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A5XG48 (A5XG48_BURMA) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Putative arginyl-tRNA--protein transferase HAMAP MF_00689

Short name=Arginyltransferase HAMAP MF_00689
Short name=R-transferase HAMAP MF_00689
EC=2.3.2.8 HAMAP MF_00689
Gene names
Name:ate HAMAP MF_00689
ORF Names:BMAFMH_C0779 EMBL EDK56535.1
OrganismBurkholderia mallei FMH EMBL EDK56535.1
Taxonomic identifier334802 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length276 AA.
Sequence statusComplete.
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 By similarity. HAMAP MF_00689 SAAS SAAS007472

Catalytic activity

L-arginyl-tRNA + protein = tRNA + L-arginyl-protein. HAMAP MF_00689 SAAS SAAS007472

Subcellular location

Cytoplasm By similarity HAMAP MF_00689 SAAS SAAS007472.

Sequence similarities

Belongs to the R-transferase family. HAMAP MF_00689

Ontologies

Keywords
   Cellular componentCytoplasm HAMAP MF_00689 SAAS SAAS007472
   Molecular functionAcyltransferase HAMAP MF_00689 SAAS SAAS007472
Transferase
Gene Ontology (GO)
   Biological processprotein arginylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionarginyltransferase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
A5XG48 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: A453F2CA29198D6A

FASTA27631,209
        10         20         30         40         50         60 
MTHPTELPLS PLSALQFYAT APYPCSYLDG RVARSQVATP SHLINSDIYT ELVKAGFRRS 

        70         80         90        100        110        120 
GVFTYRPYCD GCRACVPVRV PVDAFAPNRT QRRTWKRHRA LVATVAALHY DEEHYALYMR 

       130        140        150        160        170        180 
YQSARHAGGG MDRDSRDQYE QFLLQSRINS RLVEFRDLDP AENGASTLRM VSMIDILGDG 

       190        200        210        220        230        240 
LSSVYTFFDP DESHASYGTY NILWQIEQAK SLRLPYVYLG YWIRESPKMA YKANFHPLEG 

       250        260        270 
LVDGRWKVLD PTLADLPPVD AALARAPLPG GHSGTR 

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References

[1]DeShazer D., Woods D.E., Nierman W.C.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: FMH EMBL EDK56535.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS264094 Genomic DNA. Translation: EDK56535.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

PATRIC26911335. VBIBurMal45758_0452.

Phylogenomic databases

OMAYAMMVED.

Family and domain databases

HAMAPMF_00689. Ate.
[Tree]
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR007472. 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.
SUPFAMSSF55729. Acyl_CoA_acyltransferase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameA5XG48_BURMA
AccessionPrimary (citable) accession number: A5XG48
Entry history
Integrated into UniProtKB/TrEMBL: July 10, 2007
Last sequence update: July 10, 2007
Last modified: December 14, 2011
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)