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Q83HT0 (SYR_TROW8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 68. 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:TW419
OrganismTropheryma whipplei (strain TW08/27) (Whipple's bacillus) [Complete proteome] [HAMAP]
Taxonomic identifier218496 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeTropheryma

Protein attributes

Sequence length550 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 – 550550Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000242117

Regions

Motif122 – 13211"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q83HT0 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 28C4A5E032A5A0EF

FASTA55062,760
        10         20         30         40         50         60 
MEDLKKSVTN IVHSMYNFDC SEIVSLTRPP KPEYGDWALS LPLKLASLLK SPAIDIAQSI 

        70         80         90        100        110        120 
ASALLELDGV QDVYVAKPGF INLKLSREHT TGIISEVLEQ GSSFGRNTTQ SSKKINLEFV 

       130        140        150        160        170        180 
SGNPTGPLHL AHTRWAAVGD SIARILINCG ADVTREYYIN NVGNQIHLFS ESVYARALSK 

       190        200        210        220        230        240 
SLPKDGYPGE YVKDIARRIQ CEFPNIIDLS YEDAIKIFRK RSWQIQIEEI KKSCIAFRVN 

       250        260        270        280        290        300 
FDVWFSEESL HEPDRFGKSQ IDKALARCKQ NGYLFQKNGA FFIRTTEFGD DKDRAVLRSD 

       310        320        330        340        350        360 
TSYTYYAADC AYYLNKINRG FSDLVILVGA DHHGYVKRFQ AMSNIFHVDS ENNRKNVQVL 

       370        380        390        400        410        420 
LGQMVSLKNK RQSKREGNVI GLSEIIQSVG VDPLRFWFCR YPIDTPIDLD EQHLKKRSND 

       430        440        450        460        470        480 
NPVYYVQYAY ARTRSLIRSA NLLQMEKFGF FPELLVHETE TALVSLLYDY KTVVIDAARF 

       490        500        510        520        530        540 
LQPHRVVRYL ESLAGAYHKW YDKCRIIPRK GILDKSEAEL VNTRLELNRA VGQVLYNALD 

       550 
LIGVSAPERM 

« Hide

References

[1]"Sequencing and analysis of the genome of the Whipple's disease bacterium Tropheryma whipplei."
Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G., Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A., Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J., Relman D.A.
Lancet 361:637-644(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TW08/27.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX251411 Genomic DNA. Translation: CAD67089.1.
RefSeqNP_789351.1. NC_004551.1.

3D structure databases

ProteinModelPortalQ83HT0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING218496.TW419.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD67089; CAD67089; TW419.
GeneID1064262.
KEGGtws:TW419.
PATRIC23999313. VBITroWhi42739_0485.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMAMEHMGFG.
OrthoDBEOG6JB13C.

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.
InterProIPR001278. 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.
ProtoNetSearch...

Entry information

Entry nameSYR_TROW8
AccessionPrimary (citable) accession number: Q83HT0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 68 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