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Conserved domains on  [gi|492447672|ref|WP_005846839|]
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MULTISPECIES: bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG [Phocaeicola]

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 ...
 64-162 1.31e-18

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: 78.91  E-value: 1.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672  64 AEGNILDVGAGSGCHALALQEMGKEVCAIDISPRSVEVMEKRGVR---NVRQMNLFD-PHFLETFDTILMlmngSGIIGK 139
Cdd:COG2227   24 AGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAElnvDFVQGDLEDlPLEDGSFDLVIC----SEVLEH 99

                         90       100
                 ....*....|....*....|...
gi 492447672 140 LENMAAFFQKMKQLLRPGGCILM 162
Cdd:COG2227  100 LPDPAALLRELARLLKPGGLLLL 122
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 64-162 1.31e-18

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: 78.91  E-value: 1.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672  64 AEGNILDVGAGSGCHALALQEMGKEVCAIDISPRSVEVMEKRGVR---NVRQMNLFD-PHFLETFDTILMlmngSGIIGK 139
Cdd:COG2227   24 AGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAElnvDFVQGDLEDlPLEDGSFDLVIC----SEVLEH 99

                         90       100
                 ....*....|....*....|...
gi 492447672 140 LENMAAFFQKMKQLLRPGGCILM 162
Cdd:COG2227  100 LPDPAALLRELARLLKPGGLLLL 122
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 68-158 2.35e-14

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 66.43  E-value: 2.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672   68 ILDVGAGSGCHALALQEM-GKEVCAIDISPRSVEVMEKRGVRN-----VRQMNLFDPHFL-ETFDTIlmLMNGSGIIGKL 140
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAglnveFVQGDAEDLPFPdGSFDLV--VSSGVLHHLPD 78

                          90
                  ....*....|....*...
gi 492447672  141 ENMAAFFQKMKQLLRPGG 158
Cdd:pfam13649  79 PDLEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 67-158 2.87e-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: 58.60  E-value: 2.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672  67 NILDVGAGSGCHALALQE-MGKEVCAIDISPRSVEVMEKRGVRN------VRQMNLFDPHFL--ETFDTIlmLMNGSgII 137
Cdd:cd02440    1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELARKAAAALladnveVLKGDAEELPPEadESFDVI--ISDPP-LH 77

                         90       100
                 ....*....|....*....|.
gi 492447672 138 GKLENMAAFFQKMKQLLRPGG 158
Cdd:cd02440   78 HLVEDLARFLEEARRLLKPGG 98
PRK14968 PRK14968
putative methyltransferase; Provisional
 56-128 8.22e-08

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 50.67  E-value: 8.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672  56 LEQIALQMAEGNILDVGAGSGCHALALQEMGKEVCAIDISPRSVE----VMEKRGVRN----VRQMNLFDPHFLETFDTI 127
Cdd:PRK14968  15 LAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVEcakcNAKLNNIRNngveVIRSDLFEPFRGDKFDVI 94


                 .
gi 492447672 128 L 128
Cdd:PRK14968  95 L 95
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 53-127 4.03e-05

HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 43.88  E-value: 4.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672   53 MPELEQIALQMAEGNILDVGAGSGCHALAL--QEMGKEVCAIDISPRSVEVMEKRGVRN-------VRQMNLFDPHFLET 123
Cdd:TIGR00536 103 EKALASLISQPPILHILDLGTGSGCIALALayEFPNAEVIAVDISPDALAVAEENAEKNqlehrveFIQSNLFEPLAGQK 182


                  ....
gi 492447672  124 FDTI 127
Cdd:TIGR00536 183 IDII 186
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 64-162 1.31e-18

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: 78.91  E-value: 1.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672  64 AEGNILDVGAGSGCHALALQEMGKEVCAIDISPRSVEVMEKRGVR---NVRQMNLFD-PHFLETFDTILMlmngSGIIGK 139
Cdd:COG2227   24 AGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAElnvDFVQGDLEDlPLEDGSFDLVIC----SEVLEH 99

                         90       100
                 ....*....|....*....|...
gi 492447672 140 LENMAAFFQKMKQLLRPGGCILM 162
Cdd:COG2227  100 LPDPAALLRELARLLKPGGLLLL 122
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
49-187 7.20e-15

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 70.41  E-value: 7.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672  49 PYDEMPELEQIALQMA----EGNILDVGAGSGCHALALQEMGKEVCAIDISPRSVEVMEKRGV-RNVRQMNLFDPHFL-E 122
Cdd:COG4976   27 GYEAPALLAEELLARLppgpFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREKGVyDRLLVADLADLAEPdG 106

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492447672 123 TFDTILMlmngSGIIGKLENMAAFFQKMKQLLRPGGCILMDssdlrylFEDEDGSFLIDLAGDYY 187
Cdd:COG4976  107 RFDLIVA----ADVLTYLGDLAAVFAGVARALKPGGLFIFS-------VEDADGSGRYAHSLDYV 160
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 68-158 2.35e-14

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 66.43  E-value: 2.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672   68 ILDVGAGSGCHALALQEM-GKEVCAIDISPRSVEVMEKRGVRN-----VRQMNLFDPHFL-ETFDTIlmLMNGSGIIGKL 140
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAglnveFVQGDAEDLPFPdGSFDLV--VSSGVLHHLPD 78

                          90
                  ....*....|....*...
gi 492447672  141 ENMAAFFQKMKQLLRPGG 158
Cdd:pfam13649  79 PDLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 44-162 2.38e-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: 65.40  E-value: 2.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672  44 NQLFRPYDEMPELEQIALQMAEGNILDVGAGSGCHALALQEMGKEVCAIDISPRSVEVMEKRGVR-----NVRQMNLFDP 118
Cdd:COG2226    2 DRVAARYDGREALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEaglnvEFVVGDAEDL 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 492447672 119 HFL-ETFDTILMlmngSGIIGKLENMAAFFQKMKQLLRPGGCILM 162
Cdd:COG2226   82 PFPdGSFDLVIS----SFVLHHLPDPERALAEIARVLKPGGRLVV 122
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 69-158 2.07e-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: 2.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672   69 LDVGAGSGCHALALQEMGKEVCAIDISPRSVEVMEKRGVR---NVRQMNLFDPHFL-ETFDTIL---MLMNgsgiigkLE 141
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPReglTFVVGDAEDLPFPdNSFDLVLsseVLHH-------VE 73

                          90
                  ....*....|....*..
gi 492447672  142 NMAAFFQKMKQLLRPGG 158
Cdd:pfam08241  74 DPERALREIARVLKPGG 90
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 69-160 1.32e-11

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 59.30  E-value: 1.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672   69 LDVGAGSG--CHALALQEMGKEVCAIDISPRSVEVMEKR----GVRNVRQMNLFDP----HFLETFDTILMlmngSGIIG 138
Cdd:pfam08242   1 LEIGCGTGtlLRALLEALPGLEYTGLDISPAALEAARERlaalGLLNAVRVELFQLdlgeLDPGSFDVVVA----SNVLH 76

                          90       100
                  ....*....|....*....|..
gi 492447672  139 KLENMAAFFQKMKQLLRPGGCI 160
Cdd:pfam08242  77 HLADPRAVLRNIRRLLKPGGVL 98
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 67-158 2.87e-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: 58.60  E-value: 2.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672  67 NILDVGAGSGCHALALQE-MGKEVCAIDISPRSVEVMEKRGVRN------VRQMNLFDPHFL--ETFDTIlmLMNGSgII 137
Cdd:cd02440    1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELARKAAAALladnveVLKGDAEELPPEadESFDVI--ISDPP-LH 77

                         90       100
                 ....*....|....*....|.
gi 492447672 138 GKLENMAAFFQKMKQLLRPGG 158
Cdd:cd02440   78 HLVEDLARFLEEARRLLKPGG 98
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
66-163 3.63e-11

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 58.30  E-value: 3.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672  66 GNILDVGAGSGCHALALQEM--GKEVCAIDISPRSVEVMEKR--GVRnVRQMNLFDPHFLETFDTILMlmngSGIIGKLE 141
Cdd:COG4106    3 RRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARARARlpNVR-FVVADLRDLDPPEPFDLVVS----NAALHWLP 77

                         90       100
                 ....*....|....*....|..
gi 492447672 142 NMAAFFQKMKQLLRPGGCILMD 163
Cdd:COG4106   78 DHAALLARLAAALAPGGVLAVQ 99
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 68-162 7.49e-11

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 58.79  E-value: 7.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672  68 ILDVGAGSGCHALAL-QEMGKEVCAIDISPRSVEV----MEKRGVRN---VRQMNLFDPHFLETFDTILMlmngsgiIGK 139
Cdd:COG2230   55 VLDIGCGWGGLALYLaRRYGVRVTGVTLSPEQLEYarerAAEAGLADrveVRLADYRDLPADGQFDAIVS-------IGM 127

                         90       100
                 ....*....|....*....|....*...
gi 492447672 140 LE-----NMAAFFQKMKQLLRPGGCILM 162
Cdd:COG2230  128 FEhvgpeNYPAYFAKVARLLKPGGRLLL 155
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 54-176 4.72e-10

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 57.23  E-value: 4.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672  54 PELEQIALQMAE----GNILDVGAGSGCHALAL-QEMGKEVCAIDISPRSVEVMEKR----GVRNVR--QMNLFDPHFLE 122
Cdd:COG0500   12 PGLAALLALLERlpkgGRVLDLGCGTGRNLLALaARFGGRVIGIDLSPEAIALARARaakaGLGNVEflVADLAELDPLP 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 492447672 123 T--FDTILMLMNGSGIigKLENMAAFFQKMKQLLRPGG-CILMDSSDLRYLFEDEDG 176
Cdd:COG0500   92 AesFDLVVAFGVLHHL--PPEEREALLRELARALKPGGvLLLSASDAAAALSLARLL 146
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 64-158 7.27e-08

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 50.50  E-value: 7.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672   64 AEGNILDVGAGSGCHALALQEMGKEVCAIDISPRSVEvmekrGVRNVRQMNLFDPHFL----ETFDTILMLMngsgIIGK 139
Cdd:pfam13489  22 SPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIE-----RALLNVRFDQFDEQEAavpaGKFDVIVARE----VLEH 92

                          90
                  ....*....|....*....
gi 492447672  140 LENMAAFFQKMKQLLRPGG 158
Cdd:pfam13489  93 VPDPPALLRQIAALLKPGG 111
PRK14968 PRK14968
putative methyltransferase; Provisional
 56-128 8.22e-08

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 50.67  E-value: 8.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672  56 LEQIALQMAEGNILDVGAGSGCHALALQEMGKEVCAIDISPRSVE----VMEKRGVRN----VRQMNLFDPHFLETFDTI 127
Cdd:PRK14968  15 LAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVEcakcNAKLNNIRNngveVIRSDLFEPFRGDKFDVI 94


                 .
gi 492447672 128 L 128
Cdd:PRK14968  95 L 95
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 67-198 1.10e-07

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 49.72  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672   67 NILDVGAGSG--CHALALQE-MGKEVCAIDISPRSVEVM----EKRGVRNVR----QMNLFDPHF-LETFDTILMlmngS 134
Cdd:pfam13847   6 RVLDLGCGTGhlSFELAEELgPNAEVVGIDISEEAIEKArenaQKLGFDNVEfeqgDIEELPELLeDDKFDVVIS----N 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492447672  135 GIIGKLENMAAFFQKMKQLLRPGGCILMDS----SDLRYLFEDEDGSFLIDLAGDYYGEIDFRMQYKN 198
Cdd:pfam13847  82 CVLNHIPDPDKVLQEILRVLKPGGRLIISDpdslAELPAHVKEDSTYYAGCVGGAILKKKLYELLEEA 149
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 58-127 5.63e-07

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 49.39  E-value: 5.63e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492447672  58 QIALQMAEGNILDVGAGSGCHALAL-QEM-GKEVCAIDISPRSVEV----MEKRGVRNVR--QMNLFDPHFLETFDTI 127
Cdd:PRK09328 102 EALLLKEPLRVLDLGTGSGAIALALaKERpDAEVTAVDISPEALAVarrnAKHGLGARVEflQGDWFEPLPGGRFDLI 179
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 64-162 1.55e-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: 47.11  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672  64 AEGNILDVGAGSG--CHALALQEMGKEVCAIDISPRSVEV----MEKRGVRNVR--QMNLFDPHFLETFDTIlmLMN--- 132
Cdd:COG2813   49 LGGRVLDLGCGYGviGLALAKRNPEARVTLVDVNARAVELaranAAANGLENVEvlWSDGLSGVPDGSFDLI--LSNppf 126

                         90       100       110
                 ....*....|....*....|....*....|..
gi 492447672 133 --GSGIIGKLenMAAFFQKMKQLLRPGGCILM 162
Cdd:COG2813  127 haGRAVDKEV--AHALIADAARHLRPGGELWL 156
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 64-128 4.81e-06

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 46.30  E-value: 4.81e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492447672  64 AEGNILDVGAGSGCHALAL-QEMGK-EVCAIDISPRSVEV----MEKRGVRN---VRQMNLFDP-HFLETFDTIL 128
Cdd:COG2890  112 APPRVLDLGTGSGAIALALaKERPDaRVTAVDISPDALAVarrnAERLGLEDrvrFLQGDLFEPlPGDGRFDLIV 186
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
54-129 8.38e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 45.28  E-value: 8.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672  54 PELEQ------IALQMA-----EGNI-----LDVGAGSGCHALALQEMG-KEVCAIDISPRSVEV----MEKRGVR-NVR 111
Cdd:COG2263   19 VELEQyptpaeLAAELLhlaylRGDIegktvLDLGCGTGMLAIGAALLGaKKVVGVDIDPEALEIarenAERLGVRvDFI 98

                         90
                 ....*....|....*...
gi 492447672 112 QMNLFDPHFLETFDTILM 129
Cdd:COG2263   99 RADVTRIPLGGSVDTVVM 116
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
56-162 8.41e-06

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 45.53  E-value: 8.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672  56 LEQIALQMAEG-NILDVGAGSGCHALALQEMG-KEVCAIDISPRSVEVMEKRGVRNVRQMNLFDPHFLETFDTIL--MLm 131
Cdd:PRK00517 110 LEALEKLVLPGkTVLDVGCGSGILAIAAAKLGaKKVLAVDIDPQAVEAARENAELNGVELNVYLPQGDLKADVIVanIL- 188

                         90       100       110
                 ....*....|....*....|....*....|.
gi 492447672 132 ngSGIIGKLENMaaffqkMKQLLRPGGCILM 162
Cdd:PRK00517 189 --ANPLLELAPD------LARLLKPGGRLIL 211
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 53-127 4.03e-05

HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 43.88  E-value: 4.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672   53 MPELEQIALQMAEGNILDVGAGSGCHALAL--QEMGKEVCAIDISPRSVEVMEKRGVRN-------VRQMNLFDPHFLET 123
Cdd:TIGR00536 103 EKALASLISQPPILHILDLGTGSGCIALALayEFPNAEVIAVDISPDALAVAEENAEKNqlehrveFIQSNLFEPLAGQK 182


                  ....
gi 492447672  124 FDTI 127
Cdd:TIGR00536 183 IDII 186
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
68-161 1.98e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 41.56  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672  68 ILDVGAGSGCHA-LALQEMGKEVCAIDISPRSVEVMEKRGVRN-------VRQMNLFDPHFLETFDTILMLMNGSGIIGk 139
Cdd:COG4076   39 VLDIGTGSGLLSmLAARAGAKKVYAVEVNPDIAAVARRIIAANglsdritVINADATDLDLPEKADVIISEMLDTALLD- 117

                         90       100
                 ....*....|....*....|...
gi 492447672 140 lENMAAFFQKMKQ-LLRPGGCIL 161
Cdd:COG4076  118 -EGQVPILNHARKrLLKPGGRII 139
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 66-162 2.15e-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: 40.65  E-value: 2.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672   66 GNILDVGAGSGCHALALQEMGK--EVCAIDISPRSVEVMEKRGVRN------VRQMNLFDPHFLETFDTIlmLMNGSGII 137
Cdd:pfam05175  33 GKVLDLGCGAGVLGAALAKESPdaELTMVDINARALESARENLAANglengeVVASDVYSGVEDGKFDLI--ISNPPFHA 110

                          90       100
                  ....*....|....*....|....*...
gi 492447672  138 GKLENMAA---FFQKMKQLLRPGGCILM 162
Cdd:pfam05175 111 GLATTYNVaqrFIADAKRHLRPGGELWI 138
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 67-128 3.66e-04

HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129628 [Multi-domain]  Cd Length: 179  Bit Score: 40.22  E-value: 3.66e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492447672   67 NILDVGAGSGCHALALQEMGKEVCAIDISPRSVEVMEKRGVRN-----VRQMNLFDPhFLETFDTIL 128
Cdd:TIGR00537  22 DVLEIGAGTGLVAIRLKGKGKCILTTDINPFAVKELRENAKLNnvgldVVMTDLFKG-VRGKFDVIL 87
PRK12335 PRK12335
tellurite resistance protein TehB; Provisional
 66-143 5.83e-04

tellurite resistance protein TehB; Provisional


Pssm-ID: 183450 [Multi-domain]  Cd Length: 287  Bit Score: 40.31  E-value: 5.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672  66 GNILDVGAGSGCHALALQEMGKEVCAIDISPRSV----EVMEKRGVrNVRqMNLFD---PHFLETFDTI-----LMLMNG 133
Cdd:PRK12335 122 GKALDLGCGQGRNSLYLALLGFDVTAVDINQQSLenlqEIAEKENL-NIR-TGLYDinsASIQEEYDFIlstvvLMFLNR 199

                         90
                 ....*....|
gi 492447672 134 SGIIGKLENM 143
Cdd:PRK12335 200 ERIPAIIKNM 209
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 66-158 7.47e-04

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 39.74  E-value: 7.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672  66 GNILDVGAGSG--CHALALQEMGKEVCAIDISPRSVEvMEKRGVRN--------VRQMNLFDPHFL---ETFDTILM--- 129
Cdd:COG4123   39 GRVLDLGTGTGviALMLAQRSPGARITGVEIQPEAAE-LARRNVALngledritVIHGDLKEFAAElppGSFDLVVSnpp 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 492447672 130 -LMNGSGIIGKLE-----------NMAAFFQKMKQLLRPGG 158
Cdd:COG4123  118 yFKAGSGRKSPDEaraiarhedalTLEDLIRAAARLLKPGG 158
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
54-166 7.78e-04

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 39.33  E-value: 7.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672  54 PELEQIALQMAEGNILDVGAGSGCHALALQEMGKEVCAIDISPRSVEVMEK----RGVRNV--RQMNLFDPHFLETFDTI 127
Cdd:PRK11207  20 SEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGFDVTAWDKNPMSIANLERikaaENLDNLhtAVVDLNNLTFDGEYDFI 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 492447672 128 L-----MLMNGSGIIGKLENMAAffqkmkqLLRPGGCIL----MDSSD 166
Cdd:PRK11207 100 LstvvlMFLEAKTIPGLIANMQR-------CTKPGGYNLivaaMDTAD 140
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 68-105 1.17e-03

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 39.05  E-value: 1.17e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 492447672  68 ILDVGAGSGCHALALQEMGKEVCAIDISPRSVEVMEKR 105
Cdd:PRK07580  67 ILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARER 104
PRK06922 PRK06922
class I SAM-dependent methyltransferase;
57-190 2.52e-03

class I SAM-dependent methyltransferase;


Pssm-ID: 180751 [Multi-domain]  Cd Length: 677  Bit Score: 38.70  E-value: 2.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672  57 EQIALQMAEGN-ILDVGAGSGCHALALQEM--GKEVCAIDISPRSVEVMEKRGVR-----NVRQ---MNLFDPHFLETFD 125
Cdd:PRK06922 410 KRIILDYIKGDtIVDVGAGGGVMLDMIEEEteDKRIYGIDISENVIDTLKKKKQNegrswNVIKgdaINLSSSFEKESVD 489

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672 126 TILMlmngSGIIGKL-------------ENMAAFFQKMKQLLRPGGCILM-------DSSDLRYL-FEDEDG-SFLIDLA 183
Cdd:PRK06922 490 TIVY----SSILHELfsyieyegkkfnhEVIKKGLQSAYEVLKPGGRIIIrdgimteDKRLMRVIrFKDAGGmKFLEQYV 565


                 ....*..
gi 492447672 184 GDYYGEI 190
Cdd:PRK06922 566 QEFKGRI 572
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
56-162 6.01e-03

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 37.07  E-value: 6.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672  56 LEQIALQMAEG-NILDVGAGSGCHALALQEMG-KEVCAIDISPRSVEV----MEKRGVRN---VRQMNLFDPhflETFDT 126
Cdd:COG2264  139 LEALEKLLKPGkTVLDVGCGSGILAIAAAKLGaKRVLAVDIDPVAVEAarenAELNGVEDrieVVLGDLLED---GPYDL 215

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 492447672 127 IL--MLmngSGIIgklenmAAFFQKMKQLLRPGGCILM 162
Cdd:COG2264  216 VVanIL---ANPL------IELAPDLAALLKPGGYLIL 244
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 60-162 8.34e-03

Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441843 [Multi-domain]  Cd Length: 403  Bit Score: 37.07  E-value: 8.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492447672  60 ALQMAEGNIL-DVGAGSGCHAL--ALQEMGKEVCAIDISPRSVEVME----KRGVRNVRQMNLFDPHFLE---TFDTIlm 129
Cdd:COG2242  242 KLALRPGDVLwDIGAGSGSVSIeaARLAPGGRVYAIERDPERAALIRanarRFGVPNVEVVEGEAPEALAdlpDPDAV-- 319

                         90       100       110
                 ....*....|....*....|....*....|...
gi 492447672 130 LMNGSGiigklENMAAFFQKMKQLLRPGGCILM 162
Cdd:COG2242  320 FIGGSG-----GNLPEILEACWARLRPGGRLVA 347
 
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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