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Q4L425 (SYR_STAHJ) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 61. 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:SH2293
OrganismStaphylococcus haemolyticus (strain JCSC1435) [Complete proteome] [HAMAP]
Taxonomic identifier279808 [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_0000242097

Regions

Motif130 – 14011"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q4L425 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: 22E2A63CF0D16039

FASTA55362,093
        10         20         30         40         50         60 
MNIIEKVKST LIEEIKASIE KANLAEDIPE IKVEIPKDTK NGDYSTNIAM VLTKVAKRNP 

        70         80         90        100        110        120 
REIAQAIVDN LDTSKANVKQ VDIAGPGFIN FYLDNQYLTA VIPEAINKGD KFGCAEESKN 

       130        140        150        160        170        180 
TNILLEYVSA NPTGDLHIGH ARNAAVGDSL ANILIAAGYN VTREYYINDA GNQITNLARS 

       190        200        210        220        230        240 
IETRFFEALG DTSHEMPADG YNGKDIIEIG KDLADKHPEM KDYSDEERLK TFRQLGVDYE 

       250        260        270        280        290        300 
MDKLKKDLAD FNVHFDNWFS ETSLYENGAI DNTLAKMNEL GYTYEADGAT WLRTSDFKDD 

       310        320        330        340        350        360 
KDRVLIKKDG TYTYFTPDTA YHYNKINRGN DILIDLMGAD HHGYINRLKA SLETFGVDSN 

       370        380        390        400        410        420 
RLEIQIMQMV RLMQDGVEVK MSKRTGNAIT LREIMDEVGI DAARYFLTMR SPDSHFDFDL 

       430        440        450        460        470        480 
ELAKEKSQDN PIYYAQYAHA RICSILKQAK EQGVEVTADA DFSTITNEKA IDLLKKVAEF 

       490        500        510        520        530        540 
EPTIESAAEN RAPHRLTNYI QDLASAFHKF YNAEKVLTDD AEKTKAHIAL VDAVRITLHN 

       550 
ALALVGVSAP ESM 

« Hide

References

[1]"Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species."
Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.
J. Bacteriol. 187:7292-7308(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCSC1435.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006716 Genomic DNA. Translation: BAE05602.1.
RefSeqYP_254208.1. NC_007168.1.

3D structure databases

ProteinModelPortalQ4L425.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279808.SH2293.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE05602; BAE05602; SH2293.
GeneID3482386.
KEGGsha:SH2293.
PATRIC19620677. VBIStaHae67511_2258.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMAYNARENG.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycSHAE279808:GJX7-2351-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_STAHJ
AccessionPrimary (citable) accession number: Q4L425
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: August 2, 2005
Last modified: April 16, 2014
This is version 61 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