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Conserved domains on  [gi|794205316|gb|AKA51307|]
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methyltransferase [Bacteroides fragilis]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 55-162 3.70e-16

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


:

Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 72.36  E-value: 3.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205316  55 LLERTALAmaTGTILDVGAGSGCHALALQESGKEVSAIDISPLSVEVMKLRGVK---DARQVNLFDERFA-ETFDTILMl 130
Cdd:COG2227   17 LLARLLPA--GGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAElnvDFVQGDLEDLPLEdGSFDLVIC- 93

                         90       100       110
                 ....*....|....*....|....*....|..
gi 794205316 131 mngSGIIGRLENMPLFFRKMKQLLRPDGCILM 162
Cdd:COG2227   94 ---SEVLEHLPDPAALLRELARLLKPGGLLLL 122
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 55-162 3.70e-16

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 72.36  E-value: 3.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205316  55 LLERTALAmaTGTILDVGAGSGCHALALQESGKEVSAIDISPLSVEVMKLRGVK---DARQVNLFDERFA-ETFDTILMl 130
Cdd:COG2227   17 LLARLLPA--GGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAElnvDFVQGDLEDLPLEdGSFDLVIC- 93

                         90       100       110
                 ....*....|....*....|....*....|..
gi 794205316 131 mngSGIIGRLENMPLFFRKMKQLLRPDGCILM 162
Cdd:COG2227   94 ---SEVLEHLPDPAALLRELARLLKPGGLLLL 122
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 69-160 4.68e-10

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 55.07  E-value: 4.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205316   69 LDVGAGSG--CHALALQESGKEVSAIDISPLSVEVMKLR----GVKDARQVNLF----DERFAETFDTILMlmngSGIIG 138
Cdd:pfam08242   1 LEIGCGTGtlLRALLEALPGLEYTGLDISPAALEAARERlaalGLLNAVRVELFqldlGELDPGSFDVVVA----SNVLH 76

                          90       100
                  ....*....|....*....|..
gi 794205316  139 RLENMPLFFRKMKQLLRPDGCI 160
Cdd:pfam08242  77 HLADPRAVLRNIRRLLKPGGVL 98
PRK14968 PRK14968
putative methyltransferase; Provisional
 55-128 7.18e-08

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 51.05  E-value: 7.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205316  55 LLERTALAMATGTILDVGAGSGCHALALQESGKEVSAIDISPLSVE----VMKLRGVKDA----RQVNLFDERFAETFDT 126
Cdd:PRK14968  14 LLAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVEcakcNAKLNNIRNNgvevIRSDLFEPFRGDKFDV 93


                 ..
gi 794205316 127 IL 128
Cdd:PRK14968  94 IL 95
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 67-158 5.80e-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: 46.65  E-value: 5.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205316  67 TILDVGAGSGCHALALQES-GKEVSAIDISPLSVEVMK------LRGVKDARQVNLFDERFA--ETFDTIlmLMNGSgII 137
Cdd:cd02440    1 RVLDLGCGTGALALALASGpGARVTGVDISPVALELARkaaaalLADNVEVLKGDAEELPPEadESFDVI--ISDPP-LH 77

                         90       100
                 ....*....|....*....|.
gi 794205316 138 GRLENMPLFFRKMKQLLRPDG 158
Cdd:cd02440   78 HLVEDLARFLEEARRLLKPGG 98
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 68-127 5.75e-04

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: 40.41  E-value: 5.75e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 794205316   68 ILDVGAGSGCHALAL--QESGKEVSAIDISPLSVEV----MKLRGVKDA---RQVNLFDERFAETFDTI 127
Cdd:TIGR00536 118 ILDLGTGSGCIALALayEFPNAEVIAVDISPDALAVaeenAEKNQLEHRvefIQSNLFEPLAGQKIDII 186
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 55-162 3.70e-16

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 72.36  E-value: 3.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205316  55 LLERTALAmaTGTILDVGAGSGCHALALQESGKEVSAIDISPLSVEVMKLRGVK---DARQVNLFDERFA-ETFDTILMl 130
Cdd:COG2227   17 LLARLLPA--GGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAElnvDFVQGDLEDLPLEdGSFDLVIC- 93

                         90       100       110
                 ....*....|....*....|....*....|..
gi 794205316 131 mngSGIIGRLENMPLFFRKMKQLLRPDGCILM 162
Cdd:COG2227   94 ---SEVLEHLPDPAALLRELARLLKPGGLLLL 122
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 50-162 3.73e-10

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 56.86  E-value: 3.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205316  50 AGQMPLLERTA--LAMATG-TILDVGAGSGCHALAL-QESGKEVSAIDISPLSVEV----MKLRGVKD---ARQVNLFDE 118
Cdd:COG2230   34 EAQEAKLDLILrkLGLKPGmRVLDIGCGWGGLALYLaRRYGVRVTGVTLSPEQLEYarerAAEAGLADrveVRLADYRDL 113

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 794205316 119 RFAETFDTILMlmngsgiIGRLE-----NMPLFFRKMKQLLRPDGCILM 162
Cdd:COG2230  114 PADGQFDAIVS-------IGMFEhvgpeNYPAYFAKVARLLKPGGRLLL 155
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
58-187 4.45e-10

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 56.93  E-value: 4.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205316  58 RTALAMATGTILDVGAGSGCHALALQESGKEVSAIDISPLSVEVMKLRGVKDA-RQVNLFD-ERFAETFDTILMlmngSG 135
Cdd:COG4976   40 ARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREKGVYDRlLVADLADlAEPDGRFDLIVA----AD 115

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 794205316 136 IIGRLENMPLFFRKMKQLLRPDGCILMDssdlrylFEDEDGSFLIDLAGDYY 187
Cdd:COG4976  116 VLTYLGDLAAVFAGVARALKPGGLFIFS-------VEDADGSGRYAHSLDYV 160
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 69-160 4.68e-10

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 55.07  E-value: 4.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205316   69 LDVGAGSG--CHALALQESGKEVSAIDISPLSVEVMKLR----GVKDARQVNLF----DERFAETFDTILMlmngSGIIG 138
Cdd:pfam08242   1 LEIGCGTGtlLRALLEALPGLEYTGLDISPAALEAARERlaalGLLNAVRVELFqldlGELDPGSFDVVVA----SNVLH 76

                          90       100
                  ....*....|....*....|..
gi 794205316  139 RLENMPLFFRKMKQLLRPDGCI 160
Cdd:pfam08242  77 HLADPRAVLRNIRRLLKPGGVL 98
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 55-162 1.41e-09

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: 55.00  E-value: 1.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205316  55 LLERTALAmATGTILDVGAGSGCHALALQESGKEVSAIDISPLSVEVMKLRGVKDARQVNL---------FDErfaETFD 125
Cdd:COG2226   14 LLAALGLR-PGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLNVEFvvgdaedlpFPD---GSFD 89

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 794205316 126 TILMlmngSGIIGRLENMPLFFRKMKQLLRPDGCILM 162
Cdd:COG2226   90 LVIS----SFVLHHLPDPERALAEIARVLKPGGRLVV 122
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 68-158 1.52e-09

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 53.72  E-value: 1.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205316   68 ILDVGAGSGCHALAL-QESGKEVSAIDISPLSVEVMKLRGVKDARQVNLF-----DERFA-ETFDTIlmLMNGSGIIGRL 140
Cdd:pfam13649   1 VLDLGCGTGRLTLALaRRGGARVTGVDLSPEMLERARERAAEAGLNVEFVqgdaeDLPFPdGSFDLV--VSSGVLHHLPD 78

                          90
                  ....*....|....*...
gi 794205316  141 ENMPLFFRKMKQLLRPDG 158
Cdd:pfam13649  79 PDLEAALREIARVLKPGG 96
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 69-158 3.53e-09

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 52.67  E-value: 3.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205316   69 LDVGAGSGCHALALQESGKEVSAIDISPLSVEVMKLRGVKDA---RQVNLFDERFA-ETFDTIL---MLMNgsgiigrLE 141
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGltfVVGDAEDLPFPdNSFDLVLsseVLHH-------VE 73

                          90
                  ....*....|....*..
gi 794205316  142 NMPLFFRKMKQLLRPDG 158
Cdd:pfam08241  74 DPERALREIARVLKPGG 90
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 44-158 4.32e-08

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 51.27  E-value: 4.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205316   44 KQLFRKAGQmpLLERTALAM-ATGTILDVGAGSGCHALALQESGKEVSAIDISPLSVEvmklrGVKDARQVNLFDERFA- 121
Cdd:pfam13489   3 HQRERLLAD--LLLRLLPKLpSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIE-----RALLNVRFDQFDEQEAa 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 794205316  122 ---ETFDTILMLMngsgIIGRLENMPLFFRKMKQLLRPDG 158
Cdd:pfam13489  76 vpaGKFDVIVARE----VLEHVPDPPALLRQIAALLKPGG 111
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
66-163 4.63e-08

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 49.44  E-value: 4.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205316  66 GTILDVGAGSGCHALALQE--SGKEVSAIDISPLSVEV--MKLRGVkDARQVNLFDERFAETFDTILMlmngSGIIGRLE 141
Cdd:COG4106    3 RRVLDLGCGTGRLTALLAErfPGARVTGVDLSPEMLARarARLPNV-RFVVADLRDLDPPEPFDLVVS----NAALHWLP 77

                         90       100
                 ....*....|....*....|..
gi 794205316 142 NMPLFFRKMKQLLRPDGCILMD 163
Cdd:COG4106   78 DHAALLARLAAALAPGGVLAVQ 99
PRK14968 PRK14968
putative methyltransferase; Provisional
 55-128 7.18e-08

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 51.05  E-value: 7.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205316  55 LLERTALAMATGTILDVGAGSGCHALALQESGKEVSAIDISPLSVE----VMKLRGVKDA----RQVNLFDERFAETFDT 126
Cdd:PRK14968  14 LLAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVEcakcNAKLNNIRNNgvevIRSDLFEPFRGDKFDV 93


                 ..
gi 794205316 127 IL 128
Cdd:PRK14968  94 IL 95
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 67-158 5.80e-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: 46.65  E-value: 5.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205316  67 TILDVGAGSGCHALALQES-GKEVSAIDISPLSVEVMK------LRGVKDARQVNLFDERFA--ETFDTIlmLMNGSgII 137
Cdd:cd02440    1 RVLDLGCGTGALALALASGpGARVTGVDISPVALELARkaaaalLADNVEVLKGDAEELPPEadESFDVI--ISDPP-LH 77

                         90       100
                 ....*....|....*....|.
gi 794205316 138 GRLENMPLFFRKMKQLLRPDG 158
Cdd:cd02440   78 HLVEDLARFLEEARRLLKPGG 98
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 67-194 2.10e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 46.26  E-value: 2.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205316   67 TILDVGAGSG--CHALALQE-SGKEVSAIDISPLSVEVMK-------LRGVK-DARQVNLFDERFA-ETFDTILMlmngS 134
Cdd:pfam13847   6 RVLDLGCGTGhlSFELAEELgPNAEVVGIDISEEAIEKARenaqklgFDNVEfEQGDIEELPELLEdDKFDVVIS----N 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 794205316  135 GIIGRLENMPLFFRKMKQLLRPDGCILMDS----SDLRYLFEDEDGSFLIDLAGDYYGEIDFRM 194
Cdd:pfam13847  82 CVLNHIPDPDKVLQEILRVLKPGGRLIISDpdslAELPAHVKEDSTYYAGCVGGAILKKKLYEL 145
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 54-176 2.24e-05

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 44.14  E-value: 2.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205316  54 PLLERTALAMAT----GTILDVGAGSGCHALAL-QESGKEVSAIDISPLSVEvmklRGVKDARQVNL------------F 116
Cdd:COG0500   12 PGLAALLALLERlpkgGRVLDLGCGTGRNLLALaARFGGRVIGIDLSPEAIA----LARARAAKAGLgnveflvadlaeL 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 794205316 117 DERFAETFDTILMlmngSGIIGRL--ENMPLFFRKMKQLLRPDG-CILMDSSDLRYLFEDEDG 176
Cdd:COG0500   88 DPLPAESFDLVVA----FGVLHHLppEEREALLRELARALKPGGvLLLSASDAAAALSLARLL 146
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 55-129 3.12e-05

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: 43.25  E-value: 3.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205316  55 LLERTALAMATGTILDVGAGSG--CHALALQESGKEVSAIDISPLSVEV----MKLRGVKDAR--QVNLFDERFAETFDT 126
Cdd:COG2813   40 LLLEHLPEPLGGRVLDLGCGYGviGLALAKRNPEARVTLVDVNARAVELaranAAANGLENVEvlWSDGLSGVPDGSFDL 119


                 ...
gi 794205316 127 ILM 129
Cdd:COG2813  120 ILS 122
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
66-166 3.97e-05

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 43.18  E-value: 3.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205316  66 GTILDVGAGSGCHALALQESGKEVSAIDISPLSVEVM-------KLRGVKDARqVNLFDERFAETFDTIL-----MLMNG 133
Cdd:PRK11207  32 GKTLDLGCGNGRNSLYLAANGFDVTAWDKNPMSIANLerikaaeNLDNLHTAV-VDLNNLTFDGEYDFILstvvlMFLEA 110

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 794205316 134 SGIIGRLENmplffrkMKQLLRPDGCIL----MDSSD 166
Cdd:PRK11207 111 KTIPGLIAN-------MQRCTKPGGYNLivaaMDTAD 140
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 67-127 8.45e-05

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 42.64  E-value: 8.45e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 794205316   67 TILDVGAGSGCHALALQESG-KEVSAIDISPLSVEVMK----LRGVKDARQVNLFDERFAETFDTI 127
Cdd:pfam06325 164 SVLDVGCGSGILAIAALKLGaKKVVGVDIDPVAVRAAKenaeLNGVEARLEVYLPGDLPKEKADVV 229
PRK12335 PRK12335
tellurite resistance protein TehB; Provisional
 66-143 1.44e-04

tellurite resistance protein TehB; Provisional


Pssm-ID: 183450 [Multi-domain]  Cd Length: 287  Bit Score: 42.24  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205316  66 GTILDVGAGSGCHALALQESGKEVSAIDISPLSVEvmKLRGVKDARQVN----LFDERFA---ETFDTI-----LMLMNG 133
Cdd:PRK12335 122 GKALDLGCGQGRNSLYLALLGFDVTAVDINQQSLE--NLQEIAEKENLNirtgLYDINSAsiqEEYDFIlstvvLMFLNR 199

                         90
                 ....*....|
gi 794205316 134 SGIIGRLENM 143
Cdd:PRK12335 200 ERIPAIIKNM 209
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 67-127 3.94e-04

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 40.53  E-value: 3.94e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 794205316  67 TILDVGAGSGCHALAL-QE-SGKEVSAIDISPLSVEV----MKLRGVKDAR--QVNLFDERFAETFDTI 127
Cdd:PRK09328 111 RVLDLGTGSGAIALALaKErPDAEVTAVDISPEALAVarrnAKHGLGARVEflQGDWFEPLPGGRFDLI 179
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 55-162 4.29e-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: 39.88  E-value: 4.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205316   55 LLERTALAMATGTILDVGAGSGCHALAL-QESGK-EVSAIDISPLSVEV----MKLRGVKDA--RQVNLFDERFAETFDT 126
Cdd:pfam05175  22 LLLEHLPKDLSGKVLDLGCGAGVLGAALaKESPDaELTMVDINARALESarenLAANGLENGevVASDVYSGVEDGKFDL 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 794205316  127 ILM---LMNGSGIIGRL-ENmplFFRKMKQLLRPDGCILM 162
Cdd:pfam05175 102 IISnppFHAGLATTYNVaQR---FIADAKRHLRPGGELWI 138
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 68-127 5.75e-04

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: 40.41  E-value: 5.75e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 794205316   68 ILDVGAGSGCHALAL--QESGKEVSAIDISPLSVEV----MKLRGVKDA---RQVNLFDERFAETFDTI 127
Cdd:TIGR00536 118 ILDLGTGSGCIALALayEFPNAEVIAVDISPDALAVaeenAEKNQLEHRvefIQSNLFEPLAGQKIDII 186
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 55-128 7.42e-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: 39.07  E-value: 7.42e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 794205316   55 LLERTALAMATGTILDVGAGSGCHALALQESGKEVSAIDISPLSVEVMKLRGVKDARQVNLFDERFAE----TFDTIL 128
Cdd:TIGR00537  10 LLEANLRELKPDDVLEIGAGTGLVAIRLKGKGKCILTTDINPFAVKELRENAKLNNVGLDVVMTDLFKgvrgKFDVIL 87
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 64-128 1.00e-03

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 39.36  E-value: 1.00e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 794205316  64 ATGTILDVGAGSGC--HALALQESGKEVSAIDISPLSVEV----MKLRGVKDA---RQVNLFDE-RFAETFDTIL 128
Cdd:COG2890  112 APPRVLDLGTGSGAiaLALAKERPDARVTAVDISPDALAVarrnAERLGLEDRvrfLQGDLFEPlPGDGRFDLIV 186
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 67-164 1.56e-03

Mycolic acid cyclopropane synthetase; This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyze the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 38.85  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205316   67 TILDVGAGSGCHAL-ALQESGKEVSAIDIS----PLSVEVMKLRGVKDARQVNLFD-ERFAETFDTILMlmngsgiIGRL 140
Cdd:pfam02353  64 TLLDIGCGWGGLMRrAAERYDVNVVGLTLSknqyKLARKRVAAEGLARKVEVLLQDyRDFDEPFDRIVS-------VGMF 136

                          90       100
                  ....*....|....*....|....*....
gi 794205316  141 E-----NMPLFFRKMKQLLRPDGCILMDS 164
Cdd:pfam02353 137 EhvgheNYDTFFKKLYNLLPPGGLMLLHT 165
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
67-162 3.48e-03

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 37.82  E-value: 3.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205316  67 TILDVGAGSGCHALALQESG-KEVSAIDISPLSVEV----MKLRGVKDARQVNLFDERfaetFDTIL--MLmngSGIIGR 139
Cdd:PRK00517 122 TVLDVGCGSGILAIAAAKLGaKKVLAVDIDPQAVEAarenAELNGVELNVYLPQGDLK----ADVIVanIL---ANPLLE 194

                         90       100
                 ....*....|....*....|...
gi 794205316 140 LenMPLFfrkmKQLLRPDGCILM 162
Cdd:PRK00517 195 L--APDL----ARLLKPGGRLIL 211
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
66-161 3.49e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 37.71  E-value: 3.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205316  66 GTILDVGAGSGCHA-LALQESGKEVSAIDISPLSVEVmklrgvkdARQV---NLFDER------------FAETFDTILM 129
Cdd:COG4076   37 DVVLDIGTGSGLLSmLAARAGAKKVYAVEVNPDIAAV--------ARRIiaaNGLSDRitvinadatdldLPEKADVIIS 108

                         90       100       110
                 ....*....|....*....|....*....|...
gi 794205316 130 LMNGSGIIGrlENM-PLFFRKMKQLLRPDGCIL 161
Cdd:COG4076  109 EMLDTALLD--EGQvPILNHARKRLLKPGGRII 139
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
55-162 7.96e-03

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 36.69  E-value: 7.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205316  55 LLERTALAMATgtILDVGAGSGCHALALQESG-KEVSAIDISPLSVEV----MKLRGVKD---ARQVNLFDErfaETFDT 126
Cdd:COG2264  141 ALEKLLKPGKT--VLDVGCGSGILAIAAAKLGaKRVLAVDIDPVAVEAarenAELNGVEDrieVVLGDLLED---GPYDL 215

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 794205316 127 IL--MLmngSGIIgrLENMPLffrkMKQLLRPDGCILM 162
Cdd:COG2264  216 VVanIL---ANPL--IELAPD----LAALLKPGGYLIL 244
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 67-105 8.75e-03

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 36.35  E-value: 8.75e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 794205316  67 TILDVGAGSGCHALALQESGKEVSAIDISPLSVEVMKLR 105
Cdd:PRK07580  66 RILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARER 104
 
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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