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A7WZ56 (SYR_STAA1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 45. 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:SAHV_0605
OrganismStaphylococcus aureus (strain Mu3 / ATCC 700698) [Complete proteome] [HAMAP]
Taxonomic identifier418127 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length553 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 – 553553Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000018125

Regions

Motif130 – 14011"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
A7WZ56 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: E6F27FBD94CDA9A9

FASTA55362,346
        10         20         30         40         50         60 
MNIIDQVKQT LVEEIAASIN KAGLADEIPD IKIEVPKDTK NGDYATNIAM VLTKIAKRNP 

        70         80         90        100        110        120 
REIAQAIVDN LDTEKAHVKQ IDIAGPGFIN FYLDNQYLTA IIPEAIEKGD QFGHVNESKG 

       130        140        150        160        170        180 
QNVLLEYVSA NPTGDLHIGH ARNAAVGDAL ANILTAAGYN VTREYYINDA GNQITNLARS 

       190        200        210        220        230        240 
IETHFFEALG DNSYSMPEDG YNGKDIIEIG KDLAEKHPEI KDYSEEARLK EFRKLGVEYE 

       250        260        270        280        290        300 
MAKLKNDLAE FNTHFDNWFS ETSLYEKGEI LEVLAKMKEL GYTYEADGAT WLRTTDFKDD 

       310        320        330        340        350        360 
KDRVLIKNDG TYTYFLPDIA YHFDKVKRGN DILIDLFGAD HHGYINRLKA SLETFGVDSN 

       370        380        390        400        410        420 
RLEIQIMQMV RLMENGKEVK MSKRTGNAIT LREIMDEVGV DAARYFLTMR SPDSHFDFDM 

       430        440        450        460        470        480 
ELAKEQSQDN PVYYAQYAHA RICSILKQAK EQGIEVTAAN DFTTITNEKA IELLKKVADF 

       490        500        510        520        530        540 
EPTIESAAEH RSAHRITNYI QDLAAHFHKF YNAEKVLTDD IEKTKAHVAM IEAVRITLKN 

       550 
ALAMVGVSAP ESM 

« Hide

References

[1]"Mutated response regulator graR is responsible for phenotypic conversion of Staphylococcus aureus from heterogeneous vancomycin-intermediate resistance to vancomycin-intermediate resistance."
Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.
Antimicrob. Agents Chemother. 52:45-53(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Mu3 / ATCC 700698.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009324 Genomic DNA. Translation: BAF77488.1.
RefSeqYP_001441195.1. NC_009782.1.

3D structure databases

ProteinModelPortalA7WZ56.
SMRA7WZ56. Positions 30-553.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING418127.SAHV_0605.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF77488; BAF77488; SAHV_0605.
GeneID5560321.
KEGGsaw:SAHV_0605.
PATRIC19556187. VBIStaAur127830_0614.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMAMEHMGFG.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycSAUR418127:GJP9-622-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_STAA1
AccessionPrimary (citable) accession number: A7WZ56
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 23, 2007
Last modified: May 14, 2014
This is version 45 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