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Conserved domains on  [gi|446457925|ref|WP_000535779|]
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bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG [Escherichia coli]

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 ...
39-141 3.51e-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: 74.67  E-value: 3.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457925  39 PDGVIADIGCGRGEWLEILTENGIANIGVDLDDGMLARAREA----GLNVQKMDC--LQFLQSQADqsliALTGFHIAEH 112
Cdd:COG2227   24 AGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERaaelNVDFVQGDLedLPLEDGSFD----LVICSEVLEH 99
                         90       100       110
                 ....*....|....*....|....*....|.
gi 446457925 113 L--PFEVLQQLVmhtlRVLKPGGLLILETPN 141
Cdd:COG2227  100 LpdPAALLRELA----RLLKPGGLLLLSTPN 126
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
39-141 3.51e-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: 74.67  E-value: 3.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457925  39 PDGVIADIGCGRGEWLEILTENGIANIGVDLDDGMLARAREA----GLNVQKMDC--LQFLQSQADqsliALTGFHIAEH 112
Cdd:COG2227   24 AGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERaaelNVDFVQGDLedLPLEDGSFD----LVICSEVLEH 99
                         90       100       110
                 ....*....|....*....|....*....|.
gi 446457925 113 L--PFEVLQQLVmhtlRVLKPGGLLILETPN 141
Cdd:COG2227  100 LpdPAALLRELA----RLLKPGGLLLLSTPN 126
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
43-133 3.43e-14

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 67.97  E-value: 3.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457925   43 IADIGCGRGEWLEILTENGIANI-GVDLDDGMLARARE----AGLNVQ--KMDCLQFlqSQADQSLIALTGFHIAEHLPF 115
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVtGVDLSPEMLERAREraaeAGLNVEfvQGDAEDL--PFPDGSFDLVVSSGVLHHLPD 78
                          90
                  ....*....|....*...
gi 446457925  116 EVLQQLVMHTLRVLKPGG 133
Cdd:pfam13649  79 PDLEAALREIARVLKPGG 96
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
43-144 2.37e-08

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 54.39  E-value: 2.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457925  43 IADIGCGRGEWLEILTENGIAN---IGVDLDDGMLARAREAGLNVQKMDCLQFLqsQADqslialtgfhiAEHLPFE--- 116
Cdd:PRK00216  55 VLDLACGTGDLAIALAKAVGKTgevVGLDFSEGMLAVGREKLRDLGLSGNVEFV--QGD-----------AEALPFPdns 121
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446457925 117 ------------------VLQQlvMHtlRVLKPGG-LLILETPNPEN 144
Cdd:PRK00216 122 fdavtiafglrnvpdidkALRE--MY--RVLKPGGrLVILEFSKPTN 164
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
43-138 1.23e-07

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 49.74  E-value: 1.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457925  43 IADIGCGRGEWLEILTENGIAN-IGVDLDDGMLARAREAGLN-------VQKMDCLQFLQsQADQS---LIALTGFHIAE 111
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARvTGVDISPVALELARKAAAAlladnveVLKGDAEELPP-EADESfdvIISDPPLHHLV 80
                         90       100
                 ....*....|....*....|....*..
gi 446457925 112 HLPFEVLQQLvmhtLRVLKPGGLLILE 138
Cdd:cd02440   81 EDLARFLEEA----RRLLKPGGVLVLT 103
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
43-144 6.59e-06

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 46.87  E-value: 6.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457925   43 IADIGCGRGEWLEILTENG--IANI-GVDLDDGMLARAREAGlnvQKMDCLQFLQSQA------DQSLIALT---GFHIA 110
Cdd:TIGR01934  43 VLDVACGTGDLAIELAKSApdRGKVtGVDFSSEMLEVAKKKS---ELPLNIEFIQADAealpfeDNSFDAVTiafGLRNV 119
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 446457925  111 EHLPfEVLQQlvMHtlRVLKPGG-LLILETPNPEN 144
Cdd:TIGR01934 120 TDIQ-KALRE--MY--RVLKPGGrLVILEFSKPAN 149
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
39-141 3.51e-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: 74.67  E-value: 3.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457925  39 PDGVIADIGCGRGEWLEILTENGIANIGVDLDDGMLARAREA----GLNVQKMDC--LQFLQSQADqsliALTGFHIAEH 112
Cdd:COG2227   24 AGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERaaelNVDFVQGDLedLPLEDGSFD----LVICSEVLEH 99
                         90       100       110
                 ....*....|....*....|....*....|.
gi 446457925 113 L--PFEVLQQLVmhtlRVLKPGGLLILETPN 141
Cdd:COG2227  100 LpdPAALLRELA----RLLKPGGLLLLSTPN 126
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
43-133 3.43e-14

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 67.97  E-value: 3.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457925   43 IADIGCGRGEWLEILTENGIANI-GVDLDDGMLARARE----AGLNVQ--KMDCLQFlqSQADQSLIALTGFHIAEHLPF 115
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVtGVDLSPEMLERAREraaeAGLNVEfvQGDAEDL--PFPDGSFDLVVSSGVLHHLPD 78
                          90
                  ....*....|....*...
gi 446457925  116 EVLQQLVMHTLRVLKPGG 133
Cdd:pfam13649  79 PDLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
39-142 1.71e-13

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: 67.33  E-value: 1.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457925  39 PDGVIADIGCGRGEWLEILTENGIANIGVDLDDGMLARARE----AGLNVQ----KMDCLQFlqsqADQSLIALTGFHIA 110
Cdd:COG2226   22 PGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELAREraaeAGLNVEfvvgDAEDLPF----PDGSFDLVISSFVL 97
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446457925 111 EHLP--FEVLQQLvmhtLRVLKPGGLLILETPNP 142
Cdd:COG2226   98 HHLPdpERALAEI----ARVLKPGGRLVVVDFSP 127
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
39-139 4.46e-12

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 62.15  E-value: 4.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457925  39 PDGVIADIGCGRGEWLEILTENGIAN--IGVDLDDGMLARARE--AGLNVQKMDCLQF-LQSQADqsLI--ALTGFHIAE 111
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERFPGArvTGVDLSPEMLARARArlPNVRFVVADLRDLdPPEPFD--LVvsNAALHWLPD 78
                         90       100
                 ....*....|....*....|....*...
gi 446457925 112 HLpfEVLQQLVmhtlRVLKPGGLLILET 139
Cdd:COG4106   79 HA--ALLARLA----AALAPGGVLAVQV 100
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
45-137 5.51e-12

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 61.53  E-value: 5.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457925   45 DIGCGRGEWLEILTENGIANIGVDLDDGMLARAREAGLNVQkmdcLQFLqsQADqslialtgfhiAEHLPFE------VL 118
Cdd:pfam08241   2 DVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREG----LTFV--VGD-----------AEDLPFPdnsfdlVL 64
                          90       100       110
                  ....*....|....*....|....*....|
gi 446457925  119 QQLVMHTL-----------RVLKPGGLLIL 137
Cdd:pfam08241  65 SSEVLHHVedperalreiaRVLKPGGILII 94
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
27-138 1.17e-11

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 63.40  E-value: 1.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457925  27 YLPFLAGLKDIYPDGVIADIGCGRGEWLEILTENGIAN-IGVDLDDGMLARARE----AGLN---VQKMDCLQFLQSqAD 98
Cdd:COG0500   14 LAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRvIGIDLSPEAIALARAraakAGLGnveFLVADLAELDPL-PA 92
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446457925  99 QSLIALTGFHIAEHLPFEVLQQLVMHTLRVLKPGGLLILE 138
Cdd:COG0500   93 ESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLLS 132
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
39-144 1.24e-11

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 63.09  E-value: 1.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457925  39 PDGVIADIGCGRGEWLEILTENGIANIGVDLDDGMLARAREAGL--NVQKMDCLQFLQSQADQSLIALTG-FHIAEHLPf 115
Cdd:COG4976   46 PFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREKGVydRLLVADLADLAEPDGRFDLIVAADvLTYLGDLA- 124
                         90       100
                 ....*....|....*....|....*....
gi 446457925 116 EVLQQLvmhtLRVLKPGGLLILETPNPEN 144
Cdd:COG4976  125 AVFAGV----ARALKPGGLFIFSVEDADG 149
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
39-140 1.98e-09

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 56.09  E-value: 1.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457925  39 PDGVIADIGCGRGEWLEILTENGIANI-GVDLDDGMLARAR----EAGLN----VQKMDCLQF-LQSQADqsliALTGFH 108
Cdd:COG2230   51 PGMRVLDIGCGWGGLALYLARRYGVRVtGVTLSPEQLEYAReraaEAGLAdrveVRLADYRDLpADGQFD----AIVSIG 126
                         90       100       110
                 ....*....|....*....|....*....|..
gi 446457925 109 IAEHLPFEVLQQLVMHTLRVLKPGGLLILETP 140
Cdd:COG2230  127 MFEHVGPENYPAYFAKVARLLKPGGRLLLHTP 158
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
18-141 2.32e-09

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 55.90  E-value: 2.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457925   18 EEIKRRLSFYLPFLAGLKDiyPDGVIADIGCGRGEWLEILTENGIANIGVDLDDGMLARAREAglNVQKMDCLQFLQSQA 97
Cdd:pfam13489   3 HQRERLLADLLLRLLPKLP--SPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLN--VRFDQFDEQEAAVPA 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 446457925   98 DQ-SLIalTGFHIAEHLPF--EVLQQLvmhtLRVLKPGGLLILETPN 141
Cdd:pfam13489  79 GKfDVI--VAREVLEHVPDppALLRQI----AALLKPGGLLLLSTPL 119
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
43-144 2.37e-08

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 54.39  E-value: 2.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457925  43 IADIGCGRGEWLEILTENGIAN---IGVDLDDGMLARAREAGLNVQKMDCLQFLqsQADqslialtgfhiAEHLPFE--- 116
Cdd:PRK00216  55 VLDLACGTGDLAIALAKAVGKTgevVGLDFSEGMLAVGREKLRDLGLSGNVEFV--QGD-----------AEALPFPdns 121
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446457925 117 ------------------VLQQlvMHtlRVLKPGG-LLILETPNPEN 144
Cdd:PRK00216 122 fdavtiafglrnvpdidkALRE--MY--RVLKPGGrLVILEFSKPTN 164
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
43-138 1.23e-07

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 49.74  E-value: 1.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457925  43 IADIGCGRGEWLEILTENGIAN-IGVDLDDGMLARAREAGLN-------VQKMDCLQFLQsQADQS---LIALTGFHIAE 111
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARvTGVDISPVALELARKAAAAlladnveVLKGDAEELPP-EADESfdvIISDPPLHHLV 80
                         90       100
                 ....*....|....*....|....*..
gi 446457925 112 HLPFEVLQQLvmhtLRVLKPGGLLILE 138
Cdd:cd02440   81 EDLARFLEEA----RRLLKPGGVLVLT 103
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
45-135 2.02e-07

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 48.90  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457925   45 DIGCGRGEWLE-ILTENGIANI-GVDLDDGMLARARE--AGLNVQKMDCLQFLQSQADQSLI----ALTGFHIAEHLPfe 116
Cdd:pfam08242   2 EIGCGTGTLLRaLLEALPGLEYtGLDISPAALEAARErlAALGLLNAVRVELFQLDLGELDPgsfdVVVASNVLHHLA-- 79
                          90
                  ....*....|....*....
gi 446457925  117 VLQQLVMHTLRVLKPGGLL 135
Cdd:pfam08242  80 DPRAVLRNIRRLLKPGGVL 98
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
45-179 1.62e-06

Predicted SAM-depedendent methyltransferase [General function prediction only];


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 47.94  E-value: 1.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457925  45 DIGCGR---GEWLEI-LTENGIANIGVDLDDGmlarareaglnvqkmdcLQFlqsqADQSLIALTGFHIAEHLPFEVLQQ 120
Cdd:COG4627    8 NIGCGPkrlPGWLNVdIVPAPGVDIVGDLTDP-----------------LPF----PDNSVDAIYSSHVLEHLDYEEAPL 66
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446457925 121 LVMHTLRVLKPGGLLILETPNPENVsvgtCSFYMDPTHNHPLPPPLLEFLPIHYGFNRA 179
Cdd:COG4627   67 ALKECYRVLKPGGILRIVVPDLEHV----ARLYLAEYDAALDVAELRLAGPIDPLGIIL 121
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
43-144 6.59e-06

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 46.87  E-value: 6.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457925   43 IADIGCGRGEWLEILTENG--IANI-GVDLDDGMLARAREAGlnvQKMDCLQFLQSQA------DQSLIALT---GFHIA 110
Cdd:TIGR01934  43 VLDVACGTGDLAIELAKSApdRGKVtGVDFSSEMLEVAKKKS---ELPLNIEFIQADAealpfeDNSFDAVTiafGLRNV 119
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 446457925  111 EHLPfEVLQQlvMHtlRVLKPGG-LLILETPNPEN 144
Cdd:TIGR01934 120 TDIQ-KALRE--MY--RVLKPGGrLVILEFSKPAN 149
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
19-145 6.96e-06

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: 46.90  E-value: 6.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457925   19 EIKRRLSFYLpfLAGLKDIYPD--GVIADIGCGRGEWLEILTENGIAN--IGVDLDDGMLARAREAgLNVQkmdcLQFLq 94
Cdd:TIGR02072  14 KIQREMAKRL--LALLKEKGIFipASVLDIGCGTGYLTRALLKRFPQAefIALDISAGMLAQAKTK-LSEN----VQFI- 85
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446457925   95 sQADqslialtgfhiAEHLPFEV-----------------LQQLVMHTLRVLKPGGLLILETPNPENV 145
Cdd:TIGR02072  86 -CGD-----------AEKLPLEDssfdlivsnlalqwcddLSQALSELARVLKPGGLLAFSTFGPGTL 141
PRK08317 PRK08317
hypothetical protein; Provisional
28-139 2.46e-05

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 45.31  E-value: 2.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457925  28 LPFLAGLK-------DIYPDGVIADIGCGRGEWLEIL----TENGIAnIGVDLDDGMLARAREAGLNvqkmDCLQFLQSQ 96
Cdd:PRK08317   1 LPDFRRYRartfellAVQPGDRVLDVGCGPGNDARELarrvGPEGRV-VGIDRSEAMLALAKERAAG----LGPNVEFVR 75
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446457925  97 ADqslialtgfhiAEHLPFE-----------VLQ------QLVMHTLRVLKPGG-LLILET 139
Cdd:PRK08317  76 GD-----------ADGLPFPdgsfdavrsdrVLQhledpaRALAEIARVLRPGGrVVVLDT 125
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
4-140 4.27e-05

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 44.93  E-value: 4.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457925   4 SFYRSFE-ERHRGSVEEIKRrlsfyLPFLAGLKdiypdgvIADIGCGRGEWLEILTE----NGIanIGVDLDDGMLARAR 78
Cdd:PRK01683   7 SLYLKFEdERTRPARDLLAR-----VPLENPRY-------VVDLGCGPGNSTELLVErwpaARI--TGIDSSPAMLAEAR 72
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446457925  79 EA--GLNVQKMDCLQFLQSQADQSLIALTGFH-IAEHLpfEVLQQLVmhtlRVLKPGGLLILETP 140
Cdd:PRK01683  73 SRlpDCQFVEADIASWQPPQALDLIFANASLQwLPDHL--ELFPRLV----SLLAPGGVLAVQMP 131
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
39-144 8.20e-05

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 42.40  E-value: 8.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457925   39 PDGVIADIGCGRGEWLEILTENGIAN---IGVDLDDGMLARARE-------AGLNVQKMDCLQFLQSQADQS--LIALTG 106
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGPNaevVGIDISEEAIEKAREnaqklgfDNVEFEQGDIEELPELLEDDKfdVVISNC 82
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 446457925  107 FHIAEHLPFEVLQQLvmhtLRVLKPGGLLILETPNPEN 144
Cdd:pfam13847  83 VLNHIPDPDKVLQEI----LRVLKPGGRLIISDPDSLA 116
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
30-141 5.98e-04

Methionine biosynthesis protein MetW; This family consists of several bacterial and one archaeal methionine biosynthesis MetW proteins. Biosynthesis of methionine from homoserine in Pseudomonas putida takes place in three steps. The first step is the acylation of homoserine to yield an acyl-L-homoserine. This reaction is catalyzed by the products of the metXW genes and is equivalent to the first step in enterobacteria, gram-positive bacteria and fungi, except that in these microorganizms the reaction is catalyzed by a single polypeptide (the product of the metA gene in Escherichia coli and the met5 gene product in Neurospora crassa). In Pseudomonas putida, as in gram-positive bacteria and certain fungi, the second and third steps are a direct sulfhydrylation that converts the O-acyl-L-homoserine into homocysteine and further methylation to yield methionine. The latter reaction can be mediated by either of the two methionine synthetases present in the cells.


Pssm-ID: 399779  Cd Length: 193  Bit Score: 40.90  E-value: 5.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457925   30 FLAGLKDIYPDGVIADIGCGRGEWLEILTEN-GIANIGVDLDDGMLARAREAGLNVQKMDCLQFLQSQADQSL--IALTG 106
Cdd:pfam07021   4 FRYILEWIPPGSRVLDLGCGDGTLLYLLKEEkGVDGYGIELDAAGVAECVAKGLYVIQGDLDEGLEHFPDKSFdyVILSQ 83
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 446457925  107 FHIAEHLPFEVLQQLvmhtLRVlkpGGLLILETPN 141
Cdd:pfam07021  84 TLQATRNPREVLDEM----LRI---GRRCIVSFPN 111
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
39-137 1.51e-03

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: 39.40  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457925  39 PDGVIADIGCGrgeW----LEILTENGIANI-GVDLDdgmlARARE-AGLNVQK--MDCLQFLQSQADQSLIALT----- 105
Cdd:COG2813   49 LGGRVLDLGCG---YgvigLALAKRNPEARVtLVDVN----ARAVElARANAAAngLENVEVLWSDGLSGVPDGSfdlil 121
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446457925 106 ---GFHIAEHLPFEVLQQLVMHTLRVLKPGGLLIL 137
Cdd:COG2813  122 snpPFHAGRAVDKEVAHALIADAARHLRPGGELWL 156
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
43-144 2.47e-03

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 39.34  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457925   43 IADIGCGRGEWLEILTENGIAN---IGVDLDDGMLARAREAGLNVQKMDcLQFLQSQA------DQSLIALT-GFHIAEh 112
Cdd:pfam01209  46 FLDVAGGTGDWTFGLSDSAGSSgkvVGLDINENMLKEGEKKAKEEGKYN-IEFLQGNAeelpfeDDSFDIVTiSFGLRN- 123
                          90       100       110
                  ....*....|....*....|....*....|...
gi 446457925  113 lpFEVLQQLVMHTLRVLKPGG-LLILETPNPEN 144
Cdd:pfam01209 124 --FPDYLKVLKEAFRVLKPGGrVVCLEFSKPEN 154
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
35-137 6.29e-03

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 37.57  E-value: 6.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446457925   35 KDIYPDGVIADIGCGRGEWLEILTENGIANI-GVDLDDGMLARAREA------GLNVQKMDCLQFLQSQADQS---LIA- 103
Cdd:pfam01728  17 GLLKPGKTVLDLGAAPGGWSQVALQRGAGKVvGVDLGPMQLWKPRNDpgvtfiQGDIRDPETLDLLEELLGRKvdlVLSd 96
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 446457925  104 ----LTGFHIAEH-LPFE-VLQQLVMhTLRVLKPGGLLIL 137
Cdd:pfam01728  97 gspfISGNKVLDHlRSLDlVKAALEV-ALELLRKGGNFVC 135
 
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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