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Q2K975 (SYR_RHIEC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 50. 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:RHE_CH01818
OrganismRhizobium etli (strain CFN 42 / ATCC 51251) [Complete proteome] [HAMAP]
Taxonomic identifier347834 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

Protein attributes

Sequence length585 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 – 585585Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000242076

Regions

Motif131 – 14111"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q2K975 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: E73EC4BCFAA93325

FASTA58564,687
        10         20         30         40         50         60 
MNLFTDFEAR IKTALEQIDL VREKRSELDF GRIAVEPPRD ASHGDVATNA AMVLAKPLGT 

        70         80         90        100        110        120 
NPRALADVII AKLKEDADVA DVSVAGPGFI NIRLAVGYWQ RLLASIIGAG IDYGRSSLGE 

       130        140        150        160        170        180 
GRTVNVEYVS ANPTGPMHVG HCRGAVVGDA LANLLAFAGY GVEKEYYIND AGSQIDVLAR 

       190        200        210        220        230        240 
SVFLRYREAL GERIGEIPSG LYPGDYLVPV GQSLAADYGV RLHNMPEEEW MPIVKDRTID 

       250        260        270        280        290        300 
AMMAMIREDL AALNVHHDIF FSERTLHANG AAAIRTAIND LTFKGYVYKG TLPPPKGQLP 

       310        320        330        340        350        360 
EDWEDREQTL FRSTEVGDDI DRPLIKSDGS YTYFAADVAY FKNKFDRGFE EMIYVLGADH 

       370        380        390        400        410        420 
GGYVKRLEAV ARGVSDGKAK LTVLLCQLVK LYRNGEPVKM SKRSGDFVTL RDVVEEVGRD 

       430        440        450        460        470        480 
SVRFMMLYRK NSEPLDFDFA KVTEQSKDNP VFYVQYAHAR CMSVFRQAKE AFAGLDVSPE 

       490        500        510        520        530        540 
DLAKAVAGIE DPAELQLVAK LAEFPRIIES AAQSQEPHRI AFYLYDLASA FHAHWNKGKD 

       550        560        570        580 
QPELRFVNDK NRESTIARLG LVYAVASVLK SGLAITGTAA PDEMR 

« Hide

References

[1]"The partitioned Rhizobium etli genome: genetic and metabolic redundancy in seven interacting replicons."
Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I., Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A., Jimenez-Jacinto V., Collado-Vides J., Davila G.
Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CFN 42 / ATCC 51251.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000133 Genomic DNA. Translation: ABC90611.1.
RefSeqYP_469338.1. NC_007761.1.

3D structure databases

ProteinModelPortalQ2K975.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING347834.RHE_CH01818.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC90611; ABC90611; RHE_CH01818.
GeneID3893858.
KEGGret:RHE_CH01818.
PATRIC23085101. VBIRhiEtl108884_2212.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMANPNGPLH.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycRETL347834:GJJ0-1829-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_RHIEC
AccessionPrimary (citable) accession number: Q2K975
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: March 7, 2006
Last modified: April 16, 2014
This is version 50 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