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Conserved domains on  [gi|446637072|ref|WP_000714418|]
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MULTISPECIES: bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG [Bacillus]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 11454890)

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

EC:  2.1.1.-
Gene Ontology:  GO:0032259|GO:0008168|GO:1904047
PubMed:  12504684|12826405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 22-142 6.29e-31

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: 110.49  E-value: 6.29e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072  22 NKNSQEMWDSgsrsTIIPFFEQYVEKEAQVLDVGCGDGYGTYKLSCVGYKAVGVDLSEIMIQKGKERGEDSNLSFVKGDL 101
Cdd:COG2227    3 DPDARDFWDR----RLAALLARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNVDFVQGDL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446637072 102 SALPFENEQFKAIMAINSLEWTENPLQALNEIKRVLKKDGY 142
Cdd:COG2227   79 EDLPLEDGSFDLVICSEVLEHLPDPAALLRELARLLKPGGL 119
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 22-142 6.29e-31

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: 110.49  E-value: 6.29e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072  22 NKNSQEMWDSgsrsTIIPFFEQYVEKEAQVLDVGCGDGYGTYKLSCVGYKAVGVDLSEIMIQKGKERGEDSNLSFVKGDL 101
Cdd:COG2227    3 DPDARDFWDR----RLAALLARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNVDFVQGDL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446637072 102 SALPFENEQFKAIMAINSLEWTENPLQALNEIKRVLKKDGY 142
Cdd:COG2227   79 EDLPLEDGSFDLVICSEVLEHLPDPAALLRELARLLKPGGL 119
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 52-145 9.32e-30

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 106.21  E-value: 9.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072   52 LDVGCGDGYGTYKLSCVGYKAVGVDLSEIMIQKGKERGEDSNLSFVKGDLSALPFENEQFKAIMAINSLEWTENPLQALN 131
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERALR 80

                          90
                  ....*....|....
gi 446637072  132 EIKRVLKKDGYACI 145
Cdd:pfam08241  81 EIARVLKPGGILII 94
PRK08317 PRK08317
hypothetical protein; Provisional
 38-146 8.56e-18

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 78.83  E-value: 8.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072  38 IPFFEQY---------VEKEAQVLDVGCGDGYGTYKLS---CVGYKAVGVDLSEIMIQKGKERGED--SNLSFVKGDLSA 103
Cdd:PRK08317   1 LPDFRRYrartfellaVQPGDRVLDVGCGPGNDARELArrvGPEGRVVGIDRSEAMLALAKERAAGlgPNVEFVRGDADG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446637072 104 LPFENEQFKAIMAINSLEWTENPLQALNEIKRVLKKDGYACIA 146
Cdd:PRK08317  81 LPFPDGSFDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVL 123
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 51-148 5.66e-16

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: 70.92  E-value: 5.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072  51 VLDVGCGDGYGTYKL-SCVGYKAVGVDLSEIMIQKGKE---RGEDSNLSFVKGDLSALPF-ENEQFKAIMAINSLEWT-E 124
Cdd:cd02440    2 VLDLGCGTGALALALaSGPGARVTGVDISPVALELARKaaaALLADNVEVLKGDAEELPPeADESFDVIISDPPLHHLvE 81

                         90       100
                 ....*....|....*....|....
gi 446637072 125 NPLQALNEIKRVLKKDGYACIAIL 148
Cdd:cd02440   82 DLARFLEEARRLLKPGGVLVLTLV 105
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 45-168 2.87e-14

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 69.21  E-value: 2.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072   45 VEKEAQVLDVGCGDGYGTYKLSCVG---YKAVGVDLSEIMIQKGKERGE-DSNLSFVKGDLSALPFENEQFKAIMAINSL 120
Cdd:TIGR01934  37 VFKGQKVLDVACGTGDLAIELAKSApdrGKVTGVDFSSEMLEVAKKKSElPLNIEFIQADAEALPFEDNSFDAVTIAFGL 116

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 446637072  121 EWTENPLQALNEIKRVLKKDG-YACIAILGPTAKPRENSYpRLYGKDVV 168
Cdd:TIGR01934 117 RNVTDIQKALREMYRVLKPGGrLVILEFSKPANALLKKFY-KFYLKNVL 164
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 22-142 6.29e-31

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: 110.49  E-value: 6.29e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072  22 NKNSQEMWDSgsrsTIIPFFEQYVEKEAQVLDVGCGDGYGTYKLSCVGYKAVGVDLSEIMIQKGKERGEDSNLSFVKGDL 101
Cdd:COG2227    3 DPDARDFWDR----RLAALLARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNVDFVQGDL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446637072 102 SALPFENEQFKAIMAINSLEWTENPLQALNEIKRVLKKDGY 142
Cdd:COG2227   79 EDLPLEDGSFDLVICSEVLEHLPDPAALLRELARLLKPGGL 119
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 45-187 1.26e-30

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: 110.08  E-value: 1.26e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072  45 VEKEAQVLDVGCGDGYGTYKLSCVGYKAVGVDLSEIMIQKGKERGEDS--NLSFVKGDLSALPFENEQFKAIMAINSLEW 122
Cdd:COG2226   20 LRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAglNVEFVVGDAEDLPFPDGSFDLVISSFVLHH 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446637072 123 TENPLQALNEIKRVLKKDGYACIAILGPTAKprensyprlygkdvvcntmmpWEFEQLAKEQGFE 187
Cdd:COG2226  100 LPDPERALAEIARVLKPGGRLVVVDFSPPDL---------------------AELEELLAEAGFE 143
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 52-145 9.32e-30

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 106.21  E-value: 9.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072   52 LDVGCGDGYGTYKLSCVGYKAVGVDLSEIMIQKGKERGEDSNLSFVKGDLSALPFENEQFKAIMAINSLEWTENPLQALN 131
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERALR 80

                          90
                  ....*....|....
gi 446637072  132 EIKRVLKKDGYACI 145
Cdd:pfam08241  81 EIARVLKPGGILII 94
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 51-141 2.65e-27

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 99.95  E-value: 2.65e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072   51 VLDVGCGDGYGTYKLS-CVGYKAVGVDLSEIMIQKGKERGEDS--NLSFVKGDLSALPFENEQFKAIMAINSLEWTENP- 126
Cdd:pfam13649   1 VLDLGCGTGRLTLALArRGGARVTGVDLSPEMLERARERAAEAglNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPd 80

                          90
                  ....*....|....*.
gi 446637072  127 -LQALNEIKRVLKKDG 141
Cdd:pfam13649  81 lEAALREIARVLKPGG 96
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
49-145 6.89e-18

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 75.63  E-value: 6.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072  49 AQVLDVGCGDGYGTYKLS--CVGYKAVGVDLSEIMIQKGKERGedSNLSFVKGDLSALPFEnEQFKAIMAINSLEWTENP 126
Cdd:COG4106    3 RRVLDLGCGTGRLTALLAerFPGARVTGVDLSPEMLARARARL--PNVRFVVADLRDLDPP-EPFDLVVSNAALHWLPDH 79

                         90
                 ....*....|....*....
gi 446637072 127 LQALNEIKRVLKKDGYACI 145
Cdd:COG4106   80 AALLARLAAALAPGGVLAV 98
PRK08317 PRK08317
hypothetical protein; Provisional
 38-146 8.56e-18

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 78.83  E-value: 8.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072  38 IPFFEQY---------VEKEAQVLDVGCGDGYGTYKLS---CVGYKAVGVDLSEIMIQKGKERGED--SNLSFVKGDLSA 103
Cdd:PRK08317   1 LPDFRRYrartfellaVQPGDRVLDVGCGPGNDARELArrvGPEGRVVGIDRSEAMLALAKERAAGlgPNVEFVRGDADG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446637072 104 LPFENEQFKAIMAINSLEWTENPLQALNEIKRVLKKDGYACIA 146
Cdd:PRK08317  81 LPFPDGSFDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVL 123
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 29-164 1.74e-17

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 77.26  E-value: 1.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072  29 WDSGSRSTIIPFFEQYV------EKEAQVLDVGCGDGYGTYKL-SCVGYKAVGVDLSEIMIQKGKERGEDSNLS---FVK 98
Cdd:COG0500    2 WDSYYSDELLPGLAALLallerlPKGGRVLDLGCGTGRNLLALaARFGGRVIGIDLSPEAIALARARAAKAGLGnveFLV 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446637072  99 GDLSAL-PFENEQFKAIMAINSLEWT--ENPLQALNEIKRVLKKDGyacIAILGPTAKPRENSYPRLYG 164
Cdd:COG0500   82 ADLAELdPLPAESFDLVVAFGVLHHLppEEREALLRELARALKPGG---VLLLSASDAAAALSLARLLL 147
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
11-147 1.85e-17

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 76.96  E-value: 1.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072  11 EKKWDSSAEYWNKNSQEMWD-SGSRSTIIPFFEQYV-EKEAQVLDVGCGDGYGTYKLSCVGYKAVGVDLSEIMIQKGKER 88
Cdd:COG4976    8 EALFDQYADSYDAALVEDLGyEAPALLAEELLARLPpGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREK 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446637072  89 GEDSNlsFVKGDLSALPFENEQFKAIMAINSLEWTENPLQALNEIKRVLKKDGYACIAI 147
Cdd:COG4976   88 GVYDR--LLVADLADLAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSV 144
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 51-148 5.66e-16

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: 70.92  E-value: 5.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072  51 VLDVGCGDGYGTYKL-SCVGYKAVGVDLSEIMIQKGKE---RGEDSNLSFVKGDLSALPF-ENEQFKAIMAINSLEWT-E 124
Cdd:cd02440    2 VLDLGCGTGALALALaSGPGARVTGVDISPVALELARKaaaALLADNVEVLKGDAEELPPeADESFDVIISDPPLHHLvE 81

                         90       100
                 ....*....|....*....|....
gi 446637072 125 NPLQALNEIKRVLKKDGYACIAIL 148
Cdd:cd02440   82 DLARFLEEARRLLKPGGVLVLTLV 105
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 46-146 1.84e-15

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 70.91  E-value: 1.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072   46 EKEAQVLDVGCGDGYGTYKL---SCVGYKAVGVDLSEIMIQKGKERGED---SNLSFVKGDLSALP--FENEQFKAIMAI 117
Cdd:pfam13847   2 DKGMRVLDLGCGTGHLSFELaeeLGPNAEVVGIDISEEAIEKARENAQKlgfDNVEFEQGDIEELPelLEDDKFDVVISN 81

                          90       100
                  ....*....|....*....|....*....
gi 446637072  118 NSLEWTENPLQALNEIKRVLKKDGYACIA 146
Cdd:pfam13847  82 CVLNHIPDPDKVLQEILRVLKPGGRLIIS 110
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 45-168 2.87e-14

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 69.21  E-value: 2.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072   45 VEKEAQVLDVGCGDGYGTYKLSCVG---YKAVGVDLSEIMIQKGKERGE-DSNLSFVKGDLSALPFENEQFKAIMAINSL 120
Cdd:TIGR01934  37 VFKGQKVLDVACGTGDLAIELAKSApdrGKVTGVDFSSEMLEVAKKKSElPLNIEFIQADAEALPFEDNSFDAVTIAFGL 116

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 446637072  121 EWTENPLQALNEIKRVLKKDG-YACIAILGPTAKPRENSYpRLYGKDVV 168
Cdd:TIGR01934 117 RNVTDIQKALREMYRVLKPGGrLVILEFSKPANALLKKFY-KFYLKNVL 164
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 37-189 5.01e-14

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 67.07  E-value: 5.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072   37 IIPFFEQYVEKEAQVLDVGCGDGYGTYKLSCVGYKAVGVDLSEIMIQKGKergedSNLSFVKGDLSALPFENEQFKAIMA 116
Cdd:pfam13489  12 LLLRLLPKLPSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERAL-----LNVRFDQFDEQEAAVPAGKFDVIVA 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446637072  117 INSLEWTENPLQALNEIKRVLKKDGYacIAILGPTAKPRENSYPRLYGKDVVCNTMMPW----EFEQLAKEQGFEAV 189
Cdd:pfam13489  87 REVLEHVPDPPALLRQIAALLKPGGL--LLLSTPLASDEADRLLLEWPYLRPRNGHISLfsarSLKRLLEEAGFEVV 161
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 51-147 1.85e-13

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 65.72  E-value: 1.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072  51 VLDVGCGDGYGTYKL-SCVGYKAVGVDLSEIMIQKGKERGEDSNLS----FVKGDLSALPFEnEQFKAIMAINSLEW--T 123
Cdd:COG2230   55 VLDIGCGWGGLALYLaRRYGVRVTGVTLSPEQLEYARERAAEAGLAdrveVRLADYRDLPAD-GQFDAIVSIGMFEHvgP 133

                         90       100
                 ....*....|....*....|....
gi 446637072 124 ENPLQALNEIKRVLKKDGYACIAI 147
Cdd:COG2230  134 ENYPAYFAKVARLLKPGGRLLLHT 157
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 51-150 4.97e-13

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: 66.16  E-value: 4.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072   51 VLDVGCGDGYGTYKLSCVGYKA--VGVDLSEIMIQKGKERgEDSNLSFVKGDLSALPFENEQFKAIMAINSLEWTENPLQ 128
Cdd:TIGR02072  38 VLDIGCGTGYLTRALLKRFPQAefIALDISAGMLAQAKTK-LSENVQFICGDAEKLPLEDSSFDLIVSNLALQWCDDLSQ 116

                          90       100
                  ....*....|....*....|..
gi 446637072  129 ALNEIKRVLKKDGYACIAILGP 150
Cdd:TIGR02072 117 ALSELARVLKPGGLLAFSTFGP 138
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 50-148 1.81e-12

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 64.40  E-value: 1.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072  50 QVLDVGCGDGYGTYKLS-CVGYKA--VGVDLSEIMIQKGKER----GEDSNLSFVKGDLSALPFENEQFKAI-MAI---N 118
Cdd:PRK00216  54 KVLDLACGTGDLAIALAkAVGKTGevVGLDFSEGMLAVGREKlrdlGLSGNVEFVQGDAEALPFPDNSFDAVtIAFglrN 133

                         90       100       110
                 ....*....|....*....|....*....|
gi 446637072 119 slewTENPLQALNEIKRVLKKDGYAciAIL 148
Cdd:PRK00216 134 ----VPDIDKALREMYRVLKPGGRL--VIL 157
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 52-142 3.10e-12

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 60.84  E-value: 3.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072   52 LDVGCGDGYGTYKL--SCVGYKAVGVDLSEIMIQKGKER-GEDSNLSFVKGDLSALPFENE---QFKAIMAINSLEWTEN 125
Cdd:pfam08242   1 LEIGCGTGTLLRALleALPGLEYTGLDISPAALEAARERlAALGLLNAVRVELFQLDLGELdpgSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*..
gi 446637072  126 PLQALNEIKRVLKKDGY 142
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGV 97
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
49-190 1.29e-10

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 58.99  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072   49 AQVLDVGCGDGYGTYKLS-CVG--YKAVGVDLSEIMIQKGKERGED---SNLSFVKGDLSALPFENEQFKAIMAINSLEW 122
Cdd:pfam01209  44 NKFLDVAGGTGDWTFGLSdSAGssGKVVGLDINENMLKEGEKKAKEegkYNIEFLQGNAEELPFEDDSFDIVTISFGLRN 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072  123 TENPLQALNEIKRVLKKDG-YACIAILGPTAKPRENSYpRLYGKDVvcntmMPW-------------------------- 175
Cdd:pfam01209 124 FPDYLKVLKEAFRVLKPGGrVVCLEFSKPENPLLSQAY-ELYFKYV-----MPFmgkmfaksyksyqylqesirdfpdqk 197

                         170
                  ....*....|....*
gi 446637072  176 EFEQLAKEQGFEAVD 190
Cdd:pfam01209 198 TLASMFEKAGFKSVG 212
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 49-141 3.14e-08

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 52.45  E-value: 3.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072  49 AQVLDVGCGDGYGTYKLSCVGYKAVGVDLSEIMIQKGKERgeDSNLSFVKGDLSALPFENEQFKAIMAINSLEWTENPLQ 128
Cdd:PRK10258  44 THVLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQARQK--DAADHYLAGDIESLPLATATFDLAWSNLAVQWCGNLST 121

                         90
                 ....*....|...
gi 446637072 129 ALNEIKRVLKKDG 141
Cdd:PRK10258 122 ALRELYRVVRPGG 134
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 42-142 3.48e-08

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 52.61  E-value: 3.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072  42 EQYVEKEAQVLDVGCGDGYGTYKL-----SCVGYKAVGVDLSEIMIQKGKERGedSNLSFVKGDLSALPFENEQFKAIMA 116
Cdd:PRK11088  80 ERLDEKATALLDIGCGEGYYTHALadalpEITTMQLFGLDISKVAIKYAAKRY--PQVTFCVASSHRLPFADQSLDAIIR 157

                         90       100
                 ....*....|....*....|....*.
gi 446637072 117 INSlewtenPLQAlNEIKRVLKKDGY 142
Cdd:PRK11088 158 IYA------PCKA-EELARVVKPGGI 176
PLN02490 PLN02490
MPBQ/MSBQ methyltransferase
 51-150 8.75e-08

MPBQ/MSBQ methyltransferase


Pssm-ID: 215270 [Multi-domain]  Cd Length: 340  Bit Score: 51.82  E-value: 8.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072  51 VLDVGCGDGYGTYKL-SCVGYKAVGV-DLSEIMIQKGKERGEDSNLSFVKGDLSALPFENEQFKAIMAINSLEWTENPLQ 128
Cdd:PLN02490 117 VVDVGGGTGFTTLGIvKHVDAKNVTIlDQSPHQLAKAKQKEPLKECKIIEGDAEDLPFPTDYADRYVSAGSIEYWPDPQR 196

                         90       100
                 ....*....|....*....|..
gi 446637072 129 ALNEIKRVLKKDGYACiaILGP 150
Cdd:PLN02490 197 GIKEAYRVLKIGGKAC--LIGP 216
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 47-120 3.14e-07

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 49.45  E-value: 3.14e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446637072  47 KEAQVLDVGCGDGYGTYKLSCVGYKAVGVDLSEIMIQKGKER----GEDSNLSFVKGDLSALpfeNEQFKAIMAINSL 120
Cdd:PRK07580  63 TGLRILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERapeaGLAGNITFEVGDLESL---LGRFDTVVCLDVL 137
PLN02244 PLN02244
tocopherol O-methyltransferase
 51-189 9.55e-06

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 45.51  E-value: 9.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072  51 VLDVGCGDG----YGTYKLSCvgyKAVGVDLSEIMIQKG----KERGEDSNLSFVKGDLSALPFENEQFKAIMAINSLEW 122
Cdd:PLN02244 122 IVDVGCGIGgssrYLARKYGA---NVKGITLSPVQAARAnalaAAQGLSDKVSFQVADALNQPFEDGQFDLVWSMESGEH 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072 123 TENPLQALNEIKRVLKKDGYA-----CIAILGP---TAKPRENSYprlygKDVVCNT--MMPW----EFEQLAKEQGFEA 188
Cdd:PLN02244 199 MPDKRKFVQELARVAAPGGRIiivtwCHRDLEPgetSLKPDEQKL-----LDKICAAyyLPAWcstsDYVKLAESLGLQD 273


                 .
gi 446637072 189 V 189
Cdd:PLN02244 274 I 274
PRK05785 PRK05785
hypothetical protein; Provisional
 34-139 1.59e-05

hypothetical protein; Provisional


Pssm-ID: 235607 [Multi-domain]  Cd Length: 226  Bit Score: 44.29  E-value: 1.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072  34 RSTIIPFFEQYVEKEAQVLDVGCGDGYGTYKLSCV-GYKAVGVDLSEIMIQkgkergedsnLSFVKGD-----LSALPFE 107
Cdd:PRK05785  38 RAELVKTILKYCGRPKKVLDVAAGKGELSYHFKKVfKYYVVALDYAENMLK----------MNLVADDkvvgsFEALPFR 107

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446637072 108 NEQFKAIMAINSLEWTENPLQALNEIKRVLKK 139
Cdd:PRK05785 108 DKSFDVVMSSFALHASDNIEKVIAEFTRVSRK 139
arsM PRK11873
arsenite methyltransferase;
51-141 1.64e-05

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 44.55  E-value: 1.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072  51 VLDVGCGDGYGTYkLSC--VGY--KAVGVDLSEIMIQKGK---ERGEDSNLSFVKGDLSALPFENEQFKAIMA---INsl 120
Cdd:PRK11873  81 VLDLGSGGGFDCF-LAArrVGPtgKVIGVDMTPEMLAKARanaRKAGYTNVEFRLGEIEALPVADNSVDVIISncvIN-- 157

                         90       100
                 ....*....|....*....|.
gi 446637072 121 eWTENPLQALNEIKRVLKKDG 141
Cdd:PRK11873 158 -LSPDKERVFKEAFRVLKPGG 177
metW TIGR02081
methionine biosynthesis protein MetW; This protein is found alongside MetX, of the enzyme that ...
 45-139 4.29e-05

methionine biosynthesis protein MetW; This protein is found alongside MetX, of the enzyme that acylates homoserine as a first step toward methionine biosynthesis, in many species. It appears to act in methionine biosynthesis but is not fully characterized. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273958  Cd Length: 194  Bit Score: 42.74  E-value: 4.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072   45 VEKEAQVLDVGCGDGYGTYKLS----CVGYkavGVDLSEIMIQKGKERGedsnLSFVKGDLS-ALP-FENEQFKAIMAIN 118
Cdd:TIGR02081  11 IPPGSRVLDLGCGDGELLALLRdekqVRGY---GIEIDQDGVLACVARG----VNVIQGDLDeGLEaFPDKSFDYVILSQ 83

                          90       100
                  ....*....|....*....|.
gi 446637072  119 SLEWTENPLQALNEIKRVLKK 139
Cdd:TIGR02081  84 TLQATRNPEEILDEMLRVGRH 104
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
51-145 1.07e-04

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 42.26  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072  51 VLDVGCGDGYGTYKLSCVGYKAVGVDLSEIMIQKGKERGEDSNLSfvkgdlsalpfENEQFK--AIMAINS--------- 119
Cdd:PRK11036  48 VLDAGGGEGQTAIKLAELGHQVILCDLSAEMIQRAKQAAEAKGVS-----------DNMQFIhcAAQDIAQhletpvdli 116

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446637072 120 -----LEWTENPLQALNEIKRVLKKDGYACI 145
Cdd:PRK11036 117 lfhavLEWVADPKSVLQTLWSVLRPGGALSL 147
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
 43-139 1.89e-04

Methionine biosynthesis protein MetW; This family consists of several bacterial and one archaeal methionine biosynthesis MetW proteins. Biosynthesis of methionine from homoserine in Pseudomonas putida takes place in three steps. The first step is the acylation of homoserine to yield an acyl-L-homoserine. This reaction is catalyzed by the products of the metXW genes and is equivalent to the first step in enterobacteria, gram-positive bacteria and fungi, except that in these microorganizms the reaction is catalyzed by a single polypeptide (the product of the metA gene in Escherichia coli and the met5 gene product in Neurospora crassa). In Pseudomonas putida, as in gram-positive bacteria and certain fungi, the second and third steps are a direct sulfhydrylation that converts the O-acyl-L-homoserine into homocysteine and further methylation to yield methionine. The latter reaction can be mediated by either of the two methionine synthetases present in the cells.


Pssm-ID: 399779  Cd Length: 193  Bit Score: 40.90  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072   43 QYVEKEAQVLDVGCGDGYGTYKLS-CVGYKAVGVDLSEIMIQKGKERGedsnLSFVKGDLSA--LPFENEQFKAIMAINS 119
Cdd:pfam07021   9 EWIPPGSRVLDLGCGDGTLLYLLKeEKGVDGYGIELDAAGVAECVAKG----LYVIQGDLDEglEHFPDKSFDYVILSQT 84

                          90       100
                  ....*....|....*....|
gi 446637072  120 LEWTENPLQALNEIKRVLKK 139
Cdd:pfam07021  85 LQATRNPREVLDEMLRIGRR 104
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 51-188 2.06e-04

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 41.41  E-value: 2.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072  51 VLDVGCGDGYGTYKLS-CVGY--KAVGVDLSEIMIQKGKERGED------SNLSFVKGDLSALPFENEQFKAIMAINSLE 121
Cdd:PLN02233  77 VLDLCCGSGDLAFLLSeKVGSdgKVMGLDFSSEQLAVAASRQELkakscyKNIEWIEGDATDLPFDDCYFDAITMGYGLR 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072 122 WTENPLQALNEIKRVLKKDGYACIAILGPTAKPRENSYPRL--------------------YGKDVVCNTMMPWEFEQLA 181
Cdd:PLN02233 157 NVVDRLKAMQEMYRVLKPGSRVSILDFNKSTQPFTTSMQEWmidnvvvpvatgyglakeyeYLKSSINEYLTGEELEKLA 236


                 ....*..
gi 446637072 182 KEQGFEA 188
Cdd:PLN02233 237 LEAGFSS 243
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 42-143 8.59e-04

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 39.56  E-value: 8.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446637072   42 EQYVEKEAQVLDVGCGDG---YGTYKLSCVgyKAVGVDLSEIMIQKGKE-----RGEDSNLSFVKGDLSALPFE----Ne 109
Cdd:pfam06325 156 ERLVKPGESVLDVGCGSGilaIAALKLGAK--KVVGVDIDPVAVRAAKEnaelnGVEARLEVYLPGDLPKEKADvvvaN- 232

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 446637072  110 qfkaIMAinslewteNPLQALNE-IKRVLKKDGYA 143
Cdd:pfam06325 233 ----ILA--------DPLIELAPdIYALVKPGGYL 255
 
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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