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A5VQ54 (SYR_BRUO2) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 46. 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:BOV_0868
OrganismBrucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512) [Complete proteome] [HAMAP]
Taxonomic identifier444178 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

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_1000017995

Regions

Motif131 – 14111"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
A5VQ54 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 9808782B7A563C5E

FASTA58564,971
        10         20         30         40         50         60 
MNIFADFDAR IKKTLQDIDL KPKDGGELDL SRIGVEPPRD ASHGDIATNA AMVLSKAVGQ 

        70         80         90        100        110        120 
NPRELAARIA EALKADEDVE SVDVAGPGFI NLRLKASYWQ RELLVMLNEG TDFGRSRLGA 

       130        140        150        160        170        180 
GKKVNVEYVS ANPTGPMHVG HCRGAVVGDV LANLLKFAGY DVVKEYYIND AGAQIDVLAR 

       190        200        210        220        230        240 
SVMLRYREAL GESIGEIPAG LYPGDYLVRV GQELAGEFGT KLLEMPEAEA LAIVKDRTID 

       250        260        270        280        290        300 
AMMAMIRADL DALNVHHDVF YSERKLHVDH ARAIRNAIND LTLKGHVYKG KLPPPKGQLP 

       310        320        330        340        350        360 
GDWEDCEQTL FRSTEVGDDI DRPLMKSDGS FTYFAGDVAY FKDKYDRGFN EMIYVLGADH 

       370        380        390        400        410        420 
GGYVKRLEAV ARAVSDGKAK LTVLLCQLVK LFRNGEPARM SKRAGEFITL RDVVDEVGRD 

       430        440        450        460        470        480 
PVRFMMLYRK NDAPLDFDFA KVTEQSKDNP VFYVQYASAR CHSVFRQAAD QLGLVDLDRV 

       490        500        510        520        530        540 
AMGSHFEKLT DESEIALVRK LAEYPRLIES AAIHQEPHRL AFYLYDLASS FHSQWNRGTE 

       550        560        570        580 
NPDLRFIKVN DPDLSLARLG LVQVVSDVLT SGLTIIGADA PTEMR 

« Hide

References

[1]Paulsen I.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25840 / 63/290 / NCTC 10512.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000708 Genomic DNA. Translation: ABQ61922.1.
RefSeqYP_001258851.1. NC_009505.1.

3D structure databases

ProteinModelPortalA5VQ54.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING444178.BOV_0868.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ61922; ABQ61922; BOV_0868.
GeneID5202079.
KEGGbov:BOV_0868.
PATRIC17861596. VBIBruOvi136990_2210.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMARFIMLTR.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycBOVI444178:GH2V-866-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_BRUO2
AccessionPrimary (citable) accession number: A5VQ54
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 10, 2007
Last modified: April 16, 2014
This is version 46 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