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Conserved domains on  [gi|1589934837|ref|WP_131354709|]
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bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG [Aquitalea sp. USM4]

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 ...
 36-150 1.90e-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: 72.36  E-value: 1.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589934837  36 KELFQTGQTAICLADGEGRNSVWLAGQGLKVTAVEFSVTALHKARslAAARQVCVDFQHGDMLDSQWPDcsehNRYDWVI 115
Cdd:COG2227    19 ARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIAR--ERAAELNVDFVQGDLEDLPLED----GSFDLVI 92

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1589934837 116 A--VFIQFADPEQrqkQFADMLNLCKPGGHILLLGYN 150
Cdd:COG2227    93 CseVLEHLPDPAA---LLRELARLLKPGGLLLLSTPN 126
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 36-150 1.90e-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: 72.36  E-value: 1.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589934837  36 KELFQTGQTAICLADGEGRNSVWLAGQGLKVTAVEFSVTALHKARslAAARQVCVDFQHGDMLDSQWPDcsehNRYDWVI 115
Cdd:COG2227    19 ARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIAR--ERAAELNVDFVQGDLEDLPLED----GSFDLVI 92

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1589934837 116 A--VFIQFADPEQrqkQFADMLNLCKPGGHILLLGYN 150
Cdd:COG2227    93 CseVLEHLPDPAA---LLRELARLLKPGGLLLLSTPN 126
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 51-142 9.19e-16

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 69.90  E-value: 9.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589934837  51 GEGRNSVWLAGQ-GLKVTAVEFSVTALHKARSLAAARQVCVDFQHGDMLDSQWPDcsehNRYDWVIAVF-IQFADPEQRQ 128
Cdd:pfam13649   7 GTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPD----GSFDLVVSSGvLHHLPDPDLE 82

                          90
                  ....*....|....
gi 1589934837 129 KQFADMLNLCKPGG 142
Cdd:pfam13649  83 AALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 44-146 8.67e-06

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: 43.19  E-value: 8.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589934837  44 TAICLADGEGRNSVWLA-GQGLKVTAVEFSVTALHKARSLAAARQ-VCVDFQHGDMLDsqwPDCSEHNRYDWVIAVFIQF 121
Cdd:cd02440     1 RVLDLGCGTGALALALAsGPGARVTGVDISPVALELARKAAAALLaDNVEVLKGDAEE---LPPEADESFDVIISDPPLH 77

                          90       100
                  ....*....|....*....|....*
gi 1589934837 122 ADPEQRQKQFADMLNLCKPGGHILL 146
Cdd:cd02440    78 HLVEDLARFLEEARRLLKPGGVLVL 102
PRK12335 PRK12335
tellurite resistance protein TehB; Provisional
 51-146 5.28e-05

tellurite resistance protein TehB; Provisional


Pssm-ID: 183450 [Multi-domain]  Cd Length: 287  Bit Score: 43.01  E-value: 5.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589934837  51 GEGRNSVWLAGQGLKVTAVEFSVTALHKARSLAAARQVCVDFQHGDMLDSQWPDCsehnrYDWVIA-VFIQFADPEQRQK 129
Cdd:PRK12335  130 GQGRNSLYLALLGFDVTAVDINQQSLENLQEIAEKENLNIRTGLYDINSASIQEE-----YDFILStVVLMFLNRERIPA 204

                          90
                  ....*....|....*..
gi 1589934837 130 QFADMLNLCKPGGHILL 146
Cdd:PRK12335  205 IIKNMQEHTNPGGYNLI 221
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 36-150 1.90e-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: 72.36  E-value: 1.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589934837  36 KELFQTGQTAICLADGEGRNSVWLAGQGLKVTAVEFSVTALHKARslAAARQVCVDFQHGDMLDSQWPDcsehNRYDWVI 115
Cdd:COG2227    19 ARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIAR--ERAAELNVDFVQGDLEDLPLED----GSFDLVI 92

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1589934837 116 A--VFIQFADPEQrqkQFADMLNLCKPGGHILLLGYN 150
Cdd:COG2227    93 CseVLEHLPDPAA---LLRELARLLKPGGLLLLSTPN 126
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 51-142 9.19e-16

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 69.90  E-value: 9.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589934837  51 GEGRNSVWLAGQ-GLKVTAVEFSVTALHKARSLAAARQVCVDFQHGDMLDSQWPDcsehNRYDWVIAVF-IQFADPEQRQ 128
Cdd:pfam13649   7 GTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPD----GSFDLVVSSGvLHHLPDPDLE 82

                          90
                  ....*....|....
gi 1589934837 129 KQFADMLNLCKPGG 142
Cdd:pfam13649  83 AALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 40-155 1.83e-15

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: 70.41  E-value: 1.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589934837  40 QTGQTAICLADGEGRNSVWLAGQGLKVTAVEFSVTALHKARSLAAARQVCVDFQHGDMLDSQWPDcsehNRYDWVIAVF- 118
Cdd:COG2226    21 RPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPFPD----GSFDLVISSFv 96

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1589934837 119 IQFAdpEQRQKQFADMLNLCKPGGHILLLGYNPRQLA 155
Cdd:COG2226    97 LHHL--PDPERALAEIARVLKPGGRLVVVDFSPPDLA 131
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 11-184 5.50e-15

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 70.33  E-value: 5.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589934837  11 WEQRYQSAGDdflfgvEPNEYLASKKELFQTGQTAICLADGEGRNSVWLAGQ-GLKVTAVEFSVTALHKARSLAAARQVC 89
Cdd:COG0500     2 WDSYYSDELL------PGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARfGGRVIGIDLSPEAIALARARAAKAGLG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589934837  90 -VDFQHGDMLDsqwPDCSEHNRYDWVIAVF-IQFADPEQRQKQFADMLNLCKPGGHILLLGYNPRQ------LAHGTGGP 161
Cdd:COG0500    76 nVEFLVADLAE---LDPLPAESFDLVVAFGvLHHLPPEEREALLRELARALKPGGVLLLSASDAAAalslarLLLLATAS 152

                         170       180
                  ....*....|....*....|...
gi 1589934837 162 SALDHLYTPELLREAFSACKLIE 184
Cdd:COG0500   153 LLELLLLLRLLALELYLRALLAA 175
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 30-146 7.79e-13

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 63.80  E-value: 7.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589934837  30 EYLASKKELfQTGQTAICLADGEGRNSVWLAGQ-GLKVTAVEFSVTALHKARSLAAARQV--CVDFQHGDMLDSQWPdcs 106
Cdd:COG2230    41 DLILRKLGL-KPGMRVLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLEYARERAAEAGLadRVEVRLADYRDLPAD--- 116

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1589934837 107 ehNRYD--WVIAVFIQFaDPEQRQKQFADMLNLCKPGGHILL 146
Cdd:COG2230   117 --GQFDaiVSIGMFEHV-GPENYPAYFAKVARLLKPGGRLLL 155
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 51-146 4.53e-09

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 51.90  E-value: 4.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589934837  51 GEGRNSVWLAGQGLKVTAVEFSVTALHKARSLAAARQvcVDFQHGDMLDSQWPDcsehNRYD--WVIAVFIQFADPEqrq 128
Cdd:pfam08241   6 GTGLLTELLARLGARVTGVDISPEMLELAREKAPREG--LTFVVGDAEDLPFPD----NSFDlvLSSEVLHHVEDPE--- 76

                          90
                  ....*....|....*...
gi 1589934837 129 KQFADMLNLCKPGGHILL 146
Cdd:pfam08241  77 RALREIARVLKPGGILII 94
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
51-146 5.82e-08

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 50.77  E-value: 5.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589934837  51 GEGRNSVWLAGQGLKVTAVEFSVTALHKARslaaARQVCVDFQHGDMLDSQWPDcsehNRYDWVIA--VFIQFADPEQRq 128
Cdd:COG4976    56 GTGLLGEALRPRGYRLTGVDLSEEMLAKAR----EKGVYDRLLVADLADLAEPD----GRFDLIVAadVLTYLGDLAAV- 126

                          90
                  ....*....|....*...
gi 1589934837 129 kqFADMLNLCKPGGHILL 146
Cdd:COG4976   127 --FAGVARALKPGGLFIF 142
TPMT pfam05724
Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase ...
 51-198 1.17e-06

Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase proteins from both eukaryotes and prokaryotes. Thiopurine S-methyltransferase (TPMT) is a cytosolic enzyme that catalyzes S-methylation of aromatic and heterocyclic sulfhydryl compounds, including anticancer and immunosuppressive thiopurines.


Pssm-ID: 399030  Cd Length: 218  Bit Score: 47.42  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589934837  51 GEGRNSVWLAGQGLKVTAVEFSVTALHKARSLA---------AARQVC----VDFQHGDMLDsqWPDcSEHNRYDWVI-- 115
Cdd:pfam05724  47 GKALDMVWLAEQGHFVVGVEISELAVEKFFAEAglsppitelSGFKEYssgnISLYCGDFFT--LPR-EELGKFDLIYdr 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589934837 116 AVFIQFaDPEQRQKQFADMLNLCKPGGHILLLGYNPRQLAHgTGGPSALDHlytpELLREAFSACKLIELQEYEKVLQEG 195
Cdd:pfam05724 124 AALCAL-PPEMRPRYAKQMYELLPPGGRGLLITLDYPQTDH-EGPPFSVPA----AELEALFGGGWKVAELEREDALVPE 197


                  ...
gi 1589934837 196 MRH 198
Cdd:pfam05724 198 PRF 200
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 44-146 8.67e-06

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: 43.19  E-value: 8.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589934837  44 TAICLADGEGRNSVWLA-GQGLKVTAVEFSVTALHKARSLAAARQ-VCVDFQHGDMLDsqwPDCSEHNRYDWVIAVFIQF 121
Cdd:cd02440     1 RVLDLGCGTGALALALAsGPGARVTGVDISPVALELARKAAAALLaDNVEVLKGDAEE---LPPEADESFDVIISDPPLH 77

                          90       100
                  ....*....|....*....|....*
gi 1589934837 122 ADPEQRQKQFADMLNLCKPGGHILL 146
Cdd:cd02440    78 HLVEDLARFLEEARRLLKPGGVLVL 102
PRK12335 PRK12335
tellurite resistance protein TehB; Provisional
 51-146 5.28e-05

tellurite resistance protein TehB; Provisional


Pssm-ID: 183450 [Multi-domain]  Cd Length: 287  Bit Score: 43.01  E-value: 5.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589934837  51 GEGRNSVWLAGQGLKVTAVEFSVTALHKARSLAAARQVCVDFQHGDMLDSQWPDCsehnrYDWVIA-VFIQFADPEQRQK 129
Cdd:PRK12335  130 GQGRNSLYLALLGFDVTAVDINQQSLENLQEIAEKENLNIRTGLYDINSASIQEE-----YDFILStVVLMFLNRERIPA 204

                          90
                  ....*....|....*..
gi 1589934837 130 QFADMLNLCKPGGHILL 146
Cdd:PRK12335  205 IIKNMQEHTNPGGYNLI 221
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
51-146 5.32e-05

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 42.41  E-value: 5.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589934837  51 GEGRNSVWLAGQGLKVTAVEFSVTALHKARSLAAARQVcvdfqhgDMLDSQWPDCSEHN---RYDWVIA-VFIQFADPEQ 126
Cdd:PRK11207   40 GNGRNSLYLAANGFDVTAWDKNPMSIANLERIKAAENL-------DNLHTAVVDLNNLTfdgEYDFILStVVLMFLEAKT 112

                          90       100
                  ....*....|....*....|
gi 1589934837 127 RQKQFADMLNLCKPGGHILL 146
Cdd:PRK11207  113 IPGLIANMQRCTKPGGYNLI 132
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 51-144 5.05e-04

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 38.12  E-value: 5.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589934837  51 GEGRNSVWLAGQ--GLKVTAVEFSVTALHKARSLAAARQ----VCVDFQHGDMLDSQWPdcsehnRYDWVIAVFIqFADP 124
Cdd:pfam08242   6 GTGTLLRALLEAlpGLEYTGLDISPAALEAARERLAALGllnaVRVELFQLDLGELDPG------SFDVVVASNV-LHHL 78

                          90       100
                  ....*....|....*....|
gi 1589934837 125 EQRQKQFADMLNLCKPGGHI 144
Cdd:pfam08242  79 ADPRAVLRNIRRLLKPGGVL 98
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 51-160 1.64e-03

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 38.28  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589934837  51 GEGRNSVWLAGQGLKVTAVEFSVTALHKARSLAAARQVC--VDFQHGDMldsqwpdCSEHNRYDWVIA--VFIQFadpeq 126
Cdd:PRK07580   73 GVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLAgnITFEVGDL-------ESLLGRFDTVVCldVLIHY----- 140

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1589934837 127 RQKQFADML-NLCKPGGHILLLGYNPRQLA----HGTGG 160
Cdd:PRK07580  141 PQEDAARMLaHLASLTRGSLIFTFAPYTPLlallHWIGG 179
 
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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