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Conserved domains on  [gi|665408278|ref|NP_001285980|]
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juvenile hormone acid methyltransferase, isoform B [Drosophila melanogaster]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10549439)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; similar to Homo sapiens tRNA N(3)-methylcytidine methyltransferase METTL6

CATH:  3.40.50.150
EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008168|GO:0032259|GO:0008757
PubMed:  12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 40-137 7.53e-21

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


:

Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 85.11  E-value: 7.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278   40 LDVGSGSGNVLmDFVKPLLPiRGQLVGTDISSQMVHYASKHYQREERTRFQVLDIGCERLPEELSGRFDHVTSFYCLHWV 119
Cdd:pfam08242   1 LEIGCGTGTLL-RALLEALP-GLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELDPGSFDVVVASNVLHHL 78

                          90
                  ....*....|....*...
gi 665408278  120 QNLKGALGNIYNLLKPEG 137
Cdd:pfam08242  79 ADPRAVLRNIRRLLKPGG 96
 
Name Accession Description Interval E-value
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 40-137 7.53e-21

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 85.11  E-value: 7.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278   40 LDVGSGSGNVLmDFVKPLLPiRGQLVGTDISSQMVHYASKHYQREERTRFQVLDIGCERLPEELSGRFDHVTSFYCLHWV 119
Cdd:pfam08242   1 LEIGCGTGTLL-RALLEALP-GLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELDPGSFDVVVASNVLHHL 78

                          90
                  ....*....|....*...
gi 665408278  120 QNLKGALGNIYNLLKPEG 137
Cdd:pfam08242  79 ADPRAVLRNIRRLLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 39-158 1.16e-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: 77.73  E-value: 1.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278  39 LLDVGSGSGnvlmDFVKPLLPIRGQLVGTDISSQMVHYASKHYQREE-RTRFQVLDIgcERLPEElSGRFDHVTSFYCLH 117
Cdd:COG2226   26 VLDLGCGTG----RLALALAERGARVTGVDISPEMLELARERAAEAGlNVEFVVGDA--EDLPFP-DGSFDLVISSFVLH 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 665408278 118 WVQNLKGALGNIYNLLKPeGGDCLLAFLASNPVYEVYKILK 158
Cdd:COG2226   99 HLPDPERALAEIARVLKP-GGRLVVVDFSPPDLAELEELLA 138
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 39-137 4.31e-09

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: 53.20  E-value: 4.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278  39 LLDVGSGSGNVLMDFVKPLlpiRGQLVGTDISSQMVHYASKHYQREERTRFQVLDIGCERLPEELSGRFDHVTS-FYCLH 117
Cdd:cd02440    2 VLDLGCGTGALALALASGP---GARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIISdPPLHH 78

                         90       100
                 ....*....|....*....|
gi 665408278 118 WVQNLKGALGNIYNLLKPEG 137
Cdd:cd02440   79 LVEDLARFLEEARRLLKPGG 98
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 8-144 1.04e-06

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: 48.82  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278    8 QHANqVQRHDAKLILdefASTMQWRSDGEDALLDVGSGSGNV---LMDFVkpllpIRGQLVGTDISSQMVHYASKHYQre 84
Cdd:TIGR02072  11 RHAK-IQREMAKRLL---ALLKEKGIFIPASVLDIGCGTGYLtraLLKRF-----PQAEFIALDISAGMLAQAKTKLS-- 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278   85 ERTRFQVLDIgcERLPEELSgRFDHVTSFYCLHWVQNLKGALGNIYNLLKPEGgdcLLAF 144
Cdd:TIGR02072  80 ENVQFICGDA--EKLPLEDS-SFDLIVSNLALQWCDDLSQALSELARVLKPGG---LLAF 133
PRK08317 PRK08317
hypothetical protein; Provisional
 37-205 1.64e-06

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 48.01  E-value: 1.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278  37 DALLDVGSGSGNVLMDFVKPLLPiRGQLVGTDISSQMVHYASKHYQREERTRFQVLDIGcERLPEElSGRFDHVTSFYCL 116
Cdd:PRK08317  21 DRVLDVGCGPGNDARELARRVGP-EGRVVGIDRSEAMLALAKERAAGLGPNVEFVRGDA-DGLPFP-DGSFDAVRSDRVL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278 117 HWVQNLKGALGNIYNLLKPeGGDCLlaflasnpvyevykILKTNdkWSTF---------MQDVENFISPLHYSLSPGEEF 187
Cdd:PRK08317  98 QHLEDPARALAEIARVLRP-GGRVV--------------VLDTD--WDTLvwhsgdralMRKILNFWSDHFADPWLGRRL 160

                        170
                 ....*....|....*...
gi 665408278 188 SQLLNDVGFVQHNVEIRN 205
Cdd:PRK08317 161 PGLFREAGLTDIEVEPYT 178
 
Name Accession Description Interval E-value
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 40-137 7.53e-21

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 85.11  E-value: 7.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278   40 LDVGSGSGNVLmDFVKPLLPiRGQLVGTDISSQMVHYASKHYQREERTRFQVLDIGCERLPEELSGRFDHVTSFYCLHWV 119
Cdd:pfam08242   1 LEIGCGTGTLL-RALLEALP-GLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELDPGSFDVVVASNVLHHL 78

                          90
                  ....*....|....*...
gi 665408278  120 QNLKGALGNIYNLLKPEG 137
Cdd:pfam08242  79 ADPRAVLRNIRRLLKPGG 96
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 40-137 2.18e-18

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 78.37  E-value: 2.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278   40 LDVGSGSGNVLMDFVKPLlpiRGQLVGTDISSQMVHYASKHYQREE-RTRFQVLDIgcERLPEElSGRFDHVTSFYCLHW 118
Cdd:pfam13649   2 LDLGCGTGRLTLALARRG---GARVTGVDLSPEMLERARERAAEAGlNVEFVQGDA--EDLPFP-DGSFDLVVSSGVLHH 75

                          90       100
                  ....*....|....*....|.
gi 665408278  119 V--QNLKGALGNIYNLLKPEG 137
Cdd:pfam13649  76 LpdPDLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 39-158 1.16e-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: 77.73  E-value: 1.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278  39 LLDVGSGSGnvlmDFVKPLLPIRGQLVGTDISSQMVHYASKHYQREE-RTRFQVLDIgcERLPEElSGRFDHVTSFYCLH 117
Cdd:COG2226   26 VLDLGCGTG----RLALALAERGARVTGVDISPEMLELARERAAEAGlNVEFVVGDA--EDLPFP-DGSFDLVISSFVLH 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 665408278 118 WVQNLKGALGNIYNLLKPeGGDCLLAFLASNPVYEVYKILK 158
Cdd:COG2226   99 HLPDPERALAEIARVLKP-GGRLVVVDFSPPDLAELEELLA 138
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 40-137 2.27e-17

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 75.39  E-value: 2.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278   40 LDVGSGSGNvlmdFVKPLLPIRGQLVGTDISSQMVHYASKHYQREERTrFQVLDIgcERLPEElSGRFDHVTSFYCLHWV 119
Cdd:pfam08241   1 LDVGCGTGL----LTELLARLGARVTGVDISPEMLELAREKAPREGLT-FVVGDA--EDLPFP-DNSFDLVLSSEVLHHV 72

                          90
                  ....*....|....*...
gi 665408278  120 QNLKGALGNIYNLLKPEG 137
Cdd:pfam08241  73 EDPERALREIARVLKPGG 90
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 39-137 1.33e-16

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: 1.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278  39 LLDVGSGSGNVLMDFVKpllpiRG-QLVGTDISSQMVHYASKHYqREERTRFQVLDIgcERLPEElSGRFDHVTSFYCLH 117
Cdd:COG2227   28 VLDVGCGTGRLALALAR-----RGaDVTGVDISPEALEIARERA-AELNVDFVQGDL--EDLPLE-DGSFDLVICSEVLE 98

                         90       100
                 ....*....|....*....|
gi 665408278 118 WVQNLKGALGNIYNLLKPEG 137
Cdd:COG2227   99 HLPDPAALLRELARLLKPGG 118
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
40-144 3.81e-14

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 66.77  E-value: 3.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278  40 LDVGSGSGNVLMDFVKpLLPiRGQLVGTDISSQMVHYASKHYqreERTRFQVLDIgcERLPeeLSGRFDHVTSFYCLHWV 119
Cdd:COG4106    6 LDLGCGTGRLTALLAE-RFP-GARVTGVDLSPEMLARARARL---PNVRFVVADL--RDLD--PPEPFDLVVSNAALHWL 76

                         90       100
                 ....*....|....*....|....*
gi 665408278 120 QNLKGALGNIYNLLKPEGgdcLLAF 144
Cdd:COG4106   77 PDHAALLARLAAALAPGG---VLAV 98
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 40-137 5.06e-13

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 66.48  E-value: 5.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278  40 LDVGSGSGNVLMDFVKPLlpiRGQLVGTDISSQMVHYASKHYQREERT--RFQVLDIgcERLPEELSGRFDHVTSFYCLH 117
Cdd:COG0500   31 LDLGCGTGRNLLALAARF---GGRVIGIDLSPEAIALARARAAKAGLGnvEFLVADL--AELDPLPAESFDLVVAFGVLH 105

                         90       100
                 ....*....|....*....|..
gi 665408278 118 WV--QNLKGALGNIYNLLKPEG 137
Cdd:COG0500  106 HLppEEREALLRELARALKPGG 127
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
18-144 1.49e-11

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 61.94  E-value: 1.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278  18 AKLILDEFASTMQWRsdgedaLLDVGSGSGNVLmdfvKPLLPIRGQLVGTDISSQMVHYAskhYQREERTRFQVLDIgce 97
Cdd:COG4976   35 AEELLARLPPGPFGR------VLDLGCGTGLLG----EALRPRGYRLTGVDLSEEMLAKA---REKGVYDRLLVADL--- 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 665408278  98 RLPEELSGRFDHVTSFYCLHWVQNLKGALGNIYNLLKPEGgdcLLAF 144
Cdd:COG4976   99 ADLAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGG---LFIF 142
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 13-196 3.31e-10

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 57.82  E-value: 3.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278   13 VQRHDAKLILDEFASTMQWRSDGEDaLLDVGSGSGNVLmdfvKPLLPIRGQLVGTDISSQMVhyaskhyqrEERTRFQVL 92
Cdd:pfam13489   1 YAHQRERLLADLLLRLLPKLPSPGR-VLDFGCGTGIFL----RLLRAQGFSVTGVDPSPIAI---------ERALLNVRF 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278   93 DIGCERLPEELSGRFDHVTSFYCLHWVQNLKGALGNIYNLLKPEGgdcLLAFLASNPVYEVYKILKTNDKWSTFMQdven 172
Cdd:pfam13489  67 DQFDEQEAAVPAGKFDVIVAREVLEHVPDPPALLRQIAALLKPGG---LLLLSTPLASDEADRLLLEWPYLRPRNG---- 139

                         170       180
                  ....*....|....*....|....
gi 665408278  173 fisplHYSLSPGEEFSQLLNDVGF 196
Cdd:pfam13489 140 -----HISLFSARSLKRLLEEAGF 158
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 39-137 4.31e-09

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: 53.20  E-value: 4.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278  39 LLDVGSGSGNVLMDFVKPLlpiRGQLVGTDISSQMVHYASKHYQREERTRFQVLDIGCERLPEELSGRFDHVTS-FYCLH 117
Cdd:cd02440    2 VLDLGCGTGALALALASGP---GARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIISdPPLHH 78

                         90       100
                 ....*....|....*....|
gi 665408278 118 WVQNLKGALGNIYNLLKPEG 137
Cdd:cd02440   79 LVEDLARFLEEARRLLKPGG 98
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 34-138 1.04e-07

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 50.49  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278   34 DGEDALLDVGSGSGNVLMDFVKPLLPiRGQLVGTDISSQMVHYASKHYQRE--ERTRFQVLDIgcERLPEELS-GRFDHV 110
Cdd:pfam13847   2 DKGMRVLDLGCGTGHLSFELAEELGP-NAEVVGIDISEEAIEKARENAQKLgfDNVEFEQGDI--EELPELLEdDKFDVV 78

                          90       100
                  ....*....|....*....|....*...
gi 665408278  111 TSFYCLHWVQNLKGALGNIYNLLKPEGG 138
Cdd:pfam13847  79 ISNCVLNHIPDPDKVLQEILRVLKPGGR 106
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 22-137 1.63e-07

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 49.93  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278  22 LDEFASTMQWRSDgeDALLDVGSGSGnvlmDFVKPLLPIRG-QLVGTDISSQMVHYASKHYQR---EERTRFQVLDIgcE 97
Cdd:COG2230   40 LDLILRKLGLKPG--MRVLDIGCGWG----GLALYLARRYGvRVTGVTLSPEQLEYARERAAEaglADRVEVRLADY--R 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 665408278  98 RLPEElsGRFDHVTSFYCLHWV--QNLKGALGNIYNLLKPEG 137
Cdd:COG2230  112 DLPAD--GQFDAIVSIGMFEHVgpENYPAYFAKVARLLKPGG 151
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 8-144 1.04e-06

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: 48.82  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278    8 QHANqVQRHDAKLILdefASTMQWRSDGEDALLDVGSGSGNV---LMDFVkpllpIRGQLVGTDISSQMVHYASKHYQre 84
Cdd:TIGR02072  11 RHAK-IQREMAKRLL---ALLKEKGIFIPASVLDIGCGTGYLtraLLKRF-----PQAEFIALDISAGMLAQAKTKLS-- 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278   85 ERTRFQVLDIgcERLPEELSgRFDHVTSFYCLHWVQNLKGALGNIYNLLKPEGgdcLLAF 144
Cdd:TIGR02072  80 ENVQFICGDA--EKLPLEDS-SFDLIVSNLALQWCDDLSQALSELARVLKPGG---LLAF 133
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
40-197 1.21e-06

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 48.59  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278   40 LDVGSGSGNVLMDFVKPLLPiRGQLVGTDISSQMVHYASKHYQREERTRFQVLDIGCERLPEElSGRFDHVTSFYCLHWV 119
Cdd:pfam01209  47 LDVAGGTGDWTFGLSDSAGS-SGKVVGLDINENMLKEGEKKAKEEGKYNIEFLQGNAEELPFE-DDSFDIVTISFGLRNF 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278  120 QNLKGALGNIYNLLKPEGGDCLLAFlaSNPVYEVYK-----------------ILKTNDKWSTFMQDVENFisplhysls 182
Cdd:pfam01209 125 PDYLKVLKEAFRVLKPGGRVVCLEF--SKPENPLLSqayelyfkyvmpfmgkmFAKSYKSYQYLQESIRDF--------- 193

                         170
                  ....*....|....*.
gi 665408278  183 PG-EEFSQLLNDVGFV 197
Cdd:pfam01209 194 PDqKTLASMFEKAGFK 209
PRK08317 PRK08317
hypothetical protein; Provisional
 37-205 1.64e-06

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 48.01  E-value: 1.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278  37 DALLDVGSGSGNVLMDFVKPLLPiRGQLVGTDISSQMVHYASKHYQREERTRFQVLDIGcERLPEElSGRFDHVTSFYCL 116
Cdd:PRK08317  21 DRVLDVGCGPGNDARELARRVGP-EGRVVGIDRSEAMLALAKERAAGLGPNVEFVRGDA-DGLPFP-DGSFDAVRSDRVL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278 117 HWVQNLKGALGNIYNLLKPeGGDCLlaflasnpvyevykILKTNdkWSTF---------MQDVENFISPLHYSLSPGEEF 187
Cdd:PRK08317  98 QHLEDPARALAEIARVLRP-GGRVV--------------VLDTD--WDTLvwhsgdralMRKILNFWSDHFADPWLGRRL 160

                        170
                 ....*....|....*...
gi 665408278 188 SQLLNDVGFVQHNVEIRN 205
Cdd:PRK08317 161 PGLFREAGLTDIEVEPYT 178
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 4-137 1.93e-06

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 48.22  E-value: 1.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278   4 ASLY-QHAnQVQRHDAKLILDEFASTmqwrsdGEDALLDVGSGSGNVLMDFVKpllpiRGQLV-GTDISSQMVHYASkhy 81
Cdd:PRK10258  17 AAHYeQHA-ELQRQSADALLAMLPQR------KFTHVLDAGCGPGWMSRYWRE-----RGSQVtALDLSPPMLAQAR--- 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 665408278  82 QREERTRFQVLDIgcERLPEElSGRFDHVTSFYCLHWVQNLKGALGNIYNLLKPEG 137
Cdd:PRK10258  82 QKDAADHYLAGDI--ESLPLA-TATFDLAWSNLAVQWCGNLSTALRELYRVVRPGG 134
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 37-137 5.42e-05

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 43.60  E-value: 5.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278  37 DALLDVGSGSGNVLMDFVKPLLPIrGQLVGTDISSQMVHYA-SKHYQREERTRFQVLDIGCERLPEElSGRFDHVTSFYC 115
Cdd:PRK00216  53 DKVLDLACGTGDLAIALAKAVGKT-GEVVGLDFSEGMLAVGrEKLRDLGLSGNVEFVQGDAEALPFP-DNSFDAVTIAFG 130

                         90       100
                 ....*....|....*....|..
gi 665408278 116 LHWVQNLKGALGNIYNLLKPEG 137
Cdd:PRK00216 131 LRNVPDIDKALREMYRVLKPGG 152
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 39-113 1.40e-04

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 42.13  E-value: 1.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278  39 LLDVGSGSGnvlmdfvkpLLPI----RG-QLVGTDISSQMVHYASKHYQRE---ERTRFQVLDIgcerlpEELSGRFDHV 110
Cdd:PRK07580  67 ILDAGCGVG---------SLSIplarRGaKVVASDISPQMVEEARERAPEAglaGNITFEVGDL------ESLLGRFDTV 131


                 ...
gi 665408278 111 TSF 113
Cdd:PRK07580 132 VCL 134
PRK06922 PRK06922
class I SAM-dependent methyltransferase;
2-87 3.24e-03

class I SAM-dependent methyltransferase;


Pssm-ID: 180751 [Multi-domain]  Cd Length: 677  Bit Score: 39.08  E-value: 3.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408278   2 NQASLYQHANQVQrHDAKLILDEFAStmqwrsdgeDALLDVGSGSGnVLMDFVKPLLPiRGQLVGTDISSQMVHYASKHY 81
Cdd:PRK06922 395 NEEVYLEHMNSSA-DDKRIILDYIKG---------DTIVDVGAGGG-VMLDMIEEETE-DKRIYGIDISENVIDTLKKKK 462


                 ....*.
gi 665408278  82 QREERT 87
Cdd:PRK06922 463 QNEGRS 468
 
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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