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Q2SYE0 (TRMB_BURTA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:BTH_I1513
OrganismBurkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [Complete proteome] [HAMAP]
Taxonomic identifier271848 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group ›

Protein attributes

Sequence length265 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 methyltransferase superfamily. TrmB family.

Ontologies

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

Inferred from electronic annotation. Source: GOC

   Molecular_functiontRNA (guanine-N7-)-methyltransferase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 265265tRNA (guanine-N(7)-)-methyltransferase HAMAP-Rule MF_01057
PRO_0000288130

Regions

Region241 – 2444Substrate binding Potential

Sites

Binding site951S-adenosyl-L-methionine By similarity
Binding site1201S-adenosyl-L-methionine By similarity
Binding site1471S-adenosyl-L-methionine By similarity
Binding site1701S-adenosyl-L-methionine By similarity
Binding site1741Substrate By similarity
Binding site2061Substrate Potential

Sequences

Sequence LengthMass (Da)Tools
Q2SYE0 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 346228F881714D97

FASTA26529,365
        10         20         30         40         50         60 
MNHDDPNASG VPHDDANDAA PASASDAARA TGHADDESSP LHLRRIRSFV TRAGRVSTGQ 

        70         80         90        100        110        120 
RRAIDELGPR FVVPYDNAQP DWDTVFGRRA PRVLEIGFGM GASTAEIAAH RPGDDFIGVE 

       130        140        150        160        170        180 
VHEPGVGALL KLIGEQQLSN IRIIQHDAVE VLEHMIAPDS LDGAHIFFPD PWHKARHHKR 

       190        200        210        220        230        240 
RLIQPPFVAQ LAARLKPGAY LHCATDWQNY AEQMLEVLGA DPSLENTAQD YAPRPDYRPV 

       250        260 
TKFERRGLRL GHGVWDLVFR KKRAG

« Hide

References

[1]"Bacterial genome adaptation to niches: divergence of the potential virulence genes in three Burkholderia species of different survival strategies."
Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., DeShazer D.
BMC Genomics 6:174-174(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E264 / ATCC 700388 / DSM 13276 / CIP 106301.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000086 Genomic DNA. Translation: ABC36287.1.
RefSeqYP_442059.1. NC_007651.1.

3D structure databases

ProteinModelPortalQ2SYE0.
ModBaseSearch...

Protein-protein interaction databases

STRING271848.BTH_I1513.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC36287; ABC36287; BTH_I1513.
GeneID3846934.
KEGGbte:BTH_I1513.
PATRIC19305976. VBIBurTha36512_4296.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0220.
HOGENOMHOG000073968.
KOK03439.
OMACEVHEPG.
ProtClustDBPRK00121.

Enzyme and pathway databases

BioCycBTHA271848:GJMY-1513-MONOMER.
UniPathwayUPA00989.

Family and domain databases

HAMAPMF_01057. tRNA_methyltr_TrmB.
InterProIPR003358. tRNA_(Gua-N-7)_MeTrfase.
[Graphical view]
PfamPF02390. Methyltransf_4. 1 hit.
[Graphical view]
TIGRFAMsTIGR00091. TIGR00091. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTRMB_BURTA
AccessionPrimary (citable) accession number: Q2SYE0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: January 24, 2006
Last modified: May 1, 2013
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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