cd Length: 287  Bit Score: 121.77  E-value: 3.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808   1 MPDA-YEKFLQDLRRRKGLDLTGYKRPQMERRINSLMRSLKVEGYDTYLDLMEKEIQ--HWLKFLDTLTINVSEFYRNPN 77
Cdd:PRK10611   22 LSDAhFRRICQLIYQRAGIVLADHKREMVYNRLVRRLRSLGLNDFGQYLALLESNQNsaEWQAFINALTTNLTAFFREAH 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808  78 QWELLESkiipELITKTPFLKLWSAGCSTGEEPYSLAMLMI----NRFHKvsFTLTASDIDDEVINKAKAGVYNDKAVAN 153
Cdd:PRK10611  102 HFPILAE----HARRRSGEYRVWSAAASTGEEPYSIAMTLAdtlgTAPGR--WKVFASDIDTEVLEKARSGIYRQEELKT 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808 154 LPKQFLSLNF-----TQQGTNFVISEdVKRRVKYVKRNLLRD--PFDRSYDLILCRNVVIYFTEESKAELYRKFHDALRI 226
Cdd:PRK10611  176 LSPQQLQRYFmrgtgPHEGLVRVRQE-LANYVDFQQLNLLAKqwAVPGPFDAIFCRNVMIYFDKTTQERILRRFVPLLKP 254

                         250
                  ....*....|....
gi 1308674808 227 GGILFTGSTEQIFQ 240
Cdd:PRK10611  255 DGLLFAGHSENFSQ 268
CheR_N pfam03705
CheR methyltransferase, all-alpha domain; CheR proteins are part of the chemotaxis signaling ...
 3-53 4.49e-12

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: 59.37  E-value: 4.49e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1308674808   3 DAYEKFLQDLRRRKGLDLTGYKRPQMERRINSLMRSLKVEGYDTYLDLMEK 53
Cdd:pfam03705   1 AEFERLLELIYRRTGIDLSDYKRSLLERRLSRRMRALGLDSFSEYLDLLRS 51
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 102-228 1.63e-07

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 48.33  E-value: 1.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808 102 AGCSTGeepySLAMLMINRFHkvsFTLTASDIDDEVINKAKAgvyndkavanlpkqflslNFTQQGTNfvisedvkrrVK 181
Cdd:pfam13649   4 LGCGTG----RLTLALARRGG---ARVTGVDLSPEMLERARE------------------RAAEAGLN----------VE 48

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1308674808 182 YVKRNLLRDPF-DRSYDLILCRNVVIYFTEESKAELYRKFHDALRIGG 228
Cdd:pfam13649  49 FVQGDAEDLPFpDGSFDLVVSSGVLHHLPDPDLEAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 102-231 4.24e-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: 45.01  E-value: 4.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808 102 AGCSTGEepysLAMLMINRFHKVsftlTASDIDDEVINKAKAgvyndkavaNLPKQflslnftqqgtnfvisedvkrRVK 181
Cdd:COG2227    31 VGCGTGR----LALALARRGADV----TGVDISPEALEIARE---------RAAEL---------------------NVD 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1308674808 182 YVKRNLLRDPF-DRSYDLILCRNVVIYFTEEskAELYRKFHDALRIGGILF 231
Cdd:COG2227    73 FVQGDLEDLPLeDGSFDLVICSEVLEHLPDP--AALLRELARLLKPGGLLL 121
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 98-232 4.60e-06

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: 44.34  E-value: 4.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808  98 KLWSAGCSTGeepYSLAMLMINRFHKVsftlTASDIDDEVINKAKAGVYNDKAVanlpkqflslnftqqgtnfvisedvk 177
Cdd:cd02440     1 RVLDLGCGTG---ALALALASGPGARV----TGVDISPVALELARKAAAALLAD-------------------------- 47

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1308674808 178 rRVKYVKRNLLRDPF--DRSYDLILCrNVVIYFTEESKAELYRKFHDALRIGGILFT 232
Cdd:cd02440    48 -NVEVLKGDAEELPPeaDESFDVIIS-DPPLHHLVEDLARFLEEARRLLKPGGVLVL 102
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 103-231 7.22e-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: 7.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808 103 GCSTGeepySLAMLMINRFHkvsFTLTASDIDDEVINKAKAgVYNDKAVANLpkQFLSLNFTQQGtnfvisedvkrrvky 182
Cdd:COG0500    34 GCGTG----RNLLALAARFG---GRVIGIDLSPEAIALARA-RAAKAGLGNV--EFLVADLAELD--------------- 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1308674808 183 vkrnllrDPFDRSYDLILCRNVVIYFTEESKAELYRKFHDALRIGGILF 231
Cdd:COG0500    89 -------PLPAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLL 130
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 89-231 2.01e-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: 40.36  E-value: 2.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808  89 ELITKTPFLKLWSAGCSTGEepysLAMLMINRFHKVsftlTASDIDDEVINKAKAgvyndkavanlpkqflslNFTQQGT 168
Cdd:COG2226    16 AALGLRPGARVLDLGCGTGR----LALALAERGARV----TGVDISPEMLELARE------------------RAAEAGL 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308674808 169 NfvisedvkrrVKYVKRNLLRDPF-DRSYDLILCRNVVIYFTEESKA--ELYRkfhdALRIGGILF 231
Cdd:COG2226    70 N----------VEFVVGDAEDLPFpDGSFDLVISSFVLHHLPDPERAlaEIAR----VLKPGGRLV 121
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 103-230 2.21e-04

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 39.27  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808 103 GCSTGeepySLAMLMINRFHKVSFTLTasDIDDEVINKAKagvyndkavanlpKQFLSLNFtqqgtnfviseDVKRRVKY 182
Cdd:pfam08242   4 GCGTG----TLLRALLEALPGLEYTGL--DISPAALEAAR-------------ERLAALGL-----------LNAVRVEL 53

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1308674808 183 VKRNLLrDPFDRSYDLILCRNVVIYFTEesKAELYRKFHDALRIGGIL 230
Cdd:pfam08242  54 FQLDLG-ELDPGSFDVVVASNVLHHLAD--PRAVLRNIRRLLKPGGVL 98
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 159-231 8.39e-04

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 38.76  E-value: 8.39e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308674808 159 LSLNFTQQGTNFVISEDVKRRVKYVKRNLLRDPFDRSYDLILCRNVVIYFTEESKAELYRKFHDALRIGGILF 231
Cdd:COG2230    82 LSPEQLEYARERAAEAGLADRVEVRLADYRDLPADGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLL 154
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 102-231 8.01e-03

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 34.95  E-value: 8.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308674808 102 AGCSTGEEPYSLAmlminrfhKVSFTLTASDIDDEVINKAKAgvyndkavanlpkqflslnftqqgtnfvisEDVKRRVK 181
Cdd:pfam08241   3 VGCGTGLLTELLA--------RLGARVTGVDISPEMLELARE------------------------------KAPREGLT 44

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1308674808 182 YVKRNLLRDPF-DRSYDLILCRNVVIYFTEESKA--ELYRkfhdALRIGGILF 231
Cdd:pfam08241  45 FVVGDAEDLPFpDNSFDLVLSSEVLHHVEDPERAlrEIAR----VLKPGGILI 93
 
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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