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Q5HRD1 (SYR_STAEQ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 65. 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:SERP0262
OrganismStaphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]
Taxonomic identifier176279 [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_0000151612

Regions

Motif130 – 14011"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q5HRD1 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: D1550EBE0308FAB2

FASTA55362,545
        10         20         30         40         50         60 
MSIIDQVKQT LIEEIEVSIR KANLAEDIPE IKIEIPKDPK NGDYSSNIAM VLTKIAKRNP 

        70         80         90        100        110        120 
REIAQAIVDH LDTSKAHVKQ VDIAGPGFIN FYLDNQYLTA IIPEAITKGD RFGYATQSKN 

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

       190        200        210        220        230        240 
IEARYFEALG DTSYEMPADG YNGKDIIEIG KDLAVKHPEI KDYTDEERLK TFRQLGVDYE 

       250        260        270        280        290        300 
MEKLKKDLSD FNVHFDNWFS ETSLYENGAI ENTLSKMKEL GYTYEADGAT WLRTSDFKDD 

       310        320        330        340        350        360 
KDRVLIKKDG NYTYFTPDTA YHYNKINRGN DILIDLMGAD HHGYINRLKA SLETFGVDSD 

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

       430        440        450        460        470        480 
ELAKEQSQDN PIYYAQYAHA RICSILKQAK EQGIEVSTDA DFSKINNDKA IDLLKKVAEF 

       490        500        510        520        530        540 
ESTIESAAEH RAPHRLTNYI QDLAAAFHKF YNAEKVLTDD TEKTKAYVAM IEAVRITLHN 

       550 
ALALVGVTAP ESM 

« Hide

References

[1]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35984 / RP62A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000029 Genomic DNA. Translation: AAW53688.1.
RefSeqYP_187858.1. NC_002976.3.

3D structure databases

ProteinModelPortalQ5HRD1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING176279.SERP0262.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW53688; AAW53688; SERP0262.
GeneID3241307.
KEGGser:SERP0262.
PATRIC19611407. VBIStaEpi130894_0250.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMAMEHMGFG.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycSEPI176279:GJJB-282-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_STAEQ
AccessionPrimary (citable) accession number: Q5HRD1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: February 15, 2005
Last modified: May 14, 2014
This is version 65 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