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Conserved domains on  [gi|1055322809|ref|WP_066988242|]
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bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG [Methylomonas lenta]

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 ...
 36-148 2.69e-12

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: 62.34  E-value: 2.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322809  36 WEKFLKR--NRCIGAEvKRVLEPMCGmaEGYeiLSKNLIQN-FVYQGFDYSENMVEIARTQNPLLKIEW--NDVTTYQAS 110
Cdd:COG2227    10 WDRRLAAllARLLPAG-GRVLDVGCG--TGR--LALALARRgADVTGVDISPEALEIARERAAELNVDFvqGDLEDLPLE 84

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1055322809 111 GDLFDLIILIGGLHHVYSRtQDILKNLGNSLLPGGYFL 148
Cdd:COG2227    85 DGSFDLVICSEVLEHLPDP-AALLRELARLLKPGGLLL 121
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 36-148 2.69e-12

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: 62.34  E-value: 2.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322809  36 WEKFLKR--NRCIGAEvKRVLEPMCGmaEGYeiLSKNLIQN-FVYQGFDYSENMVEIARTQNPLLKIEW--NDVTTYQAS 110
Cdd:COG2227    10 WDRRLAAllARLLPAG-GRVLDVGCG--TGR--LALALARRgADVTGVDISPEALEIARERAAELNVDFvqGDLEDLPLE 84

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1055322809 111 GDLFDLIILIGGLHHVYSRtQDILKNLGNSLLPGGYFL 148
Cdd:COG2227    85 DGSFDLVICSEVLEHLPDP-AALLRELARLLKPGGLLL 121
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 53-145 3.24e-08

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 50.25  E-value: 3.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322809  53 VLEPMCGmaEGYeiLSKNLIQNFVYQ--GFDYSENMVEIARTQNPL--LKIEW--NDVTTYQASGDLFDLIILIGGLHHV 126
Cdd:pfam13649   1 VLDLGCG--TGR--LTLALARRGGARvtGVDLSPEMLERARERAAEagLNVEFvqGDAEDLPFPDGSFDLVVSSGVLHHL 76

                          90       100
                  ....*....|....*....|
gi 1055322809 127 -YSRTQDILKNLGNSLLPGG 145
Cdd:pfam13649  77 pDPDLEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 52-148 1.81e-04

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: 39.72  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322809  52 RVLEPMCGmaEGYEILSKNLIQNFVYQGFDYSENMVEIARTQNPLL---KIEWN--DVTTYQASGDL-FDLIILIGGLHH 125
Cdd:cd02440     1 RVLDLGCG--TGALALALASGPGARVTGVDISPVALELARKAAAALladNVEVLkgDAEELPPEADEsFDVIISDPPLHH 78

                          90       100
                  ....*....|....*....|...
gi 1055322809 126 VYSRTQDILKNLGNSLLPGGYFL 148
Cdd:cd02440    79 LVEDLARFLEEARRLLKPGGVLV 101
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 36-148 2.69e-12

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: 62.34  E-value: 2.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322809  36 WEKFLKR--NRCIGAEvKRVLEPMCGmaEGYeiLSKNLIQN-FVYQGFDYSENMVEIARTQNPLLKIEW--NDVTTYQAS 110
Cdd:COG2227    10 WDRRLAAllARLLPAG-GRVLDVGCG--TGR--LALALARRgADVTGVDISPEALEIARERAAELNVDFvqGDLEDLPLE 84

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1055322809 111 GDLFDLIILIGGLHHVYSRtQDILKNLGNSLLPGGYFL 148
Cdd:COG2227    85 DGSFDLVICSEVLEHLPDP-AALLRELARLLKPGGLLL 121
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
52-148 2.25e-09

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 53.29  E-value: 2.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322809  52 RVLEPMCGMAEGYEILSKNLIQNFVYqGFDYSENMVEIARTQNPLLKIEWNDVTTYQASGDlFDLIILIGGLHHVYSRtQ 131
Cdd:COG4106     4 RVLDLGCGTGRLTALLAERFPGARVT-GVDLSPEMLARARARLPNVRFVVADLRDLDPPEP-FDLVVSNAALHWLPDH-A 80

                          90
                  ....*....|....*..
gi 1055322809 132 DILKNLGNSLLPGGYFL 148
Cdd:COG4106    81 ALLARLAAALAPGGVLA 97
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 53-145 3.24e-08

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 50.25  E-value: 3.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322809  53 VLEPMCGmaEGYeiLSKNLIQNFVYQ--GFDYSENMVEIARTQNPL--LKIEW--NDVTTYQASGDLFDLIILIGGLHHV 126
Cdd:pfam13649   1 VLDLGCG--TGR--LTLALARRGGARvtGVDLSPEMLERARERAAEagLNVEFvqGDAEDLPFPDGSFDLVVSSGVLHHL 76

                          90       100
                  ....*....|....*....|
gi 1055322809 127 -YSRTQDILKNLGNSLLPGG 145
Cdd:pfam13649  77 pDPDLEAALREIARVLKPGG 96
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
3-165 4.03e-08

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 51.92  E-value: 4.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322809   3 KLVEQQREHFNEISEKYFEARKHPNHLLLKKLIWEKFLKRnrCIGAEVKRVLEPMCG---MAE-----GYEILsknliqn 74
Cdd:COG4976     2 ALDAYVEALFDQYADSYDAALVEDLGYEAPALLAEELLAR--LPPGPFGRVLDLGCGtglLGEalrprGYRLT------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322809  75 fvyqGFDYSENMVEIARTQNPLLKIEWNDVTTYQASGDLFDLIILIGGLHHVySRTQDILKNLGNSLLPGGYFL----SF 150
Cdd:COG4976    73 ----GVDLSEEMLAKAREKGVYDRLLVADLADLAEPDGRFDLIVAADVLTYL-GDLAAVFAGVARALKPGGLFIfsveDA 147

                         170
                  ....*....|....*.
gi 1055322809 151 EPTHDNWLARR-IRQR 165
Cdd:COG4976   148 DGSGRYAHSLDyVRDL 163
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 51-164 7.69e-07

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: 47.30  E-value: 7.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322809  51 KRVLEPMCGmaEGYeiLSKNLIQNF--VYqGFDYSENMVEIARTQNPLLKIewnDVTTYQASG-DL------FDLIILIG 121
Cdd:COG2226    24 ARVLDLGCG--TGR--LALALAERGarVT-GVDISPEMLELARERAAEAGL---NVEFVVGDAeDLpfpdgsFDLVISSF 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1055322809 122 GLHHVySRTQDILKNLGNSLLPGGYFLSFE--PTHDNWLARRIRQ 164
Cdd:COG2226    96 VLHHL-PDPERALAEIARVLKPGGRLVVVDfsPPDLAELEELLAE 139
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 58-147 1.29e-06

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 45.82  E-value: 1.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322809  58 CGMAEGYEILSKNLIQNFVYqGFDYSENMVEIARTQ---NPLLKIEWNDVTTYQASGDL---FDLIILIGGLHHVySRTQ 131
Cdd:pfam08242   5 CGTGTLLRALLEALPGLEYT-GLDISPAALEAARERlaaLGLLNAVRVELFQLDLGELDpgsFDVVVASNVLHHL-ADPR 82

                          90
                  ....*....|....*.
gi 1055322809 132 DILKNLGNSLLPGGYF 147
Cdd:pfam08242  83 AVLRNIRRLLKPGGVL 98
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 51-194 1.41e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 46.64  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322809  51 KRVLEPMCGmaEGYE--ILSKNLIQNFVYQGFDYSENMVEIARTQNPLLKIEwnDVTTYQA---------SGDLFDLIIL 119
Cdd:pfam13847   5 MRVLDLGCG--TGHLsfELAEELGPNAEVVGIDISEEAIEKARENAQKLGFD--NVEFEQGdieelpellEDDKFDVVIS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1055322809 120 IGGLHHVYSrTQDILKNLGNSLLPGGYFLSFEPTHDNWLARRIRQ-RVYKSNDLFDDDTEQgfeypDLDRYFKNAG 194
Cdd:pfam13847  81 NCVLNHIPD-PDKVLQEILRVLKPGGRLIISDPDSLAELPAHVKEdSTYYAGCVGGAILKK-----KLYELLEEAG 150
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 36-198 1.86e-06

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 46.65  E-value: 1.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322809  36 WEKFLKRNRCIGAEVKRVLEPMCGmaegYEILSKNL-IQNFVYQGFDYSENMVEIARTQNPLlkiEWNDVTTYQASGDLF 114
Cdd:pfam13489   9 LADLLLRLLPKLPSPGRVLDFGCG----TGIFLRLLrAQGFSVTGVDPSPIAIERALLNVRF---DQFDEQEAAVPAGKF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322809 115 DLIILIGGLHHVysrtQD---ILKNLGNSLLPGGYFLsfeptHDNWLARRIRQRVYKSNDLFDDDTEQGFEYP--DLDRY 189
Cdd:pfam13489  82 DVIVAREVLEHV----PDppaLLRQIAALLKPGGLLL-----LSTPLASDEADRLLLEWPYLRPRNGHISLFSarSLKRL 152


                  ....*....
gi 1055322809 190 FKNAGYEKV 198
Cdd:pfam13489 153 LEEAGFEVV 161
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 54-148 8.22e-06

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 43.42  E-value: 8.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322809  54 LEPMCGMAEGYEILSKNLIQnfVYqGFDYSENMVEIARTQNPLLKIEW--NDVTTYQASGDLFDLIILIGGLHHVYSRtQ 131
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR--VT-GVDISPEMLELAREKAPREGLTFvvGDAEDLPFPDNSFDLVLSSEVLHHVEDP-E 76

                          90
                  ....*....|....*..
gi 1055322809 132 DILKNLGNSLLPGGYFL 148
Cdd:pfam08241  77 RALREIARVLKPGGILI 93
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 74-193 8.79e-05

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 42.21  E-value: 8.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322809  74 NFVYQGFDYSENMVEIAR---TQNPLLKIEWN--DVTTYQASGDL-FDLIILIGGLHHV-YSRTQDILKNLGNSLLPGGY 146
Cdd:COG0500    49 GGRVIGIDLSPEAIALARaraAKAGLGNVEFLvaDLAELDPLPAEsFDLVVAFGVLHHLpPEEREALLRELARALKPGGV 128

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1055322809 147 FLsFEPTHDNWlARRIRQRVYKSNDLFDDDTEQGFEYPDLDRYFKNA 193
Cdd:COG0500   129 LL-LSASDAAA-ALSLARLLLLATASLLELLLLLRLLALELYLRALL 173
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 52-148 1.81e-04

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: 39.72  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055322809  52 RVLEPMCGmaEGYEILSKNLIQNFVYQGFDYSENMVEIARTQNPLL---KIEWN--DVTTYQASGDL-FDLIILIGGLHH 125
Cdd:cd02440     1 RVLDLGCG--TGALALALASGPGARVTGVDISPVALELARKAAAALladNVEVLkgDAEELPPEADEsFDVIISDPPLHH 78

                          90       100
                  ....*....|....*....|...
gi 1055322809 126 VYSRTQDILKNLGNSLLPGGYFL 148
Cdd:cd02440    79 LVEDLARFLEEARRLLKPGGVLV 101
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 79-148 5.53e-03

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 36.45  E-value: 5.53e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1055322809  79 GFDYSENMVEIARTQ------NPLLKIEWNDVTTYQASGDlFDLIILIGGLHHV-YSRTQDILKNLGNSLLPGGYFL 148
Cdd:COG2230    79 GVTLSPEQLEYARERaaeaglADRVEVRLADYRDLPADGQ-FDAIVSIGMFEHVgPENYPAYFAKVARLLKPGGRLL 154
 
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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