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Q5PMK3 (TRMB_SALPA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 63. 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:SPA2972
OrganismSalmonella paratyphi A (strain ATCC 9150 / SARB42) [Complete proteome] [HAMAP]
Taxonomic identifier295319 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length239 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

Subunit structure

Monomer By similarity. 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 – 239239tRNA (guanine-N(7)-)-methyltransferase HAMAP-Rule MF_01057
PRO_0000229194

Regions

Region150 – 1556Interaction with RNA Potential
Region217 – 2204Substrate binding By similarity

Sites

Active site1441 By similarity
Binding site691S-adenosyl-L-methionine By similarity
Binding site941S-adenosyl-L-methionine By similarity
Binding site1211S-adenosyl-L-methionine By similarity
Binding site1441S-adenosyl-L-methionine By similarity
Binding site1481Substrate By similarity
Binding site1801Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5PMK3 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: DA64534C17E54D99

FASTA23927,178
        10         20         30         40         50         60 
MKNDVISPEF DENGRPLRRI RSFVRRQGRL TKGQEHALEN YWPVMGVEFS EAPVDFATLF 

        70         80         90        100        110        120 
GREAPVTLEI GFGMGASLVA MVKARPEQNF LGIEVHSPGV GACLASAHEE GVENLRVMCH 

       130        140        150        160        170        180 
DAVEVLHKMI PDNSLSMVQL FFPDPWHKAR HNKRRIVQVP FAELVLSKLK LGGVFHMATD 

       190        200        210        220        230 
WEAYAEHMLE VMSSIDGYKN LSESNDYVPR PESRPVTKFE QRGHRLGHGV WDLMFERVK 

« Hide

References

[1]"Comparison of genome degradation in Paratyphi A and Typhi, human-restricted serovars of Salmonella enterica that cause typhoid."
McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F. expand/collapse author list , Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L., Spieth J., Wilson R.K.
Nat. Genet. 36:1268-1274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 9150 / SARB42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000026 Genomic DNA. Translation: AAV78810.1.
RefSeqYP_152122.1. NC_006511.1.

3D structure databases

ProteinModelPortalQ5PMK3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING295319.SPA2972.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV78810; AAV78810; SPA2972.
PATRIC32355521. VBISalEnt134188_3155.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0220.
HOGENOMHOG000073968.
OMATSATNDY.
OrthoDBEOG6K6VBC.

Enzyme and pathway databases

BioCycSENT295319:GJBZ-2970-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_SALPA
AccessionPrimary (citable) accession number: Q5PMK3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: January 4, 2005
Last modified: June 11, 2014
This is version 63 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