Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q0ACP5 (TRMB_ALHEH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 40. 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:Mlg_0033
OrganismAlkalilimnicola ehrlichei (strain MLHE-1) [Complete proteome] [HAMAP]
Taxonomic identifier187272 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesEctothiorhodospiraceaeAlkalilimnicola

Protein attributes

Sequence length237 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 MF_01057

Catalytic activity

S-adenosyl-L-methionine + guanine(46) in tRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine(46) in tRNA. HAMAP MF_01057

Pathway

tRNA modification; N(7)-methylguanine-tRNA biosynthesis. HAMAP MF_01057

Sequence similarities

Belongs to the 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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 237237tRNA (guanine-N(7)-)-methyltransferase HAMAP MF_01057
PRO_0000288116

Regions

Region212 – 2154Substrate binding Potential

Sites

Binding site651S-adenosyl-L-methionine By similarity
Binding site901S-adenosyl-L-methionine By similarity
Binding site1171S-adenosyl-L-methionine By similarity
Binding site1401S-adenosyl-L-methionine By similarity
Binding site1441Substrate By similarity
Binding site1761Substrate Potential

Sequences

Sequence LengthMass (Da)Tools
Q0ACP5 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 00A03E61CD8CA2E2

FASTA23727,016
        10         20         30         40         50         60 
MERRADAATG KRPIRSFVRR EGRLTAGQQR ALELLWPAFG LERPPAGQPL DLDRAFGRRA 

        70         80         90        100        110        120 
PRILEIGFGN GESLAEQAAT HPERDYLGIE VHRPGVGHLL MEVEKRHLGN VRVMMADAAE 

       130        140        150        160        170        180 
VLAHHIPDGS LHGVQLFFPD PWPKKRHHKR RLVQPQWVRA VAAKLAPGGF LHLATDWADY 

       190        200        210        220        230 
AEHMLDVLEA EPDLENTCGP RQFSPRGERP ETKFERRGLR KGHQVFDLYY RKREHPG 

« Hide

References

[1]"Complete sequence of Alkalilimnicola ehrilichei MLHE-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MLHE-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000453 Genomic DNA. Translation: ABI55392.1.
RefSeqYP_740882.1. NC_008340.1.

3D structure databases

ProteinModelPortalQ0ACP5.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0ACP5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4268890.
GenomeReviewsGene locus Mlg_0033 in contig CP000453_GR.
KEGGaeh:Mlg_0033.
NMPDRfig|187272.6.peg.32.
PATRIC20859236. VBIAlkEhr114327_0033.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0220.
HOGENOMHBG322782.
OMAAPGYKNQ.
PhylomeDBQ0ACP5.
ProtClustDBPRK00121.

Enzyme and pathway databases

BioCycAEHR187272:MLG_0033-MONOMER.

Family and domain databases

HAMAPMF_01057. tRNA_methyltr_TrmB.
[Tree]
InterProIPR003358. tRNA_(Gua-N-7)_MeTrfase.
[Graphical view]
KOK03439.
PfamPF02390. Methyltransf_4. 1 hit.
[Graphical view]
TIGRFAMsTIGR00091. TIGR00091. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTRMB_ALHEH
AccessionPrimary (citable) accession number: Q0ACP5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: October 17, 2006
Last modified: January 25, 2012
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families