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Conserved domains on  [gi|29338752|gb|AAO76552|]
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putative biotin synthesis protein bioC [Bacteroides thetaiotaomicron VPI-5482]

Protein Classification

malonyl-ACP O-methyltransferase( domain architecture ID 11493568)

malonyl-[acyl-carrier protein] O-methyltransferase BioC is a class I SAM-dependent methyltransferase in the biotin biosynthesis pathway that converts the free carboxyl group of a malonyl-thioester to its methyl ester using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 9-258 7.72e-98

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: 286.11  E-value: 7.72e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752     9 RFSKAISTYPREANVQRQIANKMIRLLQKHIPSPCPKVIEFGCGTGIYSRMLLRTLRPEELLLNDLCPEMRYCCEDLLRE 88
Cdd:TIGR02072   1 SFNKAAKTYDRHAKIQREMAKRLLALLKEKGIFIPASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752    89 kQVSFLSGDAETISFPDKS-TLITSCSALQWFDSPEEFFKRCNTLLHSQGYFAFSTFGKKNMKEIRELTG-KGLPYRSRE 166
Cdd:TIGR02072  81 -NVQFICGDAEKLPLEDSSfDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFGqHGLRYLSLD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752   167 ELEAALSLHFDILYSEEELIPLSFEDPMKVLYHLKQTGVNGLSAQSslypkhekqtWTRRDLQHFCERYTQEFtQGTSVS 246
Cdd:TIGR02072 160 ELKALLKNSFELLTLEEELITLSFDDPLDVLRHLKKTGANGLSSGR----------TSRKQLKAFLERYEQEF-QPDGLP 228

                         250
                  ....*....|..
gi 29338752   247 LTYHPIYIIAKK 258
Cdd:TIGR02072 229 LTYHVVYGIAKK 240
 
Name Accession Description Interval E-value
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 9-258 7.72e-98

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: 286.11  E-value: 7.72e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752     9 RFSKAISTYPREANVQRQIANKMIRLLQKHIPSPCPKVIEFGCGTGIYSRMLLRTLRPEELLLNDLCPEMRYCCEDLLRE 88
Cdd:TIGR02072   1 SFNKAAKTYDRHAKIQREMAKRLLALLKEKGIFIPASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752    89 kQVSFLSGDAETISFPDKS-TLITSCSALQWFDSPEEFFKRCNTLLHSQGYFAFSTFGKKNMKEIRELTG-KGLPYRSRE 166
Cdd:TIGR02072  81 -NVQFICGDAEKLPLEDSSfDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFGqHGLRYLSLD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752   167 ELEAALSLHFDILYSEEELIPLSFEDPMKVLYHLKQTGVNGLSAQSslypkhekqtWTRRDLQHFCERYTQEFtQGTSVS 246
Cdd:TIGR02072 160 ELKALLKNSFELLTLEEELITLSFDDPLDVLRHLKKTGANGLSSGR----------TSRKQLKAFLERYEQEF-QPDGLP 228

                         250
                  ....*....|..
gi 29338752   247 LTYHPIYIIAKK 258
Cdd:TIGR02072 229 LTYHVVYGIAKK 240
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 47-141 8.98e-19

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 78.48  E-value: 8.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752    47 IEFGCGTGIYSRMLLRtlRPEELLLNDLCPEMRYCCEDLLREKQVSFLSGDAETISFPDKS-TLITSCSALQWFDSPEEF 125
Cdd:pfam08241   1 LDVGCGTGLLTELLAR--LGARVTGVDISPEMLELAREKAPREGLTFVVGDAEDLPFPDNSfDLVLSSEVLHHVEDPERA 78

                          90
                  ....*....|....*.
gi 29338752   126 FKRCNTLLHSQGYFAF 141
Cdd:pfam08241  79 LREIARVLKPGGILII 94
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
42-143 1.40e-18

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 78.33  E-value: 1.40e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752  42 PCPKVIEFGCGTGIYSRMLLRTLRPEELLLNDLCPEMRycceDLLREK--QVSFLSGDAETISFPDKSTLITSCSALQWF 119
Cdd:COG4106   1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEML----ARARARlpNVRFVVADLRDLDPPEPFDLVVSNAALHWL 76

                        90       100
                ....*....|....*....|....
gi 29338752 120 DSPEEFFKRCNTLLHSQGYFAFST 143
Cdd:COG4106  77 PDHAALLARLAAALAPGGVLAVQV 100
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 2-250 3.11e-13

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 67.48  E-value: 3.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752    2 NKTIIAERFSKAISTYPREANVQRQIANKMIRLLQKHipsPCPKVIEFGCGTGIYSRMLLRtlRPEELLLNDLCPEMRyc 81
Cdd:PRK10258   5 NKQAIAAAFGRAAAHYEQHAELQRQSADALLAMLPQR---KFTHVLDAGCGPGWMSRYWRE--RGSQVTALDLSPPML-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752   82 ceDLLREKQVS--FLSGDAETISFPDKS-TLITSCSALQWFDSPEEFFKRCNTLLHSQGYFAFSTFGKKNMKEIREL--- 155
Cdd:PRK10258  78 --AQARQKDAAdhYLAGDIESLPLATATfDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFTTLVQGSLPELHQAwqa 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752  156 ---TGKGLPYRSREELEAALS-LHFdilYSEEELIPLSFEDPMKVLYHLKqtgvnGLSAqSSLYPKHEKQTWTRRDLQHF 231
Cdd:PRK10258 156 vdeRPHANRFLPPDAIEQALNgWRY---QHHIQPITLWFDDALSAMRSLK-----GIGA-THLHEGRDPRILTRSQLQRL 226

                        250
                 ....*....|....*....
gi 29338752  232 CERYTQEftQGTsVSLTYH 250
Cdd:PRK10258 227 QLAWPQQ--QGR-YPLTYH 242
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 45-144 1.28e-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: 45.88  E-value: 1.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752  45 KVIEFGCGTGIYSRMLLRTLrPEELLLNDLCPEMRYCCE---DLLREKQVSFLSGDAETISFPDKST--LITSCSALQWF 119
Cdd:cd02440   1 RVLDLGCGTGALALALASGP-GARVTGVDISPVALELARkaaAALLADNVEVLKGDAEELPPEADESfdVIISDPPLHHL 79

                        90       100
                ....*....|....*....|....*.
gi 29338752 120 -DSPEEFFKRCNTLLHSQGYFAFSTF 144
Cdd:cd02440  80 vEDLARFLEEARRLLKPGGVLVLTLV 105
 
Name Accession Description Interval E-value
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 9-258 7.72e-98

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: 286.11  E-value: 7.72e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752     9 RFSKAISTYPREANVQRQIANKMIRLLQKHIPSPCPKVIEFGCGTGIYSRMLLRTLRPEELLLNDLCPEMRYCCEDLLRE 88
Cdd:TIGR02072   1 SFNKAAKTYDRHAKIQREMAKRLLALLKEKGIFIPASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752    89 kQVSFLSGDAETISFPDKS-TLITSCSALQWFDSPEEFFKRCNTLLHSQGYFAFSTFGKKNMKEIRELTG-KGLPYRSRE 166
Cdd:TIGR02072  81 -NVQFICGDAEKLPLEDSSfDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFGqHGLRYLSLD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752   167 ELEAALSLHFDILYSEEELIPLSFEDPMKVLYHLKQTGVNGLSAQSslypkhekqtWTRRDLQHFCERYTQEFtQGTSVS 246
Cdd:TIGR02072 160 ELKALLKNSFELLTLEEELITLSFDDPLDVLRHLKKTGANGLSSGR----------TSRKQLKAFLERYEQEF-QPDGLP 228

                         250
                  ....*....|..
gi 29338752   247 LTYHPIYIIAKK 258
Cdd:TIGR02072 229 LTYHVVYGIAKK 240
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 47-141 8.98e-19

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 78.48  E-value: 8.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752    47 IEFGCGTGIYSRMLLRtlRPEELLLNDLCPEMRYCCEDLLREKQVSFLSGDAETISFPDKS-TLITSCSALQWFDSPEEF 125
Cdd:pfam08241   1 LDVGCGTGLLTELLAR--LGARVTGVDISPEMLELAREKAPREGLTFVVGDAEDLPFPDNSfDLVLSSEVLHHVEDPERA 78

                          90
                  ....*....|....*.
gi 29338752   126 FKRCNTLLHSQGYFAF 141
Cdd:pfam08241  79 LREIARVLKPGGILII 94
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
42-143 1.40e-18

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 78.33  E-value: 1.40e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752  42 PCPKVIEFGCGTGIYSRMLLRTLRPEELLLNDLCPEMRycceDLLREK--QVSFLSGDAETISFPDKSTLITSCSALQWF 119
Cdd:COG4106   1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEML----ARARARlpNVRFVVADLRDLDPPEPFDLVVSNAALHWL 76

                        90       100
                ....*....|....*....|....
gi 29338752 120 DSPEEFFKRCNTLLHSQGYFAFST 143
Cdd:COG4106  77 PDHAALLARLAAALAPGGVLAVQV 100
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 33-155 3.65e-17

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: 75.80  E-value: 3.65e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752  33 RLLQKHIPSPCPKVIEFGCGTGIYSRMLLRtlRPEELLLNDLCPEMRYCCEDLLREK--QVSFLSGDAETISFPDKS-TL 109
Cdd:COG2226  13 ALLAALGLRPGARVLDLGCGTGRLALALAE--RGARVTGVDISPEMLELARERAAEAglNVEFVVGDAEDLPFPDGSfDL 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 29338752 110 ITSCSALQWFDSPEEFFKRCNTLLHSQGYFAFSTFGKKNMKEIREL 155
Cdd:COG2226  91 VISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEEL 136
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 30-143 8.93e-17

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: 74.28  E-value: 8.93e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752  30 KMIRLLQKHIPSPCpKVIEFGCGTGIYSRMLLRtlRPEELLLNDLCPEMRYCCEDLLREKQVSFLSGDAETISFPDKS-T 108
Cdd:COG2227  13 RLAALLARLLPAGG-RVLDVGCGTGRLALALAR--RGADVTGVDISPEALEIARERAAELNVDFVQGDLEDLPLEDGSfD 89

                        90       100       110
                ....*....|....*....|....*....|....*
gi 29338752 109 LITSCSALQWFDSPEEFFKRCNTLLHSQGYFAFST 143
Cdd:COG2227  90 LVICSEVLEHLPDPAALLRELARLLKPGGLLLLST 124
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
25-175 8.31e-14

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 67.72  E-value: 8.31e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752  25 RQIANKMIRLLQKHIPSPCPKVIEFGCGTGIYSRMLLRtlRPEELLLNDLCPEMRycceDLLREK--QVSFLSGDAETIS 102
Cdd:COG4976  29 EAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRP--RGYRLTGVDLSEEML----AKAREKgvYDRLLVADLADLA 102

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29338752 103 FPDKS-TLITSCSALQWFDSPEEFFKRCNTLLHSQGYFAFStfgkknmkeIRELTGKGLPYRSREELEAALSLH 175
Cdd:COG4976 103 EPDGRfDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFS---------VEDADGSGRYAHSLDYVRDLLAAA 167
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 2-250 3.11e-13

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 67.48  E-value: 3.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752    2 NKTIIAERFSKAISTYPREANVQRQIANKMIRLLQKHipsPCPKVIEFGCGTGIYSRMLLRtlRPEELLLNDLCPEMRyc 81
Cdd:PRK10258   5 NKQAIAAAFGRAAAHYEQHAELQRQSADALLAMLPQR---KFTHVLDAGCGPGWMSRYWRE--RGSQVTALDLSPPML-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752   82 ceDLLREKQVS--FLSGDAETISFPDKS-TLITSCSALQWFDSPEEFFKRCNTLLHSQGYFAFSTFGKKNMKEIREL--- 155
Cdd:PRK10258  78 --AQARQKDAAdhYLAGDIESLPLATATfDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFTTLVQGSLPELHQAwqa 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752  156 ---TGKGLPYRSREELEAALS-LHFdilYSEEELIPLSFEDPMKVLYHLKqtgvnGLSAqSSLYPKHEKQTWTRRDLQHF 231
Cdd:PRK10258 156 vdeRPHANRFLPPDAIEQALNgWRY---QHHIQPITLWFDDALSAMRSLK-----GIGA-THLHEGRDPRILTRSQLQRL 226

                        250
                 ....*....|....*....
gi 29338752  232 CERYTQEftQGTsVSLTYH 250
Cdd:PRK10258 227 QLAWPQQ--QGR-YPLTYH 242
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 46-133 4.03e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 57.96  E-value: 4.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752    46 VIEFGCGTGIYSRMLLRTLRpEELLLNDLCPEMRYCCEDLLREK--QVSFLSGDAETISFPDKS-TLITSCSALQWFDSP 122
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG-ARVTGVDLSPEMLERARERAAEAglNVEFVQGDAEDLPFPDGSfDLVVSSGVLHHLPDP 79

                          90
                  ....*....|...
gi 29338752   123 --EEFFKRCNTLL 133
Cdd:pfam13649  80 dlEAALREIARVL 92
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 45-144 1.28e-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: 45.88  E-value: 1.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752  45 KVIEFGCGTGIYSRMLLRTLrPEELLLNDLCPEMRYCCE---DLLREKQVSFLSGDAETISFPDKST--LITSCSALQWF 119
Cdd:cd02440   1 RVLDLGCGTGALALALASGP-GARVTGVDISPVALELARkaaAALLADNVEVLKGDAEELPPEADESfdVIISDPPLHHL 79

                        90       100
                ....*....|....*....|....*.
gi 29338752 120 -DSPEEFFKRCNTLLHSQGYFAFSTF 144
Cdd:cd02440  80 vEDLARFLEEARRLLKPGGVLVLTLV 105
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 23-172 2.66e-06

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 46.27  E-value: 2.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752    23 VQRQIANKMIRLLQKHIPSPCP--KVIEFGCGTGIysrmLLRTLRPE--ELLLNDLCPEMRycceDLLREKQVSFLSGDA 98
Cdd:pfam13489   1 YAHQRERLLADLLLRLLPKLPSpgRVLDFGCGTGI----FLRLLRAQgfSVTGVDPSPIAI----ERALLNVRFDQFDEQ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752    99 ETISFPDKSTLITSCSALQWFDSPEEFFKRCNTLLHSQGYFAFSTFGkKNMKEIRELT--------GKGLPYRSREELEA 170
Cdd:pfam13489  73 EAAVPAGKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPL-ASDEADRLLLewpylrprNGHISLFSARSLKR 151


                  ..
gi 29338752   171 AL 172
Cdd:pfam13489 152 LL 153
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 47-139 2.90e-06

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 44.67  E-value: 2.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752    47 IEFGCGTGIYSRMLLRTLRPEELLLNDLCPEMRYCCEDLLRE---KQVSFLSGDAETISFPDKST--LITSCSALQWFDS 121
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAAlglLNAVRVELFQLDLGELDPGSfdVVVASNVLHHLAD 80

                          90
                  ....*....|....*...
gi 29338752   122 PEEFFKRCNTLLHSQGYF 139
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
COG3963 COG3963
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];
25-102 1.38e-05

Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];


Pssm-ID: 443163  Cd Length: 193  Bit Score: 44.43  E-value: 1.38e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752  25 RQIANKMIRllqkHIPSP-CPKVIEFGCGTGIYSRMLLRTLRPEE-LLLNDLCPEMRycceDLLREK--QVSFLSGDAET 100
Cdd:COG3963  31 RALARAMAS----EVDWSgAGPVVELGPGTGVFTRAILARGVPDArLLAVEINPEFA----EHLRRRfpRVTVVNGDAED 102


                ..
gi 29338752 101 IS 102
Cdd:COG3963 103 LA 104
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 29-143 7.38e-05

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 41.84  E-value: 7.38e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752  29 NKMIRLLQKHIPSPCPKVIEFGCGTGIYSRMLLRTLRpEELLLNDLCPEMRYCCEDLLREK----QVSFLSGDAETISFP 104
Cdd:COG2230  38 AKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYG-VRVTGVTLSPEQLEYARERAAEAgladRVEVRLADYRDLPAD 116

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 29338752 105 DKSTLITSCSALQWFDSP--EEFFKRCNTLLHSQGYFAFST 143
Cdd:COG2230 117 GQFDAIVSIGMFEHVGPEnyPAYFAKVARLLKPGGRLLLHT 157
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 17-142 5.86e-04

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 39.90  E-value: 5.86e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752  17 YPREANVQRQIANKMIRLLQKHIpspcpKVIEFGCGTGIYSRMLLRTLRpEELLLNDLCPEM-RYCCEDLLREK--QVSF 93
Cdd:COG0500   6 YSDELLPGLAALLALLERLPKGG-----RVLDLGCGTGRNLLALAARFG-GRVIGIDLSPEAiALARARAAKAGlgNVEF 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 29338752  94 LSGD-AETISFPDKST-LITSCSALQWFD--SPEEFFKRCNTLLHSQGYFAFS 142
Cdd:COG0500  80 LVADlAELDPLPAESFdLVVAFGVLHHLPpeEREALLRELARALKPGGVLLLS 132
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 42-141 1.43e-03

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 39.29  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29338752   42 PCPKVIEFGCGTGIYSRMLLR---TLRPEELllnDLCPEMRycceDLLREKQVSFLSGDAETISfPDKST-LITSCSALQ 117
Cdd:PRK14103  29 RARRVVDLGCGPGNLTRYLARrwpGAVIEAL---DSSPEMV----AAARERGVDARTGDVRDWK-PKPDTdVVVSNAALQ 100

                         90       100
                 ....*....|....*....|....
gi 29338752  118 WFDSPEEFFKRCNTLLHSQGYFAF 141
Cdd:PRK14103 101 WVPEHADLLVRWVDELAPGSWIAV 124
 
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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