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Reviewed, UniProtKB/Swiss-Prot A3M311 (ATE_ACIBT)

Last modified October 13, 2009. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Putative arginyl-tRNA--protein transferase
      Short name=R-transferase
      Short name=Arginyltransferase
    EC=2.3.2.8
Gene names
Name: ate
Ordered Locus Names: A1S_0873
OrganismAcinetobacter baumannii (strain ATCC 17978 / NCDC KC 755) [Complete proteome] [HAMAP]
Taxonomic identifier400667 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

Protein attributes

Sequence length271 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

May conjugate Arg from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate Potential.

Catalytic activity

L-arginyl-tRNA + protein = tRNA + L-arginyl-protein. HAMAP MF_00689

Subcellular location

Cytoplasm Potential.

Sequence similarities

Belongs to the R-transferase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processprotein arginylation

Inferred from electronic annotation. Source: InterPro

translation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionacyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

arginyltransferase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 271271Putative arginyl-tRNA--protein transferase HAMAP MF_00689
PRO_1000131966

Sequences

Sequence LengthMass (Da)Tools
A3M311-1 [UniParc].

Last modified September 2, 2008. Version 2.
Checksum: 34C388D1209F57B7

FASTA27131,947
        10         20         30         40         50         60 
MKSYHPKSLL NDLQYYITPP HDCSYLENKS ARMVFLDPIH RIDVVTLSEL SRLGFRRSGD 

        70         80         90        100        110        120 
FVYRPECHLC RQCLSCRVPV ADFQMNSMQK KAWKRNQDLT MTVLPTRQAS QIHYDLYERY 

       130        140        150        160        170        180 
INERHADGDM FPPSLDQFEK FLVHSCTDSF FLELWKDNRL ISVSTCDLMD DGLSAVYTFF 

       190        200        210        220        230        240 
DPDEHRRSLG VYSILNQIEY VKTLGLEYVY LGYWVPHSAK MNYKSQYTPL ELLLDGQWRR 

       250        260        270 
LNRSLSPEEI NQLGNSLMTT LPSEWNNLII K 

« Hide

References

[1]"New insights into Acinetobacter baumannii pathogenesis revealed by high-density pyrosequencing and transposon mutagenesis."
Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N., Gerstein M., Snyder M.
Genes Dev. 21:601-614(2007) [PubMed: 17344419] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000521 Genomic DNA. Translation: ABO11305.2.
RefSeqYP_001083907.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA3M311.

Genome annotation databases

GeneID4917144.
GenomeReviewsGene locus A1S_0873 in contig CP000521_GR.
KEGGacb:A1S_0873.
NMPDRfig|400667.4.peg.896.

Organism-specific databases

CMRSearch...

Family and domain databases

HAMAPMF_00689.
[Tree]
InterProIPR007472. Arg-tRNA-P_Trfase_C.
IPR017138. Arg-tRNA-P_Trfase_prd_prok.
IPR007471. Arg_tRNA_PTrfase_N.
[Graphical view]
PfamPF04377. ATE_C. 1 hit.
PF04376. ATE_N. 1 hit.
[Graphical view]
PIRSFPIRSF037208. ATE_pro_prd. 1 hit.
ProtoNetSearch...

Entry information

Entry nameATE_ACIBT
AccessionPrimary (citable) accession number: A3M311
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 2, 2008
Last modified: October 13, 2009
This is version 29 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents