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B0BW17 (SYR_RICRO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 42. 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:RrIowa_0123
OrganismRickettsia rickettsii (strain Iowa) [Complete proteome] [HAMAP]
Taxonomic identifier452659 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length576 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 – 576576Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000076226

Regions

Motif126 – 13611"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
B0BW17 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: B4BD631836470C02

FASTA57665,142
        10         20         30         40         50         60 
MNIFNQLKQD IIVASKQLYN NQAIANTATI DIPKDSFNGD LSSNVAMIIA AKESIAPREV 

        70         80         90        100        110        120 
ALKFKEVLIT LPYIASIEIA GPGFINFTIK ADSWQASIKD ILQHEEKFFE IDIDKSRNIN 

       130        140        150        160        170        180 
IEYVSANPTG PMHIGHARGA VYGDVLARIL QKVSYSVTKE YYVNDAGSQI NDLVSTVLLR 

       190        200        210        220        230        240 
YKEALGEQIT IPAGLYPGEY LIPLGQILAK EYGNKLLTMN YDERFKIIKS FAVEKMLDLN 

       250        260        270        280        290        300 
RKDLADLGIK HDIFFSEQSL HDKGEIEETV KLLESMGLIY EGTLPAPKGK IHEEWDNRVQ 

       310        320        330        340        350        360 
KLFKSTKYGD SQDRPIEKAD GSWSYFASDL AYAKDKIERG ANHLIYVLGA DHSGYVKRIE 

       370        380        390        400        410        420 
AIVKALGKEQ VKVDVKICQL VNFVENGVPV KMSKRLGSFA SVQDVNNEVG KDIIRFMMLT 

       430        440        450        460        470        480 
RQNDKPLDFD LVKVKEQSRE NPIFYVQYAH VRTISILSKA RELMPESYNN FESGKYDLSL 

       490        500        510        520        530        540 
LSSEEEIEII KLLVSWTKTL EASAKYFEPH RIAFYLINLA SKFHSMWNFG KENSEYRFVI 

       550        560        570 
ESNKELTLAR LALASAIQKV IASGLEVIGV EPMNKM 

« Hide

References

[1]"Genomic comparison of virulent Rickettsia rickettsii Sheila Smith and avirulent Rickettsia rickettsii Iowa."
Ellison D.W., Clark T.R., Sturdevant D.E., Virtaneva K., Porcella S.F., Hackstadt T.
Infect. Immun. 76:542-550(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Iowa.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000766 Genomic DNA. Translation: ABY72043.1.
RefSeqYP_001649449.1. NC_010263.2.

3D structure databases

ProteinModelPortalB0BW17.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING452659.RrIowa_0123.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABY72043; ABY72043; RrIowa_0123.
GeneID5849492.
KEGGrrj:RrIowa_0123.
PATRIC17906138. VBIRicRic59104_0125.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMARFIMLTR.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycRRIC452659:GHSN-117-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_RICRO
AccessionPrimary (citable) accession number: B0BW17
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 26, 2008
Last modified: April 16, 2014
This is version 42 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