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A0PMW8 (TRMB_MYCUA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 46. 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:MUL_1098
OrganismMycobacterium ulcerans (strain Agy99) [Complete proteome] [HAMAP]
Taxonomic identifier362242 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length278 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 – 278278tRNA (guanine-N(7)-)-methyltransferase HAMAP-Rule MF_01057
PRO_0000288184

Regions

Region256 – 2594Substrate binding By similarity

Sites

Active site1831 By similarity
Binding site1061S-adenosyl-L-methionine By similarity
Binding site1311S-adenosyl-L-methionine By similarity
Binding site1601S-adenosyl-L-methionine By similarity
Binding site1831S-adenosyl-L-methionine By similarity
Binding site1871Substrate By similarity
Binding site2191Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A0PMW8 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: B5B8C3B01B8A7630

FASTA27830,283
        10         20         30         40         50         60 
MRHDGPMHVQ PGVGLQSDTS SSTGTGSGPA DEPEAEKSAW GYLPPTAFRS RHSALSSIQQ 

        70         80         90        100        110        120 
QTWERRWPQL GRQATAHSQP SARGHEPIDP IDARAWFGRE APVVLEIGCG SGTSTLAMAQ 

       130        140        150        160        170        180 
AEPNVDVIAV EVYRRGLAQL LCAIDRADLQ RINIRLIRGN GIDVLRDLIA PESLTGVRVF 

       190        200        210        220        230        240 
FPDPWPKARH HKRRLIQPST VVLIADRLLP GGVFHAATDH PGYAEHIIAA GDAEPALARV 

       250        260        270 
DPGVDSLPVS VVRPTTKYEM KAHNAGSSIN ELIWKKQR 

« Hide

References

[1]"Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcer."
Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M. expand/collapse author list , Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.
Genome Res. 17:192-200(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Agy99.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000325 Genomic DNA. Translation: ABL03687.1.
RefSeqYP_905158.1. NC_008611.1.

3D structure databases

ProteinModelPortalA0PMW8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING362242.MUL_1098.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL03687; ABL03687; MUL_1098.
GeneID4553518.
KEGGmul:MUL_1098.
PATRIC18168975. VBIMycUlc37413_1348.

Organism-specific databases

GenoListMUL_1098.
CMRSearch...

Phylogenomic databases

eggNOGCOG0220.
HOGENOMHOG000073968.
KOK03439.
OMALDKDHTI.
OrthoDBEOG6K6VBC.
ProtClustDBPRK00121.

Enzyme and pathway databases

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_MYCUA
AccessionPrimary (citable) accession number: A0PMW8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: January 9, 2007
Last modified: April 16, 2014
This is version 46 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