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Conserved domains on  [gi|446769041|ref|WP_000846297|]
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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 ...
 46-158 6.61e-28

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: 102.79  E-value: 6.61e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041  46 DENLVSNIQKERVSKGKVLELGCGPGRNAIYLATQGFDVTAVDLSVEGINWAKERalAKGVEIHFICNSIFNLEVQNE-F 124
Cdd:COG2227   11 DRRLAALLARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARER--AAELNVDFVQGDLEDLPLEDGsF 88

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446769041 125 DFVYDSGCLHHIPPHRRInyVDLIKNSLKSGGYF 158
Cdd:COG2227   89 DLVICSEVLEHLPDPAAL--LRELARLLKPGGLL 120
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 46-158 6.61e-28

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: 102.79  E-value: 6.61e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041  46 DENLVSNIQKERVSKGKVLELGCGPGRNAIYLATQGFDVTAVDLSVEGINWAKERalAKGVEIHFICNSIFNLEVQNE-F 124
Cdd:COG2227   11 DRRLAALLARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARER--AAELNVDFVQGDLEDLPLEDGsF 88

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446769041 125 DFVYDSGCLHHIPPHRRInyVDLIKNSLKSGGYF 158
Cdd:COG2227   89 DLVICSEVLEHLPDPAAL--LRELARLLKPGGLL 120
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 63-156 4.86e-26

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 96.86  E-value: 4.86e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041   63 VLELGCGPGRNAIYLATQ-GFDVTAVDLSVEGINWAKERALAKGVEIHFICNSIFNLEVQNE-FDFVYDSGCLHHIPPHR 140
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGsFDLVVSSGVLHHLPDPD 80

                          90
                  ....*....|....*.
gi 446769041  141 RINYVDLIKNSLKSGG 156
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
PRK12335 PRK12335
tellurite resistance protein TehB; Provisional
 56-157 3.11e-13

tellurite resistance protein TehB; Provisional


Pssm-ID: 183450 [Multi-domain]  Cd Length: 287  Bit Score: 67.28  E-value: 3.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041  56 ERVSKGKVLELGCGPGRNAIYLATQGFDVTAVDLSVEGINWAKERALAKGVEIHFICNSIFNLEVQNEFDFVYDSGCLHH 135
Cdd:PRK12335 117 QTVKPGKALDLGCGQGRNSLYLALLGFDVTAVDINQQSLENLQEIAEKENLNIRTGLYDINSASIQEEYDFILSTVVLMF 196

                         90       100
                 ....*....|....*....|....*
gi 446769041 136 IPPHRrinYVDLIKN---SLKSGGY 157
Cdd:PRK12335 197 LNRER---IPAIIKNmqeHTNPGGY 218
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 62-165 3.85e-11

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: 58.21  E-value: 3.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041  62 KVLELGCGPGRNAIYLATQGFD-VTAVDLSVEGINWAKERALAKGVE-IHFICNSIFNLEVQ--NEFDFVYDSGCLHHIP 137
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGArVTGVDISPVALELARKAAAALLADnVEVLKGDAEELPPEadESFDVIISDPPLHHLV 80

                         90       100
                 ....*....|....*....|....*...
gi 446769041 138 PHRRiNYVDLIKNSLKSGGYFGLTCFAA 165
Cdd:cd02440   81 EDLA-RFLEEARRLLKPGGVLVLTLVLA 107
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 48-210 3.77e-07

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: 49.59  E-value: 3.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041   48 NLVSNIQKERVSK-GKVLELGCGPGRNAIYLATQG--FDVTAVDLSVEGINWAKERAlakGVEIHFICNSIFNLEVQ-NE 123
Cdd:TIGR02072  22 RLLALLKEKGIFIpASVLDIGCGTGYLTRALLKRFpqAEFIALDISAGMLAQAKTKL---SENVQFICGDAEKLPLEdSS 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041  124 FDFVYDSGCLHHIPPHRRInyVDLIKNSLKSGGYFGLTCFAAGNLDERNGSeitdwdvyreWSLQGGLAYSEEKLREIFK 203
Cdd:TIGR02072  99 FDLIVSNLALQWCDDLSQA--LSELARVLKPGGLLAFSTFGPGTLHELRQS----------FGQHGLRYLSLDELKALLK 166


                  ....*...
gi 446769041  204 -EFEVIEI 210
Cdd:TIGR02072 167 nSFELLTL 174
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 46-158 6.61e-28

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: 102.79  E-value: 6.61e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041  46 DENLVSNIQKERVSKGKVLELGCGPGRNAIYLATQGFDVTAVDLSVEGINWAKERalAKGVEIHFICNSIFNLEVQNE-F 124
Cdd:COG2227   11 DRRLAALLARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARER--AAELNVDFVQGDLEDLPLEDGsF 88

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446769041 125 DFVYDSGCLHHIPPHRRInyVDLIKNSLKSGGYF 158
Cdd:COG2227   89 DLVICSEVLEHLPDPAAL--LRELARLLKPGGLL 120
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 26-165 6.84e-28

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 105.00  E-value: 6.84e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041  26 FWNEFYenrekdvPFFENVPDENLVSNIQKERvSKGKVLELGCGPGRNAIYLATQ-GFDVTAVDLSVEGINWAKERALAK 104
Cdd:COG0500    1 PWDSYY-------SDELLPGLAALLALLERLP-KGGRVLDLGCGTGRNLLALAARfGGRVIGIDLSPEAIALARARAAKA 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446769041 105 GVE-IHFICNSIFNLE--VQNEFDFVYDSGCLHHIPPHRRINYVDLIKNSLKSGGYFGLTCFAA 165
Cdd:COG0500   73 GLGnVEFLVADLAELDplPAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLLSASDA 136
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 62-162 6.82e-27

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 101.16  E-value: 6.82e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041  62 KVLELGCGPGRNAIYLATQ-GFDVTAVDLSVEGINWAKERALAKGVE--IHFICNSIFNLEVQNEFDFVYDSGCLHHIPP 138
Cdd:COG2230   54 RVLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLEYARERAAEAGLAdrVEVRLADYRDLPADGQFDAIVSIGMFEHVGP 133

                         90       100
                 ....*....|....*....|....
gi 446769041 139 HRRINYVDLIKNSLKSGGYFGLTC 162
Cdd:COG2230  134 ENYPAYFAKVARLLKPGGRLLLHT 157
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 63-156 4.86e-26

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 96.86  E-value: 4.86e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041   63 VLELGCGPGRNAIYLATQ-GFDVTAVDLSVEGINWAKERALAKGVEIHFICNSIFNLEVQNE-FDFVYDSGCLHHIPPHR 140
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGsFDLVVSSGVLHHLPDPD 80

                          90
                  ....*....|....*.
gi 446769041  141 RINYVDLIKNSLKSGG 156
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 61-170 1.63e-23

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: 91.98  E-value: 1.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041  61 GKVLELGCGPGRNAIYLATQGFDVTAVDLSVEGINWAKERALAKGVEIHFICNSIFNLEVQNE-FDFVYDSGCLHHIPPH 139
Cdd:COG2226   24 ARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPFPDGsFDLVISSFVLHHLPDP 103

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446769041 140 RRInyVDLIKNSLKSGGYFGLTCFAAGNLDE 170
Cdd:COG2226  104 ERA--LAEIARVLKPGGRLVVVDFSPPDLAE 132
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
61-158 7.79e-19

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 78.33  E-value: 7.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041  61 GKVLELGCGPGRNAIYLATQ--GFDVTAVDLSVEGInwakERALAKGVEIHFICNSIFNLEVQNEFDFVYDSGCLHHIPP 138
Cdd:COG4106    3 RRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEML----ARARARLPNVRFVVADLRDLDPPEPFDLVVSNAALHWLPD 78

                         90       100
                 ....*....|....*....|
gi 446769041 139 HRRInyVDLIKNSLKSGGYF 158
Cdd:COG4106   79 HAAL--LARLAAALAPGGVL 96
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 64-158 1.65e-18

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 77.32  E-value: 1.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041   64 LELGCGPGRNAIYLATQGFDVTAVDLSVEGINWAKERalAKGVEIHFICNSIFNLEVQ-NEFDFVYDSGCLHHIPPHRRI 142
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREK--APREGLTFVVGDAEDLPFPdNSFDLVLSSEVLHHVEDPERA 78

                          90
                  ....*....|....*.
gi 446769041  143 nyVDLIKNSLKSGGYF 158
Cdd:pfam08241  79 --LREIARVLKPGGIL 92
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
61-162 1.38e-16

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 74.65  E-value: 1.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041  61 GKVLELGCGPGRNAIYLATQGFDVTAVDLSVEGInwakERALAKGVEIHFICNSIFNLEVQNE-FDFVYDSGCLHHIPPH 139
Cdd:COG4976   48 GRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEML----AKAREKGVYDRLLVADLADLAEPDGrFDLIVAADVLTYLGDL 123

                         90       100
                 ....*....|....*....|...
gi 446769041 140 RRInyVDLIKNSLKSGGYFGLTC 162
Cdd:COG4976  124 AAV--FAGVARALKPGGLFIFSV 144
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 59-209 2.73e-16

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 73.62  E-value: 2.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041   59 SKGKVLELGCGPGRNAIYLATQGFDVTAVDLSVEGINWAKERALAKGVEIHFIcnsifnLEVQNEFDFVYDSGCLHHIPP 138
Cdd:pfam13489  22 SPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRFDQFDEQEA------AVPAGKFDVIVAREVLEHVPD 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446769041  139 HRRinYVDLIKNSLKSGGYFGLTCFAAGNLDERNGSEITDWDVYREW-SLqgglaYSEEKLREIFKE--FEVIE 209
Cdd:pfam13489  96 PPA--LLRQIAALLKPGGLLLLSTPLASDEADRLLLEWPYLRPRNGHiSL-----FSARSLKRLLEEagFEVVS 162
PRK12335 PRK12335
tellurite resistance protein TehB; Provisional
 56-157 3.11e-13

tellurite resistance protein TehB; Provisional


Pssm-ID: 183450 [Multi-domain]  Cd Length: 287  Bit Score: 67.28  E-value: 3.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041  56 ERVSKGKVLELGCGPGRNAIYLATQGFDVTAVDLSVEGINWAKERALAKGVEIHFICNSIFNLEVQNEFDFVYDSGCLHH 135
Cdd:PRK12335 117 QTVKPGKALDLGCGQGRNSLYLALLGFDVTAVDINQQSLENLQEIAEKENLNIRTGLYDINSASIQEEYDFILSTVVLMF 196

                         90       100
                 ....*....|....*....|....*
gi 446769041 136 IPPHRrinYVDLIKN---SLKSGGY 157
Cdd:PRK12335 197 LNRER---IPAIIKNmqeHTNPGGY 218
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
56-157 1.07e-12

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 64.37  E-value: 1.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041  56 ERVSKGKVLELGCGPGRNAIYLATQGFDVTAVDLSVEGINWAKERALAKGVE-IHFICNSIFNLEVQNEFDFVYDSGCLH 134
Cdd:PRK11207  27 KVVKPGKTLDLGCGNGRNSLYLAANGFDVTAWDKNPMSIANLERIKAAENLDnLHTAVVDLNNLTFDGEYDFILSTVVLM 106

                         90       100
                 ....*....|....*....|...
gi 446769041 135 HIPPHRRINYVDLIKNSLKSGGY 157
Cdd:PRK11207 107 FLEAKTIPGLIANMQRCTKPGGY 129
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 62-165 3.85e-11

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: 58.21  E-value: 3.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041  62 KVLELGCGPGRNAIYLATQGFD-VTAVDLSVEGINWAKERALAKGVE-IHFICNSIFNLEVQ--NEFDFVYDSGCLHHIP 137
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGArVTGVDISPVALELARKAAAALLADnVEVLKGDAEELPPEadESFDVIISDPPLHHLV 80

                         90       100
                 ....*....|....*....|....*...
gi 446769041 138 PHRRiNYVDLIKNSLKSGGYFGLTCFAA 165
Cdd:cd02440   81 EDLA-RFLEEARRLLKPGGVLVLTLVLA 107
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 64-158 1.28e-10

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 56.61  E-value: 1.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041   64 LELGCGPGRNAIYLATQ--GFDVTAVDLSVEGINWAKERALAKG----VEIHFICNSIFNLEvQNEFDFVYDSGCLHHIP 137
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlpGLEYTGLDISPAALEAARERLAALGllnaVRVELFQLDLGELD-PGSFDVVVASNVLHHLA 79

                          90       100
                  ....*....|....*....|.
gi 446769041  138 PHRRInyVDLIKNSLKSGGYF 158
Cdd:pfam08242  80 DPRAV--LRNIRRLLKPGGVL 98
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 59-204 2.14e-10

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 57.43  E-value: 2.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041   59 SKGKVLELGCGPGRNAIYLATQGF---DVTAVDLSVEGINWAKERALAKGVE-IHFICNSIFNLEVQ---NEFDFVYDSG 131
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGpnaEVVGIDISEEAIEKARENAQKLGFDnVEFEQGDIEELPELledDKFDVVISNC 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446769041  132 CLHHIPPHRRInyVDLIKNSLKSGGYFgltCFAAGNLDERNGSEITDWDVYREWSLQGglAYSEEKLREIFKE 204
Cdd:pfam13847  83 VLNHIPDPDKV--LQEILRVLKPGGRL---IISDPDSLAELPAHVKEDSTYYAGCVGG--AILKKKLYELLEE 148
TehB pfam03848
Tellurite resistance protein TehB;
58-157 4.58e-10

Tellurite resistance protein TehB;


Pssm-ID: 397776  Cd Length: 193  Bit Score: 57.17  E-value: 4.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041   58 VSKGKVLELGCGPGRNAIYLATQGFDVTAVD---LSVEGINWAKERALAKGveIHFICNSIFNLEVQNEFDFVYDSGCLH 134
Cdd:pfam03848  29 VKPGKVLDLGCGQGRNSLYLSLLGYDVTAWDkneNSIANLQRIKEKENLDN--IHTALYDINNATIDENYDFILSTVVLM 106

                          90       100
                  ....*....|....*....|...
gi 446769041  135 HIPPHRRINYVDLIKNSLKSGGY 157
Cdd:pfam03848 107 FLEPERIPGIIANMQECTNPGGY 129
TPMT pfam05724
Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase ...
 61-156 3.83e-08

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: 52.04  E-value: 3.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041   61 GKVLELGCGPGRNAIYLATQGFDVTAVDLSVEGINWA----------KERALAK---GVEIHFICNSIFNLEVQN--EFD 125
Cdd:pfam05724  39 LRVLVPLCGKALDMVWLAEQGHFVVGVEISELAVEKFfaeaglsppiTELSGFKeysSGNISLYCGDFFTLPREElgKFD 118

                          90       100       110
                  ....*....|....*....|....*....|.
gi 446769041  126 FVYDSGCLHHIPPHRRINYVDLIKNSLKSGG 156
Cdd:pfam05724 119 LIYDRAALCALPPEMRPRYAKQMYELLPPGG 149
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 48-210 3.77e-07

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: 49.59  E-value: 3.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041   48 NLVSNIQKERVSK-GKVLELGCGPGRNAIYLATQG--FDVTAVDLSVEGINWAKERAlakGVEIHFICNSIFNLEVQ-NE 123
Cdd:TIGR02072  22 RLLALLKEKGIFIpASVLDIGCGTGYLTRALLKRFpqAEFIALDISAGMLAQAKTKL---SENVQFICGDAEKLPLEdSS 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041  124 FDFVYDSGCLHHIPPHRRInyVDLIKNSLKSGGYFGLTCFAAGNLDERNGSeitdwdvyreWSLQGGLAYSEEKLREIFK 203
Cdd:TIGR02072  99 FDLIVSNLALQWCDDLSQA--LSELARVLKPGGLLAFSTFGPGTLHELRQS----------FGQHGLRYLSLDELKALLK 166


                  ....*...
gi 446769041  204 -EFEVIEI 210
Cdd:TIGR02072 167 nSFELLTL 174
PRK06202 PRK06202
hypothetical protein; Provisional
 63-138 6.83e-07

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 48.46  E-value: 6.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041  63 VLELGCGPGRNAIYLA----TQGFD--VTAVDLSVEGINWAKERALAKGVEIHFICNSIFNLEVQnEFDFVYDSGCLHHI 136
Cdd:PRK06202  64 LLDIGCGGGDLAIDLArwarRDGLRleVTAIDPDPRAVAFARANPRRPGVTFRQAVSDELVAEGE-RFDVVTSNHFLHHL 142


                 ..
gi 446769041 137 PP 138
Cdd:PRK06202 143 DD 144
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 63-127 8.06e-07

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 48.29  E-value: 8.06e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446769041  63 VLELGCGPGRNAIYLATQGFDVTAVDLSVEGINWAKERALAKGV--EIHFICNSifnLE-VQNEFDFV 127
Cdd:PRK07580  67 ILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLagNITFEVGD---LEsLLGRFDTV 131
PRK08317 PRK08317
hypothetical protein; Provisional
 58-137 1.72e-06

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 47.62  E-value: 1.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041  58 VSKG-KVLELGCGPGRNAIYLATQ---GFDVTAVDLSVEGINWAKERALAKGVEIHFICNSIFNLEVQNE-FDFVYDSGC 132
Cdd:PRK08317  17 VQPGdRVLDVGCGPGNDARELARRvgpEGRVVGIDRSEAMLALAKERAAGLGPNVEFVRGDADGLPFPDGsFDAVRSDRV 96


                 ....*
gi 446769041 133 LHHIP 137
Cdd:PRK08317  97 LQHLE 101
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 54-212 5.29e-06

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 46.31  E-value: 5.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041  54 QKERVSKGKVLELGCGPGRNAIYLATQ--GFDVTAVDLSVEGINWAKE-RALAKGVEIHFICNSIFNLEVQNEFDFV--- 127
Cdd:PRK09328 103 ALLLKEPLRVLDLGTGSGAIALALAKErpDAEVTAVDISPEALAVARRnAKHGLGARVEFLQGDWFEPLPGGRFDLIvsn 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041 128 --Y-DSGCLHHIP-------PH-------------RRInyVDLIKNSLKSGGYFGLtcfaagnlderngsEItDWDvyre 184
Cdd:PRK09328 183 ppYiPEADIHLLQpevrdhePHlalfggedgldfyRRI--IEQAPRYLKPGGWLLL--------------EI-GYD---- 241

                        170       180       190
                 ....*....|....*....|....*....|
gi 446769041 185 wslQGglayseEKLREIFKE--FEVIEIRR 212
Cdd:PRK09328 242 ---QG------EAVRALLAAagFADVETRK 262
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
62-127 7.58e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 45.28  E-value: 7.58e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446769041  62 KVLELGCGPGRNAIYLATQGF-DVTAVDLSVEGINWAKERALAKGVEIHFICNSIFNLEVQNEFDFV 127
Cdd:COG2263   48 TVLDLGCGTGMLAIGAALLGAkKVVGVDIDPEALEIARENAERLGVRVDFIRADVTRIPLGGSVDTV 114
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 63-103 2.13e-05

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 44.36  E-value: 2.13e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 446769041  63 VLELGCGPGRNAIYLATQGFDVTAVDLSVEGINWAKERALA 103
Cdd:PRK10258  46 VLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQARQKDAA 86
TrmB COG0220
tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 ...
 63-188 2.47e-05

tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 N7-methylase TrmB is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439990  Cd Length: 204  Bit Score: 43.59  E-value: 2.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041  63 VLELGCGPGRNAIYLATQ--GFDVTAVDLSVEGINWAKERALAKGVE-IHFIC---NSIFNLEVQNEFDFVYdsgcL--- 133
Cdd:COG0220   36 VLEIGFGKGEFLVELAAAnpDINFIGIEVHEPGVAKALKKAEEEGLTnVRLLRgdaVELLELFPDGSLDRIY----Lnfp 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446769041 134 -------HHippHRRI---NYVDLIKNSLKSGGYFgltCFAagnlderngseiTDWDVYREWSLQ 188
Cdd:COG0220  112 dpwpkkrHH---KRRLvqpEFLALLARVLKPGGEL---HLA------------TDWEDYAEEMLE 158
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 62-156 7.59e-05

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 42.56  E-value: 7.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041  62 KVLELGCGPGRNAIYLATQGF-DVTAVDLSVEGINWAKERALAKGVEIHFICNSIFNLEVQNEFDFV------YDSgclh 134
Cdd:COG3897   73 RVLELGCGLGLVGIAAAKAGAaDVTATDYDPEALAALRLNAALNGVAITTRLGDWRDPPAAGGFDLIlggdvlYER---- 148

                         90       100
                 ....*....|....*....|..
gi 446769041 135 hiPPHRRInyVDLIKNSLKSGG 156
Cdd:COG3897  149 --DLAEPL--LPFLDRLAAPGG 166
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
63-112 1.96e-04

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 41.49  E-value: 1.96e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446769041  63 VLELGCGPGRNAIYLATQGFDVTAVDLSVEGINWAKERALAKGV--EIHFIC 112
Cdd:PRK11036  48 VLDAGGGEGQTAIKLAELGHQVILCDLSAEMIQRAKQAAEAKGVsdNMQFIH 99
PRK13256 PRK13256
thiopurine S-methyltransferase; Reviewed
 26-148 2.09e-04

thiopurine S-methyltransferase; Reviewed


Pssm-ID: 237318  Cd Length: 226  Bit Score: 41.17  E-value: 2.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041  26 FWNEFYENreKDVPFFENVPDENLVSNIQKERVSKGKV-LELGCGPGRNAIYLATQGFDVTAVDLSVEG---------IN 95
Cdd:PRK13256  11 YWLDRWQN--DDVGFCQESPNEFLVKHFSKLNINDSSVcLIPMCGCSIDMLFFLSKGVKVIGIELSEKAvlsffsqntIN 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446769041  96 W----AKERALAKGVEIHFICNSIFNL-EVQN---EFDFVYDSGCLHHIPPHRRINYVDLI 148
Cdd:PRK13256  89 YevihGNDYKLYKGDDIEIYVADIFNLpKIANnlpVFDIWYDRGAYIALPNDLRTNYAKMM 149
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
62-158 3.54e-04

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 40.99  E-value: 3.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041  62 KVLELGCGPGRNAIYLATQ-GFDVTAVDLSVEGINWAKERALAKGVEIHficnsifnL----EVQNEFDFVYDSGCLHHI 136
Cdd:PRK11705 170 RVLDIGCGWGGLARYAAEHyGVSVVGVTISAEQQKLAQERCAGLPVEIR--------LqdyrDLNGQFDRIVSVGMFEHV 241

                         90       100
                 ....*....|....*....|..
gi 446769041 137 PPHRRINYVDLIKNSLKSGGYF 158
Cdd:PRK11705 242 GPKNYRTYFEVVRRCLKPDGLF 263
PRK14968 PRK14968
putative methyltransferase; Provisional
 58-111 5.04e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 39.88  E-value: 5.04e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446769041  58 VSKGKVLELGCGPGRNAIYLATQGFDVTAVDLSVEGINWAKERALAKGVE---IHFI 111
Cdd:PRK14968  22 KKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRnngVEVI 78
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 49-127 5.09e-04

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 39.50  E-value: 5.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041   49 LVSNIQKERvsKGKVLELGCGPGRNAIYLA--TQGFDVTAVDLSVEGINWAKERALAKGVE-IHFICNSIFNLEVQNEFD 125
Cdd:pfam05175  23 LLEHLPKDL--SGKVLDLGCGAGVLGAALAkeSPDAELTMVDINARALESARENLAANGLEnGEVVASDVYSGVEDGKFD 100


                  ..
gi 446769041  126 FV 127
Cdd:pfam05175 101 LI 102
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 29-212 5.64e-04

Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 40.13  E-value: 5.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041  29 EFYenrekDVPFF--ENV----PD-ENLVSNIQK--ERVSKGKVLELGCGPGRNAIYLATQ--GFDVTAVDLSVEGINWA 97
Cdd:COG2890   78 EFY-----GLEFKvdPGVliprPEtEELVELALAllPAGAPPRVLDLGTGSGAIALALAKErpDARVTAVDISPDALAVA 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041  98 KERALAKGVE--IHFICNSIFN-LEVQNEFDFV-----Y-DSGCLHHIPP--------------------HRRInyVDLI 148
Cdd:COG2890  153 RRNAERLGLEdrVRFLQGDLFEpLPGDGRFDLIvsnppYiPEDEIALLPPevrdheprlaldggedgldfYRRI--IAQA 230

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446769041 149 KNSLKSGGYFGLtcfaagnlderngsEItDWDvyrewslQGglayseEKLREIFKE--FEVIEIRR 212
Cdd:COG2890  231 PRLLKPGGWLLL--------------EI-GED-------QG------EAVRALLEAagFADVETHK 268
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 41-136 9.54e-04

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 39.73  E-value: 9.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041  41 FENVPDENLVSN----IQKERVSK------GKVLELGCGPGRNAIYLAtQGFDVTAV--DLSVEGINWAKERALAKGVEI 108
Cdd:PLN02336 238 YERVFGEGFVSTggleTTKEFVDKldlkpgQKVLDVGCGIGGGDFYMA-ENFDVHVVgiDLSVNMISFALERAIGRKCSV 316

                         90       100
                 ....*....|....*....|....*....
gi 446769041 109 HF-ICNSIFNLEVQNEFDFVYDSGCLHHI 136
Cdd:PLN02336 317 EFeVADCTKKTYPDNSFDVIYSRDTILHI 345
PRK14966 PRK14966
unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; ...
 27-123 6.32e-03

unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; Provisional


Pssm-ID: 184930 [Multi-domain]  Cd Length: 423  Bit Score: 37.37  E-value: 6.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446769041  27 WNEFYENREKDVP--FFENVPDENLVSNIQKERVSKGKVLELGCGPGRNAIYLATQGFD--VTAVDLSVEGINWAKERAL 102
Cdd:PRK14966 217 VREFYGRRFAVNPnvLIPRPETEHLVEAVLARLPENGRVWDLGTGSGAVAVTVALERPDafVRASDISPPALETARKNAA 296

                         90       100
                 ....*....|....*....|.
gi 446769041 103 AKGVEIHFICNSIFNLEVQNE 123
Cdd:PRK14966 297 DLGARVEFAHGSWFDTDMPSE 317
 
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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