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A2SJR5 (TRMB_METPP) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 42. 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:Mpe_A2850
OrganismMethylibium petroleiphilum (strain PM1) [Complete proteome] [HAMAP]
Taxonomic identifier420662 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesMethylibium

Protein attributes

Sequence length469 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 – 469469tRNA (guanine-N(7)-)-methyltransferase HAMAP-Rule MF_01057
PRO_0000288178

Regions

Region1 – 221221Unknown HAMAP-Rule MF_01057
Region222 – 469248tRNA (guanine-N(7)-)-methyltransferase HAMAP-Rule MF_01057
Region433 – 4364Substrate binding By similarity

Sites

Active site3621 By similarity
Binding site2871S-adenosyl-L-methionine By similarity
Binding site3121S-adenosyl-L-methionine By similarity
Binding site3391S-adenosyl-L-methionine By similarity
Binding site3621S-adenosyl-L-methionine By similarity
Binding site3661Substrate By similarity
Binding site3981Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A2SJR5 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: E173CAD6CD3C08D3

FASTA46950,968
        10         20         30         40         50         60 
MRGGAHGPGD RAGRCREHRQ DHAGPCAGAG APFARPAGHA GGRVPARVLR RARPHAAARG 

        70         80         90        100        110        120 
TGRHRRRAMA SHRGRRAGRS HRAGRHHAAD DRGLQRVRVR RPQSLPPGAR APAPLRPHAA 

       130        140        150        160        170        180 
DRPRPGLAAR RPAARRRPGA RPGRPLGPRR AGLCRAALFG GLWRRLGAHG SRCGCAAPAA 

       190        200        210        220        230        240 
APARPGGPRA RRPAAAWPLP RMPAARMRTS VVRVRGEAPI AMSEPDSSSP PAHPPRPIRS 

       250        260        270        280        290        300 
FVLRAGRMGS GQTRALAELG PRFVLPFQRE PLDPQTVFGR RAPRVFEIGF GMGDATAQIA 

       310        320        330        340        350        360 
AARPDTDFIG CEVHTPGVGA LLKQIGEREL TNLRIVQHDA VEVLDHMIEP GSLAGIHLFF 

       370        380        390        400        410        420 
PDPWHKKKHH KRRLVQPAFV ERLVTRLAPG GYLHCATDWQ PYAEQMLEVL GAEPALRNSA 

       430        440        450        460 
DGYAPRPEYR PLTKFEQRGL RLGHGVWDLV FTKHQGRSAS KQCTATSSP 

« Hide

References

[1]"Whole-genome analysis of the methyl tert-butyl ether-degrading beta-proteobacterium Methylibium petroleiphilum PM1."
Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W., Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M., Hristova K.R.
J. Bacteriol. 189:1931-1945(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PM1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000555 Genomic DNA. Translation: ABM95804.1.
RefSeqYP_001022039.1. NC_008825.1.

3D structure databases

ProteinModelPortalA2SJR5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING420662.Mpe_A2850.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM95804; ABM95804; Mpe_A2850.
GeneID4785544.
KEGGmpt:Mpe_A2850.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0220.
KOK03439.
OrthoDBEOG6K6VBC.

Enzyme and pathway databases

BioCycMPET420662:GHBE-2884-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_METPP
AccessionPrimary (citable) accession number: A2SJR5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: March 6, 2007
Last modified: June 11, 2014
This is version 42 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