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Conserved domains on  [gi|490826323|ref|WP_004688413|]
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bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG [Brucella neotomae]

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 ...
 23-133 1.45e-14

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: 66.96  E-value: 1.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826323  23 NPKLAEFL-QHVAPGGFILELGSGSGLDAKFMIENGFKV---DPTDGSYELAEEASRLLGQPVRHMYFEDLD-AIEQYDG 97
Cdd:COG2227   11 DRRLAALLaRLLPAGGRVLDVGCGTGRLALALARRGADVtgvDISPEALEIARERAAELNVDFVQGDLEDLPlEDGSFDL 90

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 490826323  98 IYTSASLLHakrsvLPE---IVKCIHRALKTSGTVWASF 133
Cdd:COG2227   91 VICSEVLEH-----LPDpaaLLRELARLLKPGGLLLLST 124
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 23-133 1.45e-14

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: 66.96  E-value: 1.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826323  23 NPKLAEFL-QHVAPGGFILELGSGSGLDAKFMIENGFKV---DPTDGSYELAEEASRLLGQPVRHMYFEDLD-AIEQYDG 97
Cdd:COG2227   11 DRRLAALLaRLLPAGGRVLDVGCGTGRLALALARRGADVtgvDISPEALEIARERAAELNVDFVQGDLEDLPlEDGSFDL 90

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 490826323  98 IYTSASLLHakrsvLPE---IVKCIHRALKTSGTVWASF 133
Cdd:COG2227   91 VICSEVLEH-----LPDpaaLLRELARLLKPGGLLLLST 124
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 39-127 1.57e-09

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 52.95  E-value: 1.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826323   39 ILELGSGSGLDAKFMIENGFK----VDPTDGSYELAEEASRLLGQPVR--HMYFEDLD-AIEQYDGIYTSASLLHAKRSV 111
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGArvtgVDLSPEMLERARERAAEAGLNVEfvQGDAEDLPfPDGSFDLVVSSGVLHHLPDPD 80

                          90
                  ....*....|....*.
gi 490826323  112 LPEIVKCIHRALKTSG 127
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 39-133 1.47e-07

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: 47.81  E-value: 1.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826323  39 ILELGSGSGLDAKFMIENGFK----VDPTDGSYELAEEASRLLGQP---VRHMYFEDL--DAIEQYDGIYTSASLLHAKR 109
Cdd:cd02440    2 VLDLGCGTGALALALASGPGArvtgVDISPVALELARKAAAALLADnveVLKGDAEELppEADESFDVIISDPPLHHLVE 81

                         90       100
                 ....*....|....*....|....
gi 490826323 110 SVlPEIVKCIHRALKTSGTVWASF 133
Cdd:cd02440   82 DL-ARFLEEARRLLKPGGVLVLTL 104
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 23-133 1.45e-14

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: 66.96  E-value: 1.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826323  23 NPKLAEFL-QHVAPGGFILELGSGSGLDAKFMIENGFKV---DPTDGSYELAEEASRLLGQPVRHMYFEDLD-AIEQYDG 97
Cdd:COG2227   11 DRRLAALLaRLLPAGGRVLDVGCGTGRLALALARRGADVtgvDISPEALEIARERAAELNVDFVQGDLEDLPlEDGSFDL 90

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 490826323  98 IYTSASLLHakrsvLPE---IVKCIHRALKTSGTVWASF 133
Cdd:COG2227   91 VICSEVLEH-----LPDpaaLLRELARLLKPGGLLLLST 124
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
3-141 4.15e-10

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 56.16  E-value: 4.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826323   3 DQTLSFYAQNAETYAARSVVN-------PKLAEFLQHVAPGGF--ILELGSGSGLDAKFMIENGFKVDPTDGSYELAEEA 73
Cdd:COG4976    5 AYVEALFDQYADSYDAALVEDlgyeapaLLAEELLARLPPGPFgrVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKA 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826323  74 -SRLLGQPVRHMYFEDLDAI-EQYDGIYTSASLLHakRSVLPEIVKCIHRALKTSGTVWASFKDGSSEGY 141
Cdd:COG4976   85 rEKGVYDRLLVADLADLAEPdGRFDLIVAADVLTY--LGDLAAVFAGVARALKPGGLFIFSVEDADGSGR 152
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 39-127 1.57e-09

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 52.95  E-value: 1.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826323   39 ILELGSGSGLDAKFMIENGFK----VDPTDGSYELAEEASRLLGQPVR--HMYFEDLD-AIEQYDGIYTSASLLHAKRSV 111
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGArvtgVDLSPEMLERARERAAEAGLNVEfvQGDAEDLPfPDGSFDLVVSSGVLHHLPDPD 80

                          90
                  ....*....|....*.
gi 490826323  112 LPEIVKCIHRALKTSG 127
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 23-129 4.17e-09

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 53.01  E-value: 4.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826323  23 NPKLAEFLQH--VAPGGFILELGSGSGLDAKFMIEN-GFKVDPTDGS---YELAEEASRLLGQP----VRHMYFEDLDAI 92
Cdd:COG2230   37 EAKLDLILRKlgLKPGMRVLDIGCGWGGLALYLARRyGVRVTGVTLSpeqLEYARERAAEAGLAdrveVRLADYRDLPAD 116

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 490826323  93 EQYDGIYTSASLLHAKRSVLPEIVKCIHRALKTSGTV 129
Cdd:COG2230  117 GQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRL 153
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 9-129 2.11e-08

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: 50.76  E-value: 2.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826323   9 YAQNAETYAARsvvnpklAEFLQHVA--PGGFILELGSGSGLDAKFMIENGFKV---DPTDGSYELAEEASRLLGQPVR- 82
Cdd:COG2226    1 FDRVAARYDGR-------EALLAALGlrPGARVLDLGCGTGRLALALAERGARVtgvDISPEMLELARERAAEAGLNVEf 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 490826323  83 -HMYFEDLD-AIEQYDGIYTSASLLHAKRsvLPEIVKCIHRALKTSGTV 129
Cdd:COG2226   74 vVGDAEDLPfPDGSFDLVISSFVLHHLPD--PERALAEIARVLKPGGRL 120
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
35-129 7.69e-08

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 48.28  E-value: 7.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826323  35 PGGFILELGSGSGLDAKFMIEN--GFKVDPTDGSYELAEEASRLLGQ-PVRHMYFEDLDAIEQYDGIYTSASLLHAKRsv 111
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARARARLPNvRFVVADLRDLDPPEPFDLVVSNAALHWLPD-- 78

                         90
                 ....*....|....*...
gi 490826323 112 LPEIVKCIHRALKTSGTV 129
Cdd:COG4106   79 HAALLARLAAALAPGGVL 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 39-133 1.47e-07

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: 47.81  E-value: 1.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826323  39 ILELGSGSGLDAKFMIENGFK----VDPTDGSYELAEEASRLLGQP---VRHMYFEDL--DAIEQYDGIYTSASLLHAKR 109
Cdd:cd02440    2 VLDLGCGTGALALALASGPGArvtgVDISPVALELARKAAAALLADnveVLKGDAEELppEADESFDVIISDPPLHHLVE 81

                         90       100
                 ....*....|....*....|....
gi 490826323 110 SVlPEIVKCIHRALKTSGTVWASF 133
Cdd:cd02440   82 DL-ARFLEEARRLLKPGGVLVLTL 104
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 40-130 5.02e-07

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 46.12  E-value: 5.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826323   40 LELGSGSGLDAKFMIENGFKV---DPTDGSYELAEEASRLLGQPVRHMYFEDLD-AIEQYDGIYTSASLLHAKRsvLPEI 115
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVtgvDISPEMLELAREKAPREGLTFVVGDAEDLPfPDNSFDLVLSSEVLHHVED--PERA 78

                          90
                  ....*....|....*
gi 490826323  116 VKCIHRALKTSGTVW 130
Cdd:pfam08241  79 LREIARVLKPGGILI 93
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 25-163 1.95e-06

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 45.88  E-value: 1.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826323   25 KLAEFLQHVAPGGFILELGSGSGLDAKFMIENGFKVDPTDGSYELAEeasRLLGQPVRHMYFEDLDAIEQ--YDGIYTSA 102
Cdd:pfam13489  12 LLLRLLPKLPSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIE---RALLNVRFDQFDEQEAAVPAgkFDVIVARE 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490826323  103 SLLHAKrsVLPEIVKCIHRALKTSGtvWASFKD-GSSEGYDQLGRYY----------NYMQAEELASLWRNC 163
Cdd:pfam13489  89 VLEHVP--DPPALLRQIAALLKPGG--LLLLSTpLASDEADRLLLEWpylrprnghiSLFSARSLKRLLEEA 156
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 26-129 3.14e-06

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 45.68  E-value: 3.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826323  26 LAEFLQHVAPGGFILELGSGSGLDAKFMIE-NGFKVDPTDGSYELAEEASRLLGQ------PVRHMYFEDLDAIEQ--YD 96
Cdd:COG0500   17 LLALLERLPKGGRVLDLGCGTGRNLLALAArFGGRVIGIDLSPEAIALARARAAKaglgnvEFLVADLAELDPLPAesFD 96

                         90       100       110
                 ....*....|....*....|....*....|...
gi 490826323  97 GIYTSASLLHAKRSVLPEIVKCIHRALKTSGTV 129
Cdd:COG0500   97 LVVAFGVLHHLPPEEREALLRELARALKPGGVL 129
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 40-124 9.16e-04

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 36.96  E-value: 9.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826323   40 LELGSGSGLDAKFMIEN--GFKVDPTDGSYELAEEASRLL----GQPVRHMYFEDLDAIEQ----YDGIYTSASLLHAKR 109
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlpGLEYTGLDISPAALEAARERLaalgLLNAVRVELFQLDLGELdpgsFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*
gi 490826323  110 svLPEIVKCIHRALK 124
Cdd:pfam08242  81 --PRAVLRNIRRLLK 93
 
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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