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Conserved domains on  [gi|490874173|ref|WP_004736174|]
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MULTISPECIES: protein-glutamate O-methyltransferase [Vibrio]

Protein Classification

protein-glutamate O-methyltransferase( domain architecture ID 12190911)

protein-glutamate O-methyltransferase such as CheR, which catalyzes methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
 8-272 3.29e-115

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: 331.56  E-value: 3.29e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173     8 DQEYRDFSRFLESQCGIVLGDSKQYLVRSRLSPLVTKFKLASLSDLLRDVVTGRNRELRVAAVDAMTTNETLWFRDTYPF 87
Cdd:smart00138   1 DADFRRFCVLIYSRTGIVLTDYKRTLLQSRLSRRLRVLGLKDFSEYLELLTSHRGEEELAELLDLMTTNETRFFRESKHF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173    88 AVLADKLLPEIAAN---KRPIKIWSAASSSGQEAYSMAMTILETQARkpGMLPNVSITATDISASMLDMCRTGAYDNLAL 164
Cdd:smart00138  81 EALEEKVLPLLIASrrhGRRVRIWSAGCSTGEEPYSLAMLLAETLPK--GREPDVKILATDIDLKALEKARAGIYPEREL 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173   165 gRGLSPERRRTFFEDaGDGRMKVKDNVKRMVNFRPQNLMDSYALLGKFDIIFCRNVLIYFSPDMKSKVLNQMANSLNPGG 244
Cdd:smart00138 159 -EDLPKALLARYFKE-VEDKYRVKPELKERVRFAKHNLLAESPPLGDFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGG 236

                          250       260
                   ....*....|....*....|....*...
gi 490874173   245 YLLLGASESLTGLTDRFEMVRCNPGIIY 272
Cdd:smart00138 237 YLFLGHSESLPGLTDKFEPIEGTVYFYS 264
 
Name Accession Description Interval E-value
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
 8-272 3.29e-115

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: 331.56  E-value: 3.29e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173     8 DQEYRDFSRFLESQCGIVLGDSKQYLVRSRLSPLVTKFKLASLSDLLRDVVTGRNRELRVAAVDAMTTNETLWFRDTYPF 87
Cdd:smart00138   1 DADFRRFCVLIYSRTGIVLTDYKRTLLQSRLSRRLRVLGLKDFSEYLELLTSHRGEEELAELLDLMTTNETRFFRESKHF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173    88 AVLADKLLPEIAAN---KRPIKIWSAASSSGQEAYSMAMTILETQARkpGMLPNVSITATDISASMLDMCRTGAYDNLAL 164
Cdd:smart00138  81 EALEEKVLPLLIASrrhGRRVRIWSAGCSTGEEPYSLAMLLAETLPK--GREPDVKILATDIDLKALEKARAGIYPEREL 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173   165 gRGLSPERRRTFFEDaGDGRMKVKDNVKRMVNFRPQNLMDSYALLGKFDIIFCRNVLIYFSPDMKSKVLNQMANSLNPGG 244
Cdd:smart00138 159 -EDLPKALLARYFKE-VEDKYRVKPELKERVRFAKHNLLAESPPLGDFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGG 236

                          250       260
                   ....*....|....*....|....*...
gi 490874173   245 YLLLGASESLTGLTDRFEMVRCNPGIIY 272
Cdd:smart00138 237 YLFLGHSESLPGLTDKFEPIEGTVYFYS 264
CheR COG1352
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
5-275 1.95e-114

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


Pssm-ID: 440963 [Multi-domain]  Cd Length: 272  Bit Score: 329.82  E-value: 1.95e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173   5 TISDQEYRDFSRFLESQCGIVLGDSKQYLVRSRLSPLVTKFKLASLSDLLRDVVtgRNRELRVAAVDAMTTNETLWFRDT 84
Cdd:COG1352    3 ELSDAEFERLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLR--SDPEELQALIDALTINVTEFFRDP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173  85 YPFAVLADKLLPEIAANK---RPIKIWSAASSSGQEAYSMAMTILETQARKPGmlPNVSITATDISASMLDMCRTGAYDN 161
Cdd:COG1352   81 EHFEALREEVLPELLARRragRPLRIWSAGCSTGEEPYSLAMLLAEAGGELAG--WRVEILATDISEEALEKARAGIYPE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173 162 LALgRGLSPERRRTFFEdAGDGRMKVKDNVKRMVNFRPQNLMDSYALLGKFDIIFCRNVLIYFSPDMKSKVLNQMANSLN 241
Cdd:COG1352  159 RSL-RGLPPEYLSRYFT-KEGGRYRIKPELREMVTFAQHNLLDDPPPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSLA 236

                        250       260       270
                 ....*....|....*....|....*....|....
gi 490874173 242 PGGYLLLGASESLTGLTDRFEMVRCNPGIIYKLK 275
Cdd:COG1352  237 PGGYLFLGHSESLGGLSDLFEPVDKKGRFIYRKR 270
CheR pfam01739
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ...
 76-264 9.85e-73

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: 221.00  E-value: 9.85e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173   76 NETLWFRDTYPFAVLADKLLPEIAANK--RPIKIWSAASSSGQEAYSMAMTILETQARKPGMLpnVSITATDISASMLDM 153
Cdd:pfam01739   1 NETRFFREPAHFEELKKYVLPLLAKAKngKRVRIWSAGCSSGEEPYSLAMLLKETFPNAARWD--FKILATDIDLSVLEK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173  154 CRTGAYDNLALgRGLSPERRRTFFEDAGDGRMKVKDNVKRMVNFRPQNLMDSYALLGKFDIIFCRNVLIYFSPDMKSKVL 233
Cdd:pfam01739  79 ARAGVYPEREL-EGLPEELLRRYFEKTAGGGYTVKPEIKSMVLFEYLNLLDEYPPLGDFDVIFCRNVLIYFDEETQRKIL 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 490874173  234 NQMANSLNPGGYLLLGASESLTGLTDRFEMV 264
Cdd:pfam01739 158 NRFAEKLKPGGYLFLGHSEALPGNPDKFKKV 188
PRK10611 PRK10611
protein-glutamate O-methyltransferase CheR;
4-261 1.01e-47

protein-glutamate O-methyltransferase CheR;


Pssm-ID: 236725 [Multi-domain]  Cd Length: 287  Bit Score: 160.29  E-value: 1.01e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173   4 ITISDQEYRDFSRFLESQCGIVLGDSKQYLVRSRLsplVTKFKLASLSDL---LRDVVTGRNRELRVAAVDAMTTNETLW 80
Cdd:PRK10611  20 LALSDAHFRRICQLIYQRAGIVLADHKREMVYNRL---VRRLRSLGLNDFgqyLALLESNQNSAEWQAFINALTTNLTAF 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173  81 FRDTYPFAVLADKllpeiaANKRP--IKIWSAASSSGQEAYSMAMTILETQARKPGmlpNVSITATDISASMLDMCRTGA 158
Cdd:PRK10611  97 FREAHHFPILAEH------ARRRSgeYRVWSAAASTGEEPYSIAMTLADTLGTAPG---RWKVFASDIDTEVLEKARSGI 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173 159 YDNLALgRGLSPE-RRRTFFEDAGD--GRMKVKDNVKRMVNFRPQNLMDS-YALLGKFDIIFCRNVLIYFSPDMKSKVLN 234
Cdd:PRK10611 168 YRQEEL-KTLSPQqLQRYFMRGTGPheGLVRVRQELANYVDFQQLNLLAKqWAVPGPFDAIFCRNVMIYFDKTTQERILR 246

                        250       260
                 ....*....|....*....|....*..
gi 490874173 235 QMANSLNPGGYLLLGASESLTGLTDRF 261
Cdd:PRK10611 247 RFVPLLKPDGLLFAGHSENFSQLSREF 273
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 137-248 2.16e-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: 37.02  E-value: 2.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173 137 PNVSITATDISASMLDMCRTGAYDNLALGrglsperrrtffedagdgrmkvkdnvkrmVNFRPQNLMD-SYALLGKFDII 215
Cdd:cd02440   20 PGARVTGVDISPVALELARKAAAALLADN-----------------------------VEVLKGDAEElPPEADESFDVI 70

                         90       100       110
                 ....*....|....*....|....*....|...
gi 490874173 216 FCRNVLIYFSPDMKsKVLNQMANSLNPGGYLLL 248
Cdd:cd02440   71 ISDPPLHHLVEDLA-RFLEEARRLLKPGGVLVL 102
 
Name Accession Description Interval E-value
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
 8-272 3.29e-115

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: 331.56  E-value: 3.29e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173     8 DQEYRDFSRFLESQCGIVLGDSKQYLVRSRLSPLVTKFKLASLSDLLRDVVTGRNRELRVAAVDAMTTNETLWFRDTYPF 87
Cdd:smart00138   1 DADFRRFCVLIYSRTGIVLTDYKRTLLQSRLSRRLRVLGLKDFSEYLELLTSHRGEEELAELLDLMTTNETRFFRESKHF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173    88 AVLADKLLPEIAAN---KRPIKIWSAASSSGQEAYSMAMTILETQARkpGMLPNVSITATDISASMLDMCRTGAYDNLAL 164
Cdd:smart00138  81 EALEEKVLPLLIASrrhGRRVRIWSAGCSTGEEPYSLAMLLAETLPK--GREPDVKILATDIDLKALEKARAGIYPEREL 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173   165 gRGLSPERRRTFFEDaGDGRMKVKDNVKRMVNFRPQNLMDSYALLGKFDIIFCRNVLIYFSPDMKSKVLNQMANSLNPGG 244
Cdd:smart00138 159 -EDLPKALLARYFKE-VEDKYRVKPELKERVRFAKHNLLAESPPLGDFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGG 236

                          250       260
                   ....*....|....*....|....*...
gi 490874173   245 YLLLGASESLTGLTDRFEMVRCNPGIIY 272
Cdd:smart00138 237 YLFLGHSESLPGLTDKFEPIEGTVYFYS 264
CheR COG1352
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
5-275 1.95e-114

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


Pssm-ID: 440963 [Multi-domain]  Cd Length: 272  Bit Score: 329.82  E-value: 1.95e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173   5 TISDQEYRDFSRFLESQCGIVLGDSKQYLVRSRLSPLVTKFKLASLSDLLRDVVtgRNRELRVAAVDAMTTNETLWFRDT 84
Cdd:COG1352    3 ELSDAEFERLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLR--SDPEELQALIDALTINVTEFFRDP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173  85 YPFAVLADKLLPEIAANK---RPIKIWSAASSSGQEAYSMAMTILETQARKPGmlPNVSITATDISASMLDMCRTGAYDN 161
Cdd:COG1352   81 EHFEALREEVLPELLARRragRPLRIWSAGCSTGEEPYSLAMLLAEAGGELAG--WRVEILATDISEEALEKARAGIYPE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173 162 LALgRGLSPERRRTFFEdAGDGRMKVKDNVKRMVNFRPQNLMDSYALLGKFDIIFCRNVLIYFSPDMKSKVLNQMANSLN 241
Cdd:COG1352  159 RSL-RGLPPEYLSRYFT-KEGGRYRIKPELREMVTFAQHNLLDDPPPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSLA 236

                        250       260       270
                 ....*....|....*....|....*....|....
gi 490874173 242 PGGYLLLGASESLTGLTDRFEMVRCNPGIIYKLK 275
Cdd:COG1352  237 PGGYLFLGHSESLGGLSDLFEPVDKKGRFIYRKR 270
CheR pfam01739
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ...
 76-264 9.85e-73

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: 221.00  E-value: 9.85e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173   76 NETLWFRDTYPFAVLADKLLPEIAANK--RPIKIWSAASSSGQEAYSMAMTILETQARKPGMLpnVSITATDISASMLDM 153
Cdd:pfam01739   1 NETRFFREPAHFEELKKYVLPLLAKAKngKRVRIWSAGCSSGEEPYSLAMLLKETFPNAARWD--FKILATDIDLSVLEK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173  154 CRTGAYDNLALgRGLSPERRRTFFEDAGDGRMKVKDNVKRMVNFRPQNLMDSYALLGKFDIIFCRNVLIYFSPDMKSKVL 233
Cdd:pfam01739  79 ARAGVYPEREL-EGLPEELLRRYFEKTAGGGYTVKPEIKSMVLFEYLNLLDEYPPLGDFDVIFCRNVLIYFDEETQRKIL 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 490874173  234 NQMANSLNPGGYLLLGASESLTGLTDRFEMV 264
Cdd:pfam01739 158 NRFAEKLKPGGYLFLGHSEALPGNPDKFKKV 188
PRK10611 PRK10611
protein-glutamate O-methyltransferase CheR;
4-261 1.01e-47

protein-glutamate O-methyltransferase CheR;


Pssm-ID: 236725 [Multi-domain]  Cd Length: 287  Bit Score: 160.29  E-value: 1.01e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173   4 ITISDQEYRDFSRFLESQCGIVLGDSKQYLVRSRLsplVTKFKLASLSDL---LRDVVTGRNRELRVAAVDAMTTNETLW 80
Cdd:PRK10611  20 LALSDAHFRRICQLIYQRAGIVLADHKREMVYNRL---VRRLRSLGLNDFgqyLALLESNQNSAEWQAFINALTTNLTAF 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173  81 FRDTYPFAVLADKllpeiaANKRP--IKIWSAASSSGQEAYSMAMTILETQARKPGmlpNVSITATDISASMLDMCRTGA 158
Cdd:PRK10611  97 FREAHHFPILAEH------ARRRSgeYRVWSAAASTGEEPYSIAMTLADTLGTAPG---RWKVFASDIDTEVLEKARSGI 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173 159 YDNLALgRGLSPE-RRRTFFEDAGD--GRMKVKDNVKRMVNFRPQNLMDS-YALLGKFDIIFCRNVLIYFSPDMKSKVLN 234
Cdd:PRK10611 168 YRQEEL-KTLSPQqLQRYFMRGTGPheGLVRVRQELANYVDFQQLNLLAKqWAVPGPFDAIFCRNVMIYFDKTTQERILR 246

                        250       260
                 ....*....|....*....|....*..
gi 490874173 235 QMANSLNPGGYLLLGASESLTGLTDRF 261
Cdd:PRK10611 247 RFVPLLKPDGLLFAGHSENFSQLSREF 273
CheR_N pfam03705
CheR methyltransferase, all-alpha domain; CheR proteins are part of the chemotaxis signaling ...
 9-55 1.86e-08

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: 49.74  E-value: 1.86e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 490874173    9 QEYRDFSRFLESQCGIVLGDSKQYLVRSRLSPLVTKFKLASLSDLLR 55
Cdd:pfam03705   1 AEFERLLELIYRRTGIDLSDYKRSLLERRLSRRMRALGLDSFSEYLD 47
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 138-244 2.34e-08

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 50.64  E-value: 2.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173  138 NVSITATDISASMLDMCRtgaydNLALGRGLSperrrtffedagdgrmkvkdnvkrmVNFRPQNLMDSYALLGKFDIIFC 217
Cdd:pfam13649  20 GARVTGVDLSPEMLERAR-----ERAAEAGLN-------------------------VEFVQGDAEDLPFPDGSFDLVVS 69

                          90       100
                  ....*....|....*....|....*..
gi 490874173  218 RNVLIYFSPDMKSKVLNQMANSLNPGG 244
Cdd:pfam13649  70 SGVLHHLPDPDLEAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 140-248 6.62e-07

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: 47.32  E-value: 6.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173 140 SITATDISASMLDMCRtgaydnlALGRGLSperrrtffedagdgrmkvkdnvkrmVNFRPQNLMDSYALLGKFDIIFCRN 219
Cdd:COG2227   48 DVTGVDISPEALEIAR-------ERAAELN-------------------------VDFVQGDLEDLPLEDGSFDLVICSE 95

                         90       100
                 ....*....|....*....|....*....
gi 490874173 220 VLIYFsPDMKsKVLNQMANSLNPGGYLLL 248
Cdd:COG2227   96 VLEHL-PDPA-ALLRELARLLKPGGLLLL 122
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
136-248 1.02e-06

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 45.97  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173 136 LPNVSITATDISASMLDMCRTgaydnlALGRglsperrrtffedagdgrmkvkdnvkrmVNFRPQNLMDsYALLGKFDII 215
Cdd:COG4106   23 FPGARVTGVDLSPEMLARARA------RLPN----------------------------VRFVVADLRD-LDPPEPFDLV 67

                         90       100       110
                 ....*....|....*....|....*....|...
gi 490874173 216 FCRNVLIYFsPDMKsKVLNQMANSLNPGGYLLL 248
Cdd:COG4106   68 VSNAALHWL-PDHA-ALLARLAAALAPGGVLAV 98
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 136-246 1.56e-06

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 45.44  E-value: 1.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173  136 LPNVSITATDISASMLDMCRTgaydNLALGRGLSPERRRTFFEDAGDGrmkvkdnvkrmvnfrpqnlmdsyaLLGKFDII 215
Cdd:pfam08242  18 LPGLEYTGLDISPAALEAARE----RLAALGLLNAVRVELFQLDLGEL------------------------DPGSFDVV 69

                          90       100       110
                  ....*....|....*....|....*....|.
gi 490874173  216 FCRNVLIYFspDMKSKVLNQMANSLNPGGYL 246
Cdd:pfam08242  70 VASNVLHHL--ADPRAVLRNIRRLLKPGGVL 98
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 142-251 2.50e-06

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 47.22  E-value: 2.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173 142 TATDISASMLDMCRtgaydNLALGRGLSPerrrtffedagdgrmkvkdnvkrmVNFRPQNLMDSYAL-LGKFDIIFCRNV 220
Cdd:COG0500   53 IGIDLSPEAIALAR-----ARAAKAGLGN------------------------VEFLVADLAELDPLpAESFDLVVAFGV 103

                         90       100       110
                 ....*....|....*....|....*....|.
gi 490874173 221 LIYFSPDMKSKVLNQMANSLNPGGYLLLGAS 251
Cdd:COG0500  104 LHHLPPEEREALLRELARALKPGGVLLLSAS 134
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
140-248 2.16e-05

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 43.83  E-value: 2.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173 140 SITATDISASMLDMCRT-GAYDNLALGRglsperrrtffedagdgrmkvkdnvkrMVNFRPQNlmdsyallGKFDIIFCR 218
Cdd:COG4976   70 RLTGVDLSEEMLAKAREkGVYDRLLVAD---------------------------LADLAEPD--------GRFDLIVAA 114

                         90       100       110
                 ....*....|....*....|....*....|
gi 490874173 219 NVLIYFsPDMKSkVLNQMANSLNPGGYLLL 248
Cdd:COG4976  115 DVLTYL-GDLAA-VFAGVARALKPGGLFIF 142
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 130-248 7.08e-05

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 42.22  E-value: 7.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173 130 ARKPGmlpnVSITATDISASMLDMCRtgaydNLALGRGLSpERRRTFFEDAGDgrmkvkdnvkrmvnFRPQnlmdsyall 209
Cdd:COG2230   70 ARRYG----VRVTGVTLSPEQLEYAR-----ERAAEAGLA-DRVEVRLADYRD--------------LPAD--------- 116

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 490874173 210 GKFDIIFCRNVLIYFSPDMKSKVLNQMANSLNPGGYLLL 248
Cdd:COG2230  117 GQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLL 155
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 211-248 6.65e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 39.32  E-value: 6.65e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 490874173  211 KFDIIFCRNVLIYFsPDmKSKVLNQMANSLNPGGYLLL 248
Cdd:pfam13847  74 KFDVVISNCVLNHI-PD-PDKVLQEILRVLKPGGRLII 109
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 138-248 1.15e-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: 38.44  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173 138 NVSITATDISASMLDMCRtgaydnlalgrglsperRRtfFEDAGDGrmkvkdnvkrmVNFRpqnLMDSYAL---LGKFDI 214
Cdd:COG2226   44 GARVTGVDISPEMLELAR-----------------ER--AAEAGLN-----------VEFV---VGDAEDLpfpDGSFDL 90

                         90       100       110
                 ....*....|....*....|....*....|....
gi 490874173 215 IFCRNVLIYFsPDmKSKVLNQMANSLNPGGYLLL 248
Cdd:COG2226   91 VISSFVLHHL-PD-PERALAEIARVLKPGGRLVV 122
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 137-248 2.16e-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: 37.02  E-value: 2.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874173 137 PNVSITATDISASMLDMCRTGAYDNLALGrglsperrrtffedagdgrmkvkdnvkrmVNFRPQNLMD-SYALLGKFDII 215
Cdd:cd02440   20 PGARVTGVDISPVALELARKAAAALLADN-----------------------------VEVLKGDAEElPPEADESFDVI 70

                         90       100       110
                 ....*....|....*....|....*....|...
gi 490874173 216 FCRNVLIYFSPDMKsKVLNQMANSLNPGGYLLL 248
Cdd:cd02440   71 ISDPPLHHLVEDLA-RFLEEARRLLKPGGVLVL 102
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
209-248 4.68e-03

tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;


Pssm-ID: 237898  Cd Length: 322  Bit Score: 37.92  E-value: 4.68e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 490874173 209 LGKFDIIFCRNVLiY--FSP-DMkskvLNQMANSLNPGGYLLL 248
Cdd:PRK15068 187 LKAFDTVFSMGVL-YhrRSPlDH----LKQLKDQLVPGGELVL 224
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 191-248 5.76e-03

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 36.64  E-value: 5.76e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 490874173  191 VKRMVNFRPQNLMDSYALLGKFDIIFCRNVLIYFsPDMkSKVLNQMANSLNPGGYLLL 248
Cdd:pfam13489  60 ALLNVRFDQFDEQEAAVPAGKFDVIVAREVLEHV-PDP-PALLRQIAALLKPGGLLLL 115
 
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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