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Conserved domains on  [gi|495378000|ref|WP_008102711|]
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MULTISPECIES: malonyl-ACP O-methyltransferase BioC [Pantoea]

Protein Classification

malonyl-ACP O-methyltransferase BioC( domain architecture ID 1007885)

malonyl-ACP O-methyltransferase BioC converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM)

EC:  2.1.1.197
Gene Ontology:  GO:0010340|GO:0009102|GO:1904047|GO:0032259|GO:0102130|GO:0008757

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10258 super family cl30595
biotin biosynthesis protein BioC; Provisional
 2-251 6.00e-116

biotin biosynthesis protein BioC; Provisional


The actual alignment was detected with superfamily member PRK10258:

Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 332.11  E-value: 6.00e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000   2 TLQVNKQAVANAFGRAAAHYEQHAQLQRLSGDALLALAPAGFGPHLLDAGCGTGWYSRYWRDRGRTLTALDLSPNMLQTA 81
Cdd:PRK10258   1 MATVNKQAIAAAFGRAAAHYEQHAELQRQSADALLAMLPQRKFTHVLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000  82 RDQQSAQHYLLGDIDEVPLPDASVDGVWSNLAVQWSSDLHTALLQLLRVTRPGGTVLFSTLLDGSLHEVHHAWAQLDGRQ 161
Cdd:PRK10258  81 RQKDAADHYLAGDIESLPLATATFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFTTLVQGSLPELHQAWQAVDERP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000 162 HANRFLSAAQFDAATATLPIAKQQQVITLHFPSALSAMRSLKGIGATHLHDGRGASVLTRAQLAQLEQHWPQDEAGYRLS 241
Cdd:PRK10258 161 HANRFLPPDAIEQALNGWRYQHHIQPITLWFDDALSAMRSLKGIGATHLHEGRDPRILTRSQLQRLQLAWPQQQGRYPLT 240

                        250
                 ....*....|
gi 495378000 242 YHLIYGVLSK 251
Cdd:PRK10258 241 YHLFLGVIER 250
 
Name Accession Description Interval E-value
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 2-251 6.00e-116

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 332.11  E-value: 6.00e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000   2 TLQVNKQAVANAFGRAAAHYEQHAQLQRLSGDALLALAPAGFGPHLLDAGCGTGWYSRYWRDRGRTLTALDLSPNMLQTA 81
Cdd:PRK10258   1 MATVNKQAIAAAFGRAAAHYEQHAELQRQSADALLAMLPQRKFTHVLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000  82 RDQQSAQHYLLGDIDEVPLPDASVDGVWSNLAVQWSSDLHTALLQLLRVTRPGGTVLFSTLLDGSLHEVHHAWAQLDGRQ 161
Cdd:PRK10258  81 RQKDAADHYLAGDIESLPLATATFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFTTLVQGSLPELHQAWQAVDERP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000 162 HANRFLSAAQFDAATATLPIAKQQQVITLHFPSALSAMRSLKGIGATHLHDGRGASVLTRAQLAQLEQHWPQDEAGYRLS 241
Cdd:PRK10258 161 HANRFLPPDAIEQALNGWRYQHHIQPITLWFDDALSAMRSLKGIGATHLHEGRDPRILTRSQLQRLQLAWPQQQGRYPLT 240

                        250
                 ....*....|
gi 495378000 242 YHLIYGVLSK 251
Cdd:PRK10258 241 YHLFLGVIER 250
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 13-251 2.27e-73

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 223.70  E-value: 2.27e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000   13 AFGRAAAHYEQHAQLQRLSGDALLALAPAG---FGPHLLDAGCGTGWYSRYWRDRGR--TLTALDLSPNMLQTARDQQSA 87
Cdd:TIGR02072   1 SFNKAAKTYDRHAKIQREMAKRLLALLKEKgifIPASVLDIGCGTGYLTRALLKRFPqaEFIALDISAGMLAQAKTKLSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000   88 Q-HYLLGDIDEVPLPDASVDGVWSNLAVQWSSDLHTALLQLLRVTRPGGTVLFSTLLDGSLHEVHHAWaqldgRQHANRF 166
Cdd:TIGR02072  81 NvQFICGDAEKLPLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSF-----GQHGLRY 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000  167 LSAAQFDAATATLP--IAKQQQVITLHFPSALSAMRSLKGIGATHLHDGRgasvLTRAQLAQLEQHWPQ--DEAGYRLSY 242
Cdd:TIGR02072 156 LSLDELKALLKNSFelLTLEEELITLSFDDPLDVLRHLKKTGANGLSSGR----TSRKQLKAFLERYEQefQPDGLPLTY 231


                  ....*....
gi 495378000  243 HLIYGVLSK 251
Cdd:TIGR02072 232 HVVYGIAKK 240
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 14-156 8.99e-32

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: 113.94  E-value: 8.99e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000  14 FGRAAAHYEQHaqlqrlsgDALLALAPAGFGPHLLDAGCGTGWYSRYWRDRGRTLTALDLSPNMLQTARDQQSAQ----H 89
Cdd:COG2226    1 FDRVAARYDGR--------EALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAglnvE 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495378000  90 YLLGDIDEVPLPDASVDGVWSNLAVQWSSDLHTALLQLLRVTRPGGTVLFSTLLDGSLHEVHHAWAQ 156
Cdd:COG2226   73 FVVGDAEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAE 139
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 48-139 2.18e-28

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 103.51  E-value: 2.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000   48 LDAGCGTGWYSRYWRDRGRTLTALDLSPNMLQTARD--QQSAQHYLLGDIDEVPLPDASVDGVWSNLAVQWSSDLHTALL 125
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREkaPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERALR 80

                          90
                  ....*....|....
gi 495378000  126 QLLRVTRPGGTVLF 139
Cdd:pfam08241  81 EIARVLKPGGILII 94
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 47-143 1.74e-13

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: 64.76  E-value: 1.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000  47 LLDAGCGTGWYSRYWRDR-GRTLTALDLSPNMLQTARDQQSAQ-----HYLLGDIDEVPL-PDASVDGVWSNLAVQWSSD 119
Cdd:cd02440    2 VLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAAALladnvEVLKGDAEELPPeADESFDVIISDPPLHHLVE 81

                         90       100
                 ....*....|....*....|....*
gi 495378000 120 LHTALL-QLLRVTRPGGTVLFSTLL 143
Cdd:cd02440   82 DLARFLeEARRLLKPGGVLVLTLVL 106
 
Name Accession Description Interval E-value
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 2-251 6.00e-116

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 332.11  E-value: 6.00e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000   2 TLQVNKQAVANAFGRAAAHYEQHAQLQRLSGDALLALAPAGFGPHLLDAGCGTGWYSRYWRDRGRTLTALDLSPNMLQTA 81
Cdd:PRK10258   1 MATVNKQAIAAAFGRAAAHYEQHAELQRQSADALLAMLPQRKFTHVLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000  82 RDQQSAQHYLLGDIDEVPLPDASVDGVWSNLAVQWSSDLHTALLQLLRVTRPGGTVLFSTLLDGSLHEVHHAWAQLDGRQ 161
Cdd:PRK10258  81 RQKDAADHYLAGDIESLPLATATFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFTTLVQGSLPELHQAWQAVDERP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000 162 HANRFLSAAQFDAATATLPIAKQQQVITLHFPSALSAMRSLKGIGATHLHDGRGASVLTRAQLAQLEQHWPQDEAGYRLS 241
Cdd:PRK10258 161 HANRFLPPDAIEQALNGWRYQHHIQPITLWFDDALSAMRSLKGIGATHLHEGRDPRILTRSQLQRLQLAWPQQQGRYPLT 240

                        250
                 ....*....|
gi 495378000 242 YHLIYGVLSK 251
Cdd:PRK10258 241 YHLFLGVIER 250
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 13-251 2.27e-73

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 223.70  E-value: 2.27e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000   13 AFGRAAAHYEQHAQLQRLSGDALLALAPAG---FGPHLLDAGCGTGWYSRYWRDRGR--TLTALDLSPNMLQTARDQQSA 87
Cdd:TIGR02072   1 SFNKAAKTYDRHAKIQREMAKRLLALLKEKgifIPASVLDIGCGTGYLTRALLKRFPqaEFIALDISAGMLAQAKTKLSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000   88 Q-HYLLGDIDEVPLPDASVDGVWSNLAVQWSSDLHTALLQLLRVTRPGGTVLFSTLLDGSLHEVHHAWaqldgRQHANRF 166
Cdd:TIGR02072  81 NvQFICGDAEKLPLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSF-----GQHGLRY 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000  167 LSAAQFDAATATLP--IAKQQQVITLHFPSALSAMRSLKGIGATHLHDGRgasvLTRAQLAQLEQHWPQ--DEAGYRLSY 242
Cdd:TIGR02072 156 LSLDELKALLKNSFelLTLEEELITLSFDDPLDVLRHLKKTGANGLSSGR----TSRKQLKAFLERYEQefQPDGLPLTY 231


                  ....*....
gi 495378000  243 HLIYGVLSK 251
Cdd:TIGR02072 232 HVVYGIAKK 240
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 14-156 8.99e-32

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: 113.94  E-value: 8.99e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000  14 FGRAAAHYEQHaqlqrlsgDALLALAPAGFGPHLLDAGCGTGWYSRYWRDRGRTLTALDLSPNMLQTARDQQSAQ----H 89
Cdd:COG2226    1 FDRVAARYDGR--------EALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAglnvE 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495378000  90 YLLGDIDEVPLPDASVDGVWSNLAVQWSSDLHTALLQLLRVTRPGGTVLFSTLLDGSLHEVHHAWAQ 156
Cdd:COG2226   73 FVVGDAEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAE 139
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 48-139 2.18e-28

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 103.51  E-value: 2.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000   48 LDAGCGTGWYSRYWRDRGRTLTALDLSPNMLQTARD--QQSAQHYLLGDIDEVPLPDASVDGVWSNLAVQWSSDLHTALL 125
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREkaPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERALR 80

                          90
                  ....*....|....
gi 495378000  126 QLLRVTRPGGTVLF 139
Cdd:pfam08241  81 EIARVLKPGGILII 94
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
10-173 4.55e-24

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 95.07  E-value: 4.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000  10 VANAFGRAAAHYEQH-------AQLQRLSGDALLALAPAGFGpHLLDAGCGTGWYSRYWRDRGRTLTALDLSPNMLQTAR 82
Cdd:COG4976    7 VEALFDQYADSYDAAlvedlgyEAPALLAEELLARLPPGPFG-RVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000  83 DQQSAQHYLLGDIDEVPLPDASVDGVWSNLAVQWSSDLHTALLQLLRVTRPGGTVLFST-LLDGSLHEVHHawaqldgRQ 161
Cdd:COG4976   86 EKGVYDRLLVADLADLAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSVeDADGSGRYAHS-------LD 158

                        170
                 ....*....|..
gi 495378000 162 HANRFLSAAQFD 173
Cdd:COG4976  159 YVRDLLAAAGFE 170
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 44-141 1.45e-22

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: 89.31  E-value: 1.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000  44 GPHLLDAGCGTGWYSRYWRDRGRTLTALDLSPNMLQTARDQQSAQ--HYLLGDIDEVPLPDASVDGVWSNLAVQWSSDLH 121
Cdd:COG2227   25 GGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELnvDFVQGDLEDLPLEDGSFDLVICSEVLEHLPDPA 104

                         90       100
                 ....*....|....*....|
gi 495378000 122 TALLQLLRVTRPGGTVLFST 141
Cdd:COG2227  105 ALLRELARLLKPGGLLLLST 124
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 48-135 3.88e-22

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 87.23  E-value: 3.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000   48 LDAGCGTGWYSRYWRDR-GRTLTALDLSPNMLQTARDQQSAQ----HYLLGDIDEVPLPDASVDGVWSNLAVQ--WSSDL 120
Cdd:pfam13649   2 LDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAglnvEFVQGDAEDLPFPDGSFDLVVSSGVLHhlPDPDL 81

                          90
                  ....*....|....*
gi 495378000  121 HTALLQLLRVTRPGG 135
Cdd:pfam13649  82 EAALREIARVLKPGG 96
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
44-141 4.09e-21

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 84.88  E-value: 4.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000  44 GPHLLDAGCGTGWYSRYWRDR--GRTLTALDLSPNMLQTARDQQSAQHYLLGDIDEVPlPDASVDGVWSNLAVQWSSDLH 121
Cdd:COG4106    2 PRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARARARLPNVRFVVADLRDLD-PPEPFDLVVSNAALHWLPDHA 80

                         90       100
                 ....*....|....*....|
gi 495378000 122 TALLQLLRVTRPGGTVLFST 141
Cdd:COG4106   81 ALLARLAAALAPGGVLAVQV 100
PRK08317 PRK08317
hypothetical protein; Provisional
 34-138 1.29e-13

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 68.04  E-value: 1.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000  34 ALLALAPagfGPHLLDAGCGTGWYSRYWRDR----GRtLTALDLSPNMLQTARDQQSAQH----YLLGDIDEVPLPDASV 105
Cdd:PRK08317  13 ELLAVQP---GDRVLDVGCGPGNDARELARRvgpeGR-VVGIDRSEAMLALAKERAAGLGpnveFVRGDADGLPFPDGSF 88

                         90       100       110
                 ....*....|....*....|....*....|...
gi 495378000 106 DGVWSNLAVQWSSDLHTALLQLLRVTRPGGTVL 138
Cdd:PRK08317  89 DAVRSDRVLQHLEDPARALAEIARVLRPGGRVV 121
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 47-143 1.74e-13

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: 64.76  E-value: 1.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000  47 LLDAGCGTGWYSRYWRDR-GRTLTALDLSPNMLQTARDQQSAQ-----HYLLGDIDEVPL-PDASVDGVWSNLAVQWSSD 119
Cdd:cd02440    2 VLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAAALladnvEVLKGDAEELPPeADESFDVIISDPPLHHLVE 81

                         90       100
                 ....*....|....*....|....*
gi 495378000 120 LHTALL-QLLRVTRPGGTVLFSTLL 143
Cdd:cd02440   82 DLARFLeEARRLLKPGGVLVLTLVL 106
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 1-141 7.57e-13

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 65.94  E-value: 7.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000   1 MTLQVNKQAVANAFGRAAAHYEQ-----HAQLQRLSGDALLALAPAGFGPHLLDAGCGTGWYSRYWRDRGRT---LTALD 72
Cdd:PRK00216   4 VAEEEKQEKVAEMFDSIAPKYDLmndllSFGLHRVWRRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKtgeVVGLD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000  73 LSPNMLQTARDQQSAQ------HYLLGDIDEVPLPDASVDGVwS------NLavqwsSDLHTALLQLLRVTRPGGTVL-- 138
Cdd:PRK00216  84 FSEGMLAVGREKLRDLglsgnvEFVQGDAEALPFPDNSFDAV-TiafglrNV-----PDIDKALREMYRVLKPGGRLVil 157


                 ....
gi 495378000 139 -FST 141
Cdd:PRK00216 158 eFSK 161
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 25-141 2.71e-11

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 59.94  E-value: 2.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000  25 AQLQRLsgDALLALAPAGFGPHLLDAGCGTGWYSRYW-RDRGRTLTALDLSPNMLQTARDQQSAQ------HYLLGDIDE 97
Cdd:COG2230   35 AQEAKL--DLILRKLGLKPGMRVLDIGCGWGGLALYLaRRYGVRVTGVTLSPEQLEYARERAAEAgladrvEVRLADYRD 112

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 495378000  98 VPlPDASVDGVWSNLAVQWSSDLH--TALLQLLRVTRPGGTVLFST 141
Cdd:COG2230  113 LP-ADGQFDAIVSIGMFEHVGPENypAYFAKVARLLKPGGRLLLHT 157
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 34-164 1.44e-09

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 56.08  E-value: 1.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000  34 ALLALAPAGFgpHLLDAGCGTGWYSRYWRDR-GRTLTALDLSPNMLQTARDQQSAQ-----HYLLGDIDE-VPLPDASVD 106
Cdd:COG0500   19 ALLERLPKGG--RVLDLGCGTGRNLLALAARfGGRVIGIDLSPEAIALARARAAKAglgnvEFLVADLAElDPLPAESFD 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495378000 107 GVWSNLAVQW-SSDLHTALLQLL-RVTRPGGTVLFS---TLLDGSLHEVHHAWAQLDGRQHAN 164
Cdd:COG0500   97 LVVAFGVLHHlPPEEREALLRELaRALKPGGVLLLSasdAAAALSLARLLLLATASLLELLLL 159
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 46-141 6.87e-09

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 53.19  E-value: 6.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000   46 HLLDAGCGTGWYSRYWRDRGR---TLTALDLSPNMLQTARdQQSAQHYL------LGDIDEVP--LPDASVDGVWSNLAV 114
Cdd:pfam13847   6 RVLDLGCGTGHLSFELAEELGpnaEVVGIDISEEAIEKAR-ENAQKLGFdnvefeQGDIEELPelLEDDKFDVVISNCVL 84

                          90       100
                  ....*....|....*....|....*..
gi 495378000  115 QWSSDLHTALLQLLRVTRPGGTVLFST 141
Cdd:pfam13847  85 NHIPDPDKVLQEILRVLKPGGRLIISD 111
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 48-137 1.30e-08

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 51.21  E-value: 1.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000   48 LDAGCGTGWYSRYWRD--RGRTLTALDLSPNMLQTARDQQSAQHYLLGDIDEVPLPDA------SVDGVWSNLAVQWSSD 119
Cdd:pfam08242   1 LEIGCGTGTLLRALLEalPGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLgeldpgSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*...
gi 495378000  120 LHTALLQLLRVTRPGGTV 137
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
arsM PRK11873
arsenite methyltransferase;
25-140 1.54e-08

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 53.80  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000  25 AQLQRLSGDALLALA---PAGF-----GPHLLDAGCGTGW----YSRYWRDRGRTLtALDLSPNMLQTARDQQSAQHY-- 90
Cdd:PRK11873  51 EELAAVPEGANLGLGcgnPTALaelkpGETVLDLGSGGGFdcflAARRVGPTGKVI-GVDMTPEMLAKARANARKAGYtn 129

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 495378000  91 ---LLGDIDEVPLPDASVDGVWSNLAVQWSSDLHTALLQLLRVTRPGGTVLFS 140
Cdd:PRK11873 130 vefRLGEIEALPVADNSVDVIISNCVINLSPDKERVFKEAFRVLKPGGRFAIS 182
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 24-166 3.73e-08

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 51.27  E-value: 3.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000   24 HAQLQRLSGDALLALAPAGF-GPHLLDAGCGTGWYSRYWRDRGRTLTALDLSPNMLQTARDQQSAQHYllgDIDEVPLPD 102
Cdd:pfam13489   2 AHQRERLLADLLLRLLPKLPsPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRFDQF---DEQEAAVPA 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495378000  103 ASVDGVWSNLAVQWSSDLHTALLQLLRVTRPGGTVLFSTLL--DGSLHEVHHAWAQLDGRQHANRF 166
Cdd:pfam13489  79 GKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLasDEADRLLLEWPYLRPRNGHISLF 144
PLN02244 PLN02244
tocopherol O-methyltransferase
 48-141 1.74e-06

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 48.20  E-value: 1.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000  48 LDAGCGTGWYSRYW-RDRGRTLTALDLSPNMLQTARDQQSAQ------HYLLGDIDEVPLPDASVDGVWSNLAVQWSSDL 120
Cdd:PLN02244 123 VDVGCGIGGSSRYLaRKYGANVKGITLSPVQAARANALAAAQglsdkvSFQVADALNQPFEDGQFDLVWSMESGEHMPDK 202

                         90       100
                 ....*....|....*....|.
gi 495378000 121 HTALLQLLRVTRPGGTVLFST 141
Cdd:PLN02244 203 RKFVQELARVAAPGGRIIIVT 223
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 35-139 4.46e-06

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 46.61  E-value: 4.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000  35 LLALAPAGFGPHLLDAGCGTGWYSRYWRDR--GRTLTALDLSPNMLQTARDQqsAQHYLLGDI-DEVPLPDasVDGVWSN 111
Cdd:PRK14103  21 LLARVGAERARRVVDLGCGPGNLTRYLARRwpGAVIEALDSSPEMVAAARER--GVDARTGDVrDWKPKPD--TDVVVSN 96

                         90       100       110
                 ....*....|....*....|....*....|.
gi 495378000 112 LAVQW---SSDLHTALLQLLrvtRPGGTVLF 139
Cdd:PRK14103  97 AALQWvpeHADLLVRWVDEL---APGSWIAV 124
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 35-136 8.81e-06

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 45.70  E-value: 8.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000  35 LLALAPAGFGPHLLDAGCGTGWYSRYWRDR--GRTLTALDLSPNMLQTARDQQSAQHYLLGDIDEVpLPDASVDGVWSNL 112
Cdd:PRK01683  23 LLARVPLENPRYVVDLGCGPGNSTELLVERwpAARITGIDSSPAMLAEARSRLPDCQFVEADIASW-QPPQALDLIFANA 101

                         90       100
                 ....*....|....*....|....*
gi 495378000 113 AVQWSSDlHTALLQ-LLRVTRPGGT 136
Cdd:PRK01683 102 SLQWLPD-HLELFPrLVSLLAPGGV 125
BchM-ChlM TIGR02021
magnesium protoporphyrin O-methyltransferase; This model represents the ...
 44-89 1.20e-05

magnesium protoporphyrin O-methyltransferase; This model represents the S-adenosylmethionine-dependent O-methyltransferase responsible for methylation of magnesium protoporphyrin IX. This step is essentiasl for the biosynthesis of both chlorophyll and bacteriochlorophyll. This model encompasses two closely related clades, from cyanobacteria (and plants) where it is called ChlM and other photosynthetic bacteria where it is known as BchM. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273930 [Multi-domain]  Cd Length: 219  Bit Score: 45.17  E-value: 1.20e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 495378000   44 GPHLLDAGCGTGWYSRYWRDRGRTLTALDLSPNMLQTARDQQSAQH 89
Cdd:TIGR02021  56 GKRVLDAGCGTGLLSIELAKRGAIVKAVDISEQMVQMARNRAQGRD 101
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 34-141 2.33e-04

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 40.70  E-value: 2.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000  34 ALLALAPAGFGPHLLDAGCGTG-------WysrywrdRGRTLTALDLSPNMLQTAR------DQQSAqHYLLGDIDEVPL 100
Cdd:COG1041   17 ALVNLAGAKEGDTVLDPFCGTGtilieagL-------LGRRVIGSDIDPKMVEGARenlehyGYEDA-DVIRGDARDLPL 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 495378000 101 PDASVDGVWSNL----AVQWSSDLHTALLQ-----LLRVTRPGGTVLFST 141
Cdd:COG1041   89 ADESVDAIVTDPpygrSSKISGEELLELYEkaleeAARVLKPGGRVVIVT 138
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 34-139 3.64e-04

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 40.17  E-value: 3.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000  34 ALLALAPAGFGPHLLDAGCGTGWYSRY--WRDRGRTLTALDLSPNMLQTARdqQSAQHYLLGDIDEV------PLPDASV 105
Cdd:COG2813   40 LLLEHLPEPLGGRVLDLGCGYGVIGLAlaKRNPEARVTLVDVNARAVELAR--ANAAANGLENVEVLwsdglsGVPDGSF 117

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 495378000 106 DGVWSN--LAVQWSSDLHTA---LLQLLRVTRPGGTVLF 139
Cdd:COG2813  118 DLILSNppFHAGRAVDKEVAhalIADAARHLRPGGELWL 156
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
33-135 9.06e-04

tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;


Pssm-ID: 182918  Cd Length: 255  Bit Score: 39.56  E-value: 9.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000  33 DALLALAPAGfgP-HLLDAGCGTGWYSRYWRDRGRTLTALDLSPNMLQTARdQQSAQHYLLGDIDEVPLP--------DA 103
Cdd:PRK11036  35 DRLLAELPPR--PlRVLDAGGGEGQTAIKLAELGHQVILCDLSAEMIQRAK-QAAEAKGVSDNMQFIHCAaqdiaqhlET 111

                         90       100       110
                 ....*....|....*....|....*....|..
gi 495378000 104 SVDGVWSNLAVQWSSDLHTALLQLLRVTRPGG 135
Cdd:PRK11036 112 PVDLILFHAVLEWVADPKSVLQTLWSVLRPGG 143
PRK05785 PRK05785
hypothetical protein; Provisional
 47-132 9.79e-04

hypothetical protein; Provisional


Pssm-ID: 235607 [Multi-domain]  Cd Length: 226  Bit Score: 39.29  E-value: 9.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000  47 LLDAGCGTGWYSRYWRD-RGRTLTALDLSPNMLQTArdqQSAQHYLLGDIDEVPLPDASVDGVWSNLAVQWSSDLHTALL 125
Cdd:PRK05785  55 VLDVAAGKGELSYHFKKvFKYYVVALDYAENMLKMN---LVADDKVVGSFEALPFRDKSFDVVMSSFALHASDNIEKVIA 131


                 ....*..
gi 495378000 126 QLLRVTR 132
Cdd:PRK05785 132 EFTRVSR 138
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 44-98 1.47e-03

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 38.66  E-value: 1.47e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495378000  44 GPHLLDAGCGTGWYSRYWRDRGRTLTALDLSPNMLQTARDQQSAQH------YLLGDIDEV 98
Cdd:PRK07580  64 GLRILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGlagnitFEVGDLESL 124
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 20-111 5.68e-03

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 37.05  E-value: 5.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495378000  20 HYEQHAQLQRLSGDALL--ALAPAGFGPHLLDAGCGTG-----WYSRYwrdRGRTLTALDLSPNMLQTARdqQSAQ---- 88
Cdd:COG4123   12 RIIQPRCGYRFGTDAVLlaAFAPVKKGGRVLDLGTGTGvialmLAQRS---PGARITGVEIQPEAAELAR--RNVAlngl 86

                         90       100
                 ....*....|....*....|....*....
gi 495378000  89 ----HYLLGDIDEVP--LPDASVDGVWSN 111
Cdd:COG4123   87 edriTVIHGDLKEFAaeLPPGSFDLVVSN 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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