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Q3BQ14 (TRMB_XANC5) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 59. 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:XCV3418
OrganismXanthomonas campestris pv. vesicatoria (strain 85-10) [Complete proteome] [HAMAP]
Taxonomic identifier316273 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length341 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 – 341341tRNA (guanine-N(7)-)-methyltransferase HAMAP-Rule MF_01057
PRO_0000229210

Regions

Region156 – 1616Interaction with RNA Potential

Sites

Active site1501 By similarity
Binding site751S-adenosyl-L-methionine By similarity
Binding site1001S-adenosyl-L-methionine By similarity
Binding site1271S-adenosyl-L-methionine By similarity
Binding site1501S-adenosyl-L-methionine By similarity
Binding site1541Substrate By similarity
Binding site1861Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3BQ14 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: E76B4ECAC980211E

FASTA34138,568
        10         20         30         40         50         60 
MTDPFTSDGA KMPPKPFTVE EGRRQVRSFV LRQGRFTPAQ QRAFDDLWPR FGLDYTGAPR 

        70         80         90        100        110        120 
DLAATFGRDA HKVLEIGFGN GAALRFAAQQ DPSRDYIGIE VHAPGVGRLL NALDEDGSTH 

       130        140        150        160        170        180 
VRLYHHDAVE VLEHEIADGA LDEVRIYFPD PWHKKRHNKR RLIQPAFAQL LVRKLREGGR 

       190        200        210        220        230        240 
LHAATDWADY AEQMWDVLDA TPGLVNRAGP RGHVERPAWR PQTHFETRGQ KLGHGVWDLL 

       250        260        270        280        290        300 
YDRDSGIGNR KGNCPRRPDN PQRPQFSLCQ FPIPDSPFPA PNGHRADADQ RYEARPRAGR 

       310        320        330        340 
FHDGDVPVRA HSRRRGGIDR AGGLGRHRTG GAGRIVRRFL R 

« Hide

References

[1]"Insights into genome plasticity and pathogenicity of the plant pathogenic Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete genome sequence."
Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D., Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C., Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H., Niesbach-Kloesgen U. expand/collapse author list , Patschkowski T., Rueckert C., Rupp O., Schneiker S., Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D., Kaiser O.
J. Bacteriol. 187:7254-7266(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 85-10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM039952 Genomic DNA. Translation: CAJ25149.1.
RefSeqYP_365149.1. NC_007508.1.

3D structure databases

ProteinModelPortalQ3BQ14.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316273.XCV3418.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ25149; CAJ25149; XCV3418.
GeneID3730268.
KEGGxcv:XCV3418.
PATRIC24096432. VBIXanCam71633_3685.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0220.
HOGENOMHOG000073968.
KOK03439.
OMAERKGARE.
OrthoDBEOG6K6VBC.
ProtClustDBPRK00121.

Enzyme and pathway databases

BioCycXCAM316273:GJF8-3521-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_XANC5
AccessionPrimary (citable) accession number: Q3BQ14
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: November 22, 2005
Last modified: April 16, 2014
This is version 59 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