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Q9F411 (TRMB_MYCHP) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
tRNA (guanine-N(7)-)-methyltransferase

EC=2.1.1.33
Alternative name(s):
tRNA (guanine(46)-N(7))-methyltransferase
tRNA(m7G46)-methyltransferase
Gene names
Name:trmB
Ordered Locus Names:MHO_4250
OrganismMycoplasma hominis (strain ATCC 23114 / NBRC 14850 / NCTC 10111 / PG21) [Complete proteome] [HAMAP]
Taxonomic identifier347256 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma

Protein attributes

Sequence length202 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA By similarity. HAMAP-Rule MF_01057

Catalytic activity

S-adenosyl-L-methionine + guanine46 in tRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine46 in tRNA. HAMAP-Rule MF_01057

Pathway

tRNA modification; N(7)-methylguanine-tRNA biosynthesis. HAMAP-Rule MF_01057

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family.

Ontologies

Keywords
   Biological processtRNA processing
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Molecular_functiontRNA (guanine-N7-)-methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 202202tRNA (guanine-N(7)-)-methyltransferase HAMAP-Rule MF_01057
PRO_0000171352

Regions

Region181 – 1844Substrate binding Potential

Sites

Active site1071 By similarity
Binding site341S-adenosyl-L-methionine By similarity
Binding site591S-adenosyl-L-methionine By similarity
Binding site861S-adenosyl-L-methionine By similarity
Binding site1071S-adenosyl-L-methionine By similarity
Binding site1111Substrate By similarity
Binding site1431Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9F411 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: D8993C44B381BB0B

FASTA20223,951
        10         20         30         40         50         60 
MRLRFNKNAE TSLMASPMTF KDFPIDNKKN TILEIGMGRG TMLTKLALMH PDIEYIGLEK 

        70         80         90        100        110        120 
YSTPAYSALK KAIDLNLENF HIIIGDAINL STYFKNKIKT IWLTFSDPWP KKRHYKRRLV 

       130        140        150        160        170        180 
YRDFLKIYQN VLDKDGVVYF KTDNDMLYQF AIDELKEINA KIIYQTSDLH HCNFKIENVF 

       190        200 
TDYEEKFNKL NKNINFIAFT FN 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and nucleotide sequence of the DNA gyrase (gyrA) gene from Mycoplasma hominis and characterization of quinolone-resistant mutants selected In vitro with trovafloxacin."
Bebear C.M., Grau O., Charron A., Renaudin H., Gruson D., Bebear C.
Antimicrob. Agents Chemother. 44:2719-2727(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Life on arginine for Mycoplasma hominis: clues from its minimal genome and comparison with other human urogenital mycoplasmas."
Pereyre S., Sirand-Pugnet P., Beven L., Charron A., Renaudin H., Barre A., Avenaud P., Jacob D., Couloux A., Barbe V., de Daruvar A., Blanchard A., Bebear C.
PLoS Genet. 5:E1000677-E1000677(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 23114 / NBRC 14850 / NCTC 10111 / PG21.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U59880 Genomic DNA. Translation: AAG28841.1.
FP236530 Genomic DNA. Translation: CAX37560.1.
RefSeqYP_003302963.1. NC_013511.1.

3D structure databases

ProteinModelPortalQ9F411.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING2098.MHO_4250.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAX37560; CAX37560; MHO_4250.
GeneID8595146.
KEGGmho:MHO_4250.
PATRIC32274019. VBIMycHom120329_0443.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0220.
HOGENOMHOG000251689.
KOK03439.
OMAGCGKGEY.
OrthoDBEOG6K6VBC.

Enzyme and pathway databases

BioCycMHOM347256:GBZD-466-MONOMER.
UniPathwayUPA00989.

Family and domain databases

Gene3D3.40.50.150. 1 hit.
HAMAPMF_01057. tRNA_methyltr_TrmB.
InterProIPR029063. SAM-dependent_MTases-like.
IPR003358. tRNA_(Gua-N-7)_MeTrfase.
[Graphical view]
PfamPF02390. Methyltransf_4. 1 hit.
[Graphical view]
SUPFAMSSF53335. SSF53335. 1 hit.
TIGRFAMsTIGR00091. TIGR00091. 1 hit.
PROSITEPS51625. SAM_MT_TRMB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRMB_MYCHP
AccessionPrimary (citable) accession number: Q9F411
Secondary accession number(s): D1J8L3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: March 1, 2001
Last modified: June 11, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways