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Protein

Arginine--tRNA ligase, cytoplasmic

Gene

Rars

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei211L-arginineBy similarity1
Binding sitei384L-arginineBy similarity1
Binding sitei388L-arginineBy similarity1
Binding sitei412L-arginineBy similarity1

GO - Molecular functioni

  • arginine binding Source: RGD
  • arginine-tRNA ligase activity Source: RGD
  • ATP binding Source: RGD
  • cadherin binding Source: Ensembl
  • tRNA binding Source: RGD

GO - Biological processi

  • arginyl-tRNA aminoacylation Source: RGD

Keywordsi

Molecular functionAminoacyl-tRNA synthetase, Ligase
Biological processProtein biosynthesis
LigandATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Arginine--tRNA ligase, cytoplasmic (EC:6.1.1.19By similarity)
Alternative name(s):
Arginyl-tRNA synthetase
Short name:
ArgRS
Gene namesi
Name:Rars
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi1309215. Rars.

Subcellular locationi

  • Cytoplasm By similarity
  • Cytoplasmcytosol By similarity

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001516601 – 660Arginine--tRNA ligase, cytoplasmicAdd BLAST660

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP40329.
PRIDEiP40329.

PTM databases

iPTMnetiP40329.
PhosphoSitePlusiP40329.

Expressioni

Tissue specificityi

Detected in dorsal root ganglion.1 Publication

Gene expression databases

BgeeiENSRNOG00000007739.
GenevisibleiP40329. RN.

Interactioni

Subunit structurei

Interacts (via N-terminus) with AIMP1 (via N-terminus); this stimulates its catalytic activity. Interacts (via N-terminus) with LARS2 (via C-terminus). Monomer. Part of a multisubunit complex that groups tRNA ligases for Arg (RARS), Asp (DARS), Gln (QARS), Ile (IARS), Leu (LARS), Lys (KARS), Met (MARS) the bifunctional ligase for Glu and Pro (EPRS) and the auxiliary subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18. Interacts with QARS. Part of a complex composed of RARS, QARS and AIMP1.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi252058. 1 interactor.
STRINGi10116.ENSRNOP00000010252.

Structurei

3D structure databases

ProteinModelPortaliP40329.
SMRiP40329.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 72Could be involved in the assembly of the multisynthetase complexBy similarityAdd BLAST72
Regioni200 – 202L-arginine bindingBy similarity3
Regioni529 – 543Interaction with tRNABy similarityAdd BLAST15

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi201 – 212"HIGH" regionBy similarityAdd BLAST12

Domaini

The alpha-helical N-terminus (residues 1-72) mediates interaction with AIMP1 and thereby contributes to the assembly of the multisynthetase complex.By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1195. Eukaryota.
COG0018. LUCA.
GeneTreeiENSGT00530000063407.
HOGENOMiHOG000247212.
HOVERGENiHBG029238.
InParanoidiP40329.
KOiK01887.
OMAiNKPLHLG.
OrthoDBiEOG091G03A6.
PhylomeDBiP40329.
TreeFamiTF106111.

Family and domain databases

CDDicd00671. ArgRS_core. 1 hit.
Gene3Di1.10.730.10. 1 hit.
3.30.1360.70. 1 hit.
3.40.50.620. 1 hit.
HAMAPiMF_00123. Arg_tRNA_synth. 1 hit.
InterProiView protein in InterPro
IPR001412. aa-tRNA-synth_I_CS.
IPR001278. Arg-tRNA-ligase.
IPR005148. Arg-tRNA-synth_N.
IPR035684. ArgRS_core.
IPR008909. DALR_anticod-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_Ia_anticodon-bd.
PANTHERiPTHR11956. PTHR11956. 1 hit.
PfamiView protein in Pfam
PF03485. Arg_tRNA_synt_N. 1 hit.
PF05746. DALR_1. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
PRINTSiPR01038. TRNASYNTHARG.
SMARTiView protein in SMART
SM01016. Arg_tRNA_synt_N. 1 hit.
SM00836. DALR_1. 1 hit.
SUPFAMiSSF47323. SSF47323. 1 hit.
SSF55190. SSF55190. 1 hit.
TIGRFAMsiTIGR00456. argS. 1 hit.
PROSITEiView protein in PROSITE
PS00178. AA_TRNA_LIGASE_I. 1 hit.

Sequencei

Sequence statusi: Complete.

P40329-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDGLVAQCSA RLLQQEKEIK SLTAEIDRLK NCSYLEASPS LEQLREENLK
60 70 80 90 100
LKYRLNILRR SLQAERKRPT KNMININSRL QELFGCAIKA AYPDLENPPL
110 120 130 140 150
VVTPSQQPKF GDYQCNSAMG ISQMLKAKEQ KVSPREIAEN ITKHLPNNEY
160 170 180 190 200
IDRVEIAGPG FINVHLRKDF VSEQLTNLLV NGVQLPVLGE NEKVIVDFSS
210 220 230 240 250
PNIAKEMHVG HLRSTIIGES MSRLFEFAGY NVLRLNHVGD WGTQFGMLIA
260 270 280 290 300
HLQDKFPDYL TVSPPIGDLQ AFYKESKKRF DTEEEFKKRA YECVVLLQSK
310 320 330 340 350
NPDIMKAWNL ICDVSREEFN KIYDALDITL IERGESFYQD RMKDIVKEFE
360 370 380 390 400
DKGFVQVDDG RKIVFVPGCS VPLTIVKSDG GYTYDTSDLA AIKQRLFEEK
410 420 430 440 450
ANKIIYVVDN GQATHFQTVF AAAQMIGWYD PKVTRVAHVG FGVVLGEDKK
460 470 480 490 500
KFKTRSGETV RLMDLLEEGL RRSMDKLKEK ERDKVLTEEE LKAAQTSVAY
510 520 530 540 550
GCIKYADLSH NRLNDYVFSF DKMLDDRGNT AAYLLYAFTR IRSIARLANI
560 570 580 590 600
DEEMLQRAAR ETKIILDHEK EWKLGRCILR FPEILQKILD DLFLHTLCDY
610 620 630 640 650
IYELATTFTE FYDSCYCVEK DRQTGKVLKV NMWRMLLCEA VAAVMAKGFD
660
ILGIKPVQRM
Length:660
Mass (Da):75,810
Last modified:July 13, 2010 - v2
Checksum:i3C2D718AECDC4655
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC161929 mRNA. Translation: AAI61929.1.
PIRiA35857.
RefSeqiNP_001099247.2. NM_001105777.2.
UniGeneiRn.18711.

Genome annotation databases

EnsembliENSRNOT00000010252; ENSRNOP00000010252; ENSRNOG00000007739.
GeneIDi287191.
KEGGirno:287191.
UCSCiRGD:1309215. rat.

Similar proteinsi

Entry informationi

Entry nameiSYRC_RAT
AccessioniPrimary (citable) accession number: P40329
Secondary accession number(s): B1WBX8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 13, 2010
Last modified: August 30, 2017
This is version 102 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. SIMILARITY comments
    Index of protein domains and families