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A9IVK4 (SYR_BART1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 39. 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:
Arginine--tRNA ligase

EC=6.1.1.19
Alternative name(s):
Arginyl-tRNA synthetase
Short name=ArgRS
Gene names
Name:argS
Ordered Locus Names:BT_1372
OrganismBartonella tribocorum (strain CIP 105476 / IBS 506) [Complete proteome] [HAMAP]
Taxonomic identifier382640 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length585 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg). HAMAP-Rule MF_00123

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00123

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00123.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processarginyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

arginine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 585585Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000076204

Regions

Motif131 – 14111"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
A9IVK4 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 443851ABC38CF1EC

FASTA58566,474
        10         20         30         40         50         60 
MNIFKNFEKK IKKSIELSDI KGKNGEDLDL SKITVDPPRD SSHGHLSTNA AMVLAKSIGL 

        70         80         90        100        110        120 
SPRALADKII ELLKNDISIE NIDVAGPGFI NIKLTKLFWQ DAVKYMLELG LSYGRIPMGQ 

       130        140        150        160        170        180 
GKRINVEYVS ANPTGPMHVG HCRGAVVGDV LSNLLQFAGY NITKEYYIND AGQQIEVLAH 

       190        200        210        220        230        240 
SVLLRYREAL GQKINEIPEG LYPGEYLIPL GQALAQEFGD QLLTMDRDEA LSIVKERAIH 

       250        260        270        280        290        300 
TMMSMIREDL AALNIYHDIF FSERMLYADN ARAIRNTIND LTLNGYIYKG KLPPPKGQNI 

       310        320        330        340        350        360 
EDWEPSEQTL FRSTNVGDDQ DRVLIKSDGS YTYFAADVAY FRDKFNRHFD EMIYILGADH 

       370        380        390        400        410        420 
AGYVKRLEAM AKAISGNKAK LSVFLCQLVK LFRNGQPVRM SKRAGSFVTL RDVVEEVGRD 

       430        440        450        460        470        480 
PVRFMMLYRK CEAPLDFDFA KVTEQSKDNP IFYVQYANAR CHSVFRQAQE VLHIESFSND 

       490        500        510        520        530        540 
ILITYLHRLI DDNEILLIRK LSEYPRIIEQ AVVHKEPHRL AFYLYDLASC FHTHWNKGSE 

       550        560        570        580 
NLNLRFIQPH DKELSFARLG LIQAVINILS SGLSIIGVEA PIEMR 

« Hide

References

[1]"Genomic analysis of Bartonella identifies type IV secretion systems as host adaptability factors."
Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G., Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.
Nat. Genet. 39:1469-1476(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CIP 105476 / IBS 506.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM260525 Genomic DNA. Translation: CAK01734.1.
RefSeqYP_001609729.1. NC_010161.1.

3D structure databases

ProteinModelPortalA9IVK4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING382640.Btr_1372.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5829367.
KEGGbtr:Btr_1372.
PATRIC20550545. VBIBarTri113218_1414.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
KOK01887.
OMAIRNTIND.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycBTRI382640:GJEK-1242-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.30.1360.70. 1 hit.
3.40.50.620. 1 hit.
HAMAPMF_00123. Arg_tRNA_synth.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR001278. Arg-tRNA-ligase.
IPR005148. Arg-tRNA-synth_N.
IPR008909. DALR_anticod-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
PANTHERPTHR11956. PTHR11956. 1 hit.
PfamPF03485. Arg_tRNA_synt_N. 1 hit.
PF05746. DALR_1. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view]
PRINTSPR01038. TRNASYNTHARG.
SMARTSM01016. Arg_tRNA_synt_N. 1 hit.
SM00836. DALR_1. 1 hit.
[Graphical view]
SUPFAMSSF47323. SSF47323. 1 hit.
SSF55190. SSF55190. 1 hit.
TIGRFAMsTIGR00456. argS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYR_BART1
AccessionPrimary (citable) accession number: A9IVK4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: May 14, 2014
This is version 39 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

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries