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Q5HNG2 (TRMB_STAEQ) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 68. 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:SERP1307
OrganismStaphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]
Taxonomic identifier176279 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length215 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 – 215215tRNA (guanine-N(7)-)-methyltransferase HAMAP-Rule MF_01057
PRO_0000171395

Regions

Region190 – 1934Substrate binding By similarity

Sites

Active site1171 By similarity
Binding site431S-adenosyl-L-methionine By similarity
Binding site681S-adenosyl-L-methionine By similarity
Binding site951S-adenosyl-L-methionine By similarity
Binding site1171S-adenosyl-L-methionine By similarity
Binding site1211Substrate By similarity
Binding site1531Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HNG2 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: B771F6EAA004E72D

FASTA21525,716
        10         20         30         40         50         60 
MRVRYKPWAE DYLKNHPDLV DMDGAHAGKM SEWFEKEQPI YIEIGSGMGQ FITTLAAQYP 

        70         80         90        100        110        120 
EINFVSMERE KSVMYKVLDK TKEMGLKNLK MICNDAIELN EYFKDKEISR IYLNFSDPWP 

       130        140        150        160        170        180 
KKRHAKRRLT YHTYLALYKQ ILKDDGEIHF KTDNRGLFAF SIESMSQFGM YFTKMNLNLH 

       190        200        210 
DEDDEDNIVT EYEKKFSEKG SRIYRMEAKF HKCFE 

« Hide

References

[1]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35984 / RP62A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000029 Genomic DNA. Translation: AAW54627.1.
RefSeqYP_188879.1. NC_002976.3.

3D structure databases

ProteinModelPortalQ5HNG2.
SMRQ5HNG2. Positions 9-210.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING176279.SERP1307.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW54627; AAW54627; SERP1307.
GeneID3241839.
KEGGser:SERP1307.
PATRIC19613465. VBIStaEpi130894_1275.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0220.
HOGENOMHOG000251689.
KOK03439.
OMAKTDDDEL.
OrthoDBEOG6K6VBC.
ProtClustDBPRK00121.

Enzyme and pathway databases

BioCycSEPI176279:GJJB-1334-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.
PROSITEPS51625. SAM_MT_TRMB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRMB_STAEQ
AccessionPrimary (citable) accession number: Q5HNG2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: February 15, 2005
Last modified: April 16, 2014
This is version 68 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