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B2S5B0 (SYR_BRUA1) Reviewed, UniProtKB/Swiss-Prot

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

EC=6.1.1.19
Alternative name(s):
Arginyl-tRNA synthetase
Short name=ArgRS
Gene names
Name:argS
Ordered Locus Names:BAbS19_I08360
OrganismBrucella abortus (strain S19) [Complete proteome] [HAMAP]
Taxonomic identifier430066 [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_1000095339

Regions

Motif131 – 14111"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
B2S5B0 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 354143BD9F45FD56

FASTA58565,186
        10         20         30         40         50         60 
MNIFADFDAR IKKTFQDIDL 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 KLPPPKGRLP 

       310        320        330        340        350        360 
EDWEDREQTL FRSTEVGDDI DRPLMKSDGS FTYFAGDVTY FKDKYDRGFN EMIYVLGADH 

       370        380        390        400        410        420 
GGYVKRLEAV ARAVSDGKAK LTVLLCQLVK LFRNGEPVRM 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 FHSQWNRGAE 

       550        560        570        580 
NPDLRFIKVN DPDLSLARLG LVQVVSDVLT SGLTIIGADA PTEMR 

« Hide

References

[1]"Genome sequence of Brucella abortus vaccine strain S19 compared to virulent strains yields candidate virulence genes."
Crasta O.R., Folkerts O., Fei Z., Mane S.P., Evans C., Martino-Catt S., Bricker B., Yu G., Du L., Sobral B.W.
PLoS ONE 3:E2193-E2193(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: S19.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000887 Genomic DNA. Translation: ACD72357.1.
RefSeqYP_001934831.1. NC_010742.1.

3D structure databases

ProteinModelPortalB2S5B0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING430066.BAbS19_I08360.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD72357; ACD72357; BAbS19_I08360.
GeneID6327997.
KEGGbmc:BAbS19_I08360.
PATRIC17818732. VBIBruAbo38055_2136.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMAIRNTIND.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycBABO430066:GHI6-828-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_BRUA1
AccessionPrimary (citable) accession number: B2S5B0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 2008
Last modified: May 14, 2014
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

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries