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Conserved domains on  [gi|1796551998|gb|QHG11068|]
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methyl transferase [Plasmopara viticola lesion associated polymycovirus 1]

Protein Classification

bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG( domain architecture ID 11454890)

bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG UbiG is a class I SAM-dependent methyltransferase that catalyzes both methylation steps in ubiquinone biosynthesis

EC:  2.1.1.222|2.1.1.64
Gene Ontology:  GO:0102208|GO:0008425|GO:0008689|GO:0032259|GO:0006744
PubMed:  10419476|11583838

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 ...
 116-249 1.39e-08

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: 53.48  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796551998 116 IHQYIRRsVRLAGARVLVLGSGSSKSTASLLNRGVlSATFVDTSAPALAALRNNIvetgvdAAVEVEYVCDDAwEYLKgL 195
Cdd:COG2227    14 LAALLAR-LLPAGGRVLDVGCGTGRLALALARRGA-DVTGVDISPEALEIARERA------AELNVDFVQGDL-EDLP-L 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1796551998 196 DTEQFDLIIALKCVGLIlssgPDRttHEMLDMVSDCLAPDGSFItnhhaaFSTP 249
Cdd:COG2227    84 EDGSFDLVICSEVLEHL----PDP--AALLRELARLLKPGGLLL------LSTP 125
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 116-249 1.39e-08

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: 53.48  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796551998 116 IHQYIRRsVRLAGARVLVLGSGSSKSTASLLNRGVlSATFVDTSAPALAALRNNIvetgvdAAVEVEYVCDDAwEYLKgL 195
Cdd:COG2227    14 LAALLAR-LLPAGGRVLDVGCGTGRLALALARRGA-DVTGVDISPEALEIARERA------AELNVDFVQGDL-EDLP-L 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1796551998 196 DTEQFDLIIALKCVGLIlssgPDRttHEMLDMVSDCLAPDGSFItnhhaaFSTP 249
Cdd:COG2227    84 EDGSFDLVICSEVLEHL----PDP--AALLRELARLLKPGGLLL------LSTP 125
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 131-236 1.46e-07

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 49.48  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796551998 131 VLVLGSGSSKSTASLLNRGVLSATFVDTSAPALAALRNNIVETGVDaaveVEYVCDDAWEYlkGLDTEQFDLIIALKCVG 210
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLN----VEFVQGDAEDL--PFPDGSFDLVVSSGVLH 74

                          90       100
                  ....*....|....*....|....*.
gi 1796551998 211 LIlssgPDRTTHEMLDMVSDCLAPDG 236
Cdd:pfam13649  75 HL----PDPDLEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 130-240 4.43e-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: 40.11  E-value: 4.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796551998 130 RVLVLGSGSSKSTASLLNRGVLSATFVDTSAPALAALRNNIVEtgvDAAVEVEYVCDDaWEYLKGLDTEQFDLIIalkCV 209
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAA---LLADNVEVLKGD-AEELPPEADESFDVII---SD 73

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1796551998 210 GLILSSGPDRttHEMLDMVSDCLAPDGSFIT 240
Cdd:cd02440    74 PPLHHLVEDL--ARFLEEARRLLKPGGVLVL 102
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 116-249 1.39e-08

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: 53.48  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796551998 116 IHQYIRRsVRLAGARVLVLGSGSSKSTASLLNRGVlSATFVDTSAPALAALRNNIvetgvdAAVEVEYVCDDAwEYLKgL 195
Cdd:COG2227    14 LAALLAR-LLPAGGRVLDVGCGTGRLALALARRGA-DVTGVDISPEALEIARERA------AELNVDFVQGDL-EDLP-L 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1796551998 196 DTEQFDLIIALKCVGLIlssgPDRttHEMLDMVSDCLAPDGSFItnhhaaFSTP 249
Cdd:COG2227    84 EDGSFDLVICSEVLEHL----PDP--AALLRELARLLKPGGLLL------LSTP 125
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 114-204 2.04e-08

23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]; 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440709 [Multi-domain]  Cd Length: 392  Bit Score: 56.73  E-value: 2.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796551998 114 RLIHQYIRRSVRlaGARVLVL----GSgsskstASL--LNRGVLSATFVDTSAPALAALRNNIVETGVDAavEVEYVCDD 187
Cdd:COG1092   205 RENRARVAELAK--GKRVLNLfsytGG------FSVhaAAGGAKSVTSVDLSATALEWAKENAALNGLDD--RHEFVQAD 274

                          90
                  ....*....|....*....
gi 1796551998 188 AWEYLKGLDT--EQFDLII 204
Cdd:COG1092   275 AFDWLRELARegERFDLII 293
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 108-239 6.87e-08

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 52.24  E-value: 6.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796551998 108 LEREQTRLIHQYIRRSVRLAGARVLVLGSGSSKSTASLLNRGVLSATFVDTSAPALAALRNNIVETGVDAAVEVEyVCDd 187
Cdd:COG2230    32 LEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYARERAAEAGLADRVEVR-LAD- 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1796551998 188 aweYLKGLDTEQFDLIIalkCVGLILSSGPDRTThEMLDMVSDCLAPDGSFI 239
Cdd:COG2230   110 ---YRDLPADGQFDAIV---SIGMFEHVGPENYP-AYFAKVARLLKPGGRLL 154
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 131-236 1.46e-07

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 49.48  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796551998 131 VLVLGSGSSKSTASLLNRGVLSATFVDTSAPALAALRNNIVETGVDaaveVEYVCDDAWEYlkGLDTEQFDLIIALKCVG 210
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLN----VEFVQGDAEDL--PFPDGSFDLVVSSGVLH 74

                          90       100
                  ....*....|....*....|....*.
gi 1796551998 211 LIlssgPDRTTHEMLDMVSDCLAPDG 236
Cdd:pfam13649  75 HL----PDPDLEAALREIARVLKPGG 96
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 86-243 1.56e-06

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 49.03  E-value: 1.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796551998  86 GVFSDER---GTEFLnspagihLRALEREqtrlihqyirrsvrlAGARVLVLGSGSskstasllnrGVLSA--------- 153
Cdd:COG2813    27 GVFSRDRldiGTRLL-------LEHLPEP---------------LGGRVLDLGCGY----------GVIGLalakrnpea 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796551998 154 --TFVDTSAPALAALRNNIVETGVDaavEVEYVCDDAweyLKGLDTEQFDLIIalkC-----VGLILSsgpDRTTHEMLD 226
Cdd:COG2813    75 rvTLVDVNARAVELARANAAANGLE---NVEVLWSDG---LSGVPDGSFDLIL---SnppfhAGRAVD---KEVAHALIA 142

                         170
                  ....*....|....*....
gi 1796551998 227 MVSDCLAPDGSF--ITNHH 243
Cdd:COG2813   143 DAARHLRPGGELwlVANRH 161
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 128-252 3.04e-06

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: 3.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796551998 128 GARVLVLGSGSSKSTASLLNRGVlSATFVDTSAPALAALRNNIVETGVDaaveVEYVCDDAwEYLkGLDTEQFDLIIAlk 207
Cdd:COG2226    23 GARVLDLGCGTGRLALALAERGA-RVTGVDISPEMLELARERAAEAGLN----VEFVVGDA-EDL-PFPDGSFDLVIS-- 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1796551998 208 CVGLILSSGPDRTTHEMLDMvsdcLAPDGSFITNHHAAFSTPEWE 252
Cdd:COG2226    94 SFVLHHLPDPERALAEIARV----LKPGGRLVVVDFSPPDLAELE 134
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 127-239 4.11e-06

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 47.99  E-value: 4.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796551998 127 AGARVLVLGSGSSKSTASLLNRGVLSATFVDTSAPALAALRNNIVETGVDaavEVEYVCDDAwEYLKGLDTEQFDLIIAL 206
Cdd:COG0500    26 KGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLG---NVEFLVADL-AELDPLPAESFDLVVAF 101

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1796551998 207 KCVGLIlssgPDRTTHEMLDMVSDCLAPDGSFI 239
Cdd:COG0500   102 GVLHHL----PPEEREALLRELARALKPGGVLL 130
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 130-240 4.43e-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: 40.11  E-value: 4.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796551998 130 RVLVLGSGSSKSTASLLNRGVLSATFVDTSAPALAALRNNIVEtgvDAAVEVEYVCDDaWEYLKGLDTEQFDLIIalkCV 209
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAA---LLADNVEVLKGD-AEELPPEADESFDVII---SD 73

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1796551998 210 GLILSSGPDRttHEMLDMVSDCLAPDGSFIT 240
Cdd:cd02440    74 PPLHHLVEDL--ARFLEEARRLLKPGGVLVL 102
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
127-239 1.41e-03

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 38.27  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796551998 127 AGARVLVLGSGSSKSTASLLNRGV-LSATFVDTSAPALAALRNNivetgvdaAVEVEYVCDDAWEYLKGldtEQFDLIIA 205
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERFPgARVTGVDLSPEMLARARAR--------LPNVRFVVADLRDLDPP---EPFDLVVS 69

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1796551998 206 lkcvGLILSSGPDRttHEMLDMVSDCLAPDGSFI 239
Cdd:COG4106    70 ----NAALHWLPDH--AALLARLAAALAPGGVLA 97
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
105-239 1.81e-03

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 40.54  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796551998 105 LRALEReqtrlihqyirrsVRLAGARVLVLGSGSskstasllnrGVLS----------ATFVDTSAPALAALRNNIVETG 174
Cdd:COG2264   139 LEALEK-------------LLKPGKTVLDVGCGS----------GILAiaaaklgakrVLAVDIDPVAVEAARENAELNG 195

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1796551998 175 VDAAVEVeYVCDdaweylkGLDTEQFDLIIA--LKcvGLILssgpdrtthEMLDMVSDCLAPDGSFI 239
Cdd:COG2264   196 VEDRIEV-VLGD-------LLEDGPYDLVVAniLA--NPLI---------ELAPDLAALLKPGGYLI 243
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 105-240 8.33e-03

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: 38.79  E-value: 8.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796551998 105 LRALEReqtrlihqyirrsVRLAGARVLVLGSGSS-KSTASLLnRGVLSATFVDTSAPALAALRNNIVETGVDAAVEVey 183
Cdd:pfam06325 152 LEALER-------------LVKPGESVLDVGCGSGiLAIAALK-LGAKKVVGVDIDPVAVRAAKENAELNGVEARLEV-- 215

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1796551998 184 vcddaweYL-KGLDTEQFDLIIALkcvglILSsgpdRTTHEMLDMVSDCLAPDGSFIT 240
Cdd:pfam06325 216 -------YLpGDLPKEKADVVVAN-----ILA----DPLIELAPDIYALVKPGGYLIL 257
 
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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