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P40329 (SYRC_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 77. 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, cytoplasmic

EC=6.1.1.19
Alternative name(s):
Arginyl-tRNA synthetase
Short name=ArgRS
Gene names
Name:Rars
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length660 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis. Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1 By similarity. HAMAP-Rule MF_00123

Catalytic activity

ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg). HAMAP-Rule MF_00123

Subunit structure

Interacts (via N-terminus) with AIMP1 (via N-terminus); this stimulates its catalytic activity. Interacts with EPRS (via N-terminus). Interacts with LARS2. Monomer; also part of a multisubunit complex that groups tRNA ligases for Arg, Asp, Glu, Gln, Ile, Leu, Lys, Met and Pro By similarity.

Subcellular location

Cytoplasm HAMAP-Rule MF_00123.

Domain

The N-terminus (AA 1-72) has two regions predicted to be alpha-helical that might be involved in the multisynthetase complex assembly By similarity. HAMAP-Rule MF_00123

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 660660Arginine--tRNA ligase, cytoplasmic HAMAP-Rule MF_00123
PRO_0000151660

Regions

Region1 – 7272Could be involved in the assembly of the multisynthetase complex By similarity
Motif201 – 21212"HIGH" region By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity

Sequences

Sequence LengthMass (Da)Tools
P40329 [UniParc].

Last modified July 13, 2010. Version 2.
Checksum: 3C2D718AECDC4655

FASTA66075,810
        10         20         30         40         50         60 
MDGLVAQCSA RLLQQEKEIK SLTAEIDRLK NCSYLEASPS LEQLREENLK LKYRLNILRR 

        70         80         90        100        110        120 
SLQAERKRPT KNMININSRL QELFGCAIKA AYPDLENPPL VVTPSQQPKF GDYQCNSAMG 

       130        140        150        160        170        180 
ISQMLKAKEQ KVSPREIAEN ITKHLPNNEY IDRVEIAGPG FINVHLRKDF VSEQLTNLLV 

       190        200        210        220        230        240 
NGVQLPVLGE NEKVIVDFSS PNIAKEMHVG HLRSTIIGES MSRLFEFAGY NVLRLNHVGD 

       250        260        270        280        290        300 
WGTQFGMLIA HLQDKFPDYL TVSPPIGDLQ AFYKESKKRF DTEEEFKKRA YECVVLLQSK 

       310        320        330        340        350        360 
NPDIMKAWNL ICDVSREEFN KIYDALDITL IERGESFYQD RMKDIVKEFE DKGFVQVDDG 

       370        380        390        400        410        420 
RKIVFVPGCS VPLTIVKSDG GYTYDTSDLA AIKQRLFEEK ANKIIYVVDN GQATHFQTVF 

       430        440        450        460        470        480 
AAAQMIGWYD PKVTRVAHVG FGVVLGEDKK KFKTRSGETV RLMDLLEEGL RRSMDKLKEK 

       490        500        510        520        530        540 
ERDKVLTEEE LKAAQTSVAY GCIKYADLSH NRLNDYVFSF DKMLDDRGNT AAYLLYAFTR 

       550        560        570        580        590        600 
IRSIARLANI DEEMLQRAAR ETKIILDHEK EWKLGRCILR FPEILQKILD DLFLHTLCDY 

       610        620        630        640        650        660 
IYELATTFTE FYDSCYCVEK DRQTGKVLKV NMWRMLLCEA VAAVMAKGFD ILGIKPVQRM 

« Hide

References

« Hide 'large scale' references
[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Brown Norway/NHsdMcwi.
Tissue: Liver.
[2]"Existence of two forms of rat liver arginyl-tRNA synthetase suggests channeling of aminoacyl-tRNA for protein synthesis."
Sivaram P., Deutscher M.P.
Proc. Natl. Acad. Sci. U.S.A. 87:3665-3669(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 73-92.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC161929 mRNA. Translation: AAI61929.1.
PIRA35857.
RefSeqNP_001099247.2. NM_001105777.2.
UniGeneRn.18711.

3D structure databases

ProteinModelPortalP40329.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid252058. 1 interaction.
STRING10116.ENSRNOP00000010252.

Proteomic databases

PRIDEP40329.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000010252; ENSRNOP00000010252; ENSRNOG00000007739.
GeneID287191.
KEGGrno:287191.
UCSCRGD:1309215. rat.

Organism-specific databases

CTD5917.
RGD1309215. Rars.

Phylogenomic databases

GeneTreeENSGT00530000063407.
HOGENOMHOG000247212.
HOVERGENHBG029238.
KOK01887.
OMAKCFDILG.
OrthoDBEOG764725.
PhylomeDBP40329.
TreeFamTF106111.

Gene expression databases

GenevestigatorP40329.

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...

Other

NextBio625686.

Entry information

Entry nameSYRC_RAT
AccessionPrimary (citable) accession number: P40329
Secondary accession number(s): B1WBX8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 13, 2010
Last modified: May 14, 2014
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries