ID   SYRC_RAT                Reviewed;         660 AA.
AC   P40329; B1WBX8;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 2.
DT   27-MAR-2024, entry version 130.
DE   RecName: Full=Arginine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.19 {ECO:0000250|UniProtKB:P54136};
DE   AltName: Full=Arginyl-tRNA synthetase;
DE            Short=ArgRS;
GN   Name=Rars1; Synonyms=Rars;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Brown Norway/NHsdMcwi; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 73-92.
RX   PubMed=2187187; DOI=10.1073/pnas.87.10.3665;
RA   Sivaram P., Deutscher M.P.;
RT   "Existence of two forms of rat liver arginyl-tRNA synthetase suggests
RT   channeling of aminoacyl-tRNA for protein synthesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:3665-3669(1990).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=25467976; DOI=10.1007/s10735-014-9601-4;
RA   Park B.S., Jo H.W., Jung J.;
RT   "Expression profile of aminoacyl-tRNA synthetases in dorsal root ganglion
RT   neurons after peripheral nerve injury.";
RL   J. Mol. Histol. 46:115-122(2015).
CC   -!- FUNCTION: Forms part of a macromolecular complex that catalyzes the
CC       attachment of specific amino acids to cognate tRNAs during protein
CC       synthesis. Modulates the secretion of AIMP1 and may be involved in
CC       generation of the inflammatory cytokine EMAP2 from AIMP1.
CC       {ECO:0000250|UniProtKB:P54136}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-
CC         tRNA(Arg); Xref=Rhea:RHEA:20301, Rhea:RHEA-COMP:9658, Rhea:RHEA-
CC         COMP:9673, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78513, ChEBI:CHEBI:456215;
CC         EC=6.1.1.19; Evidence={ECO:0000250|UniProtKB:P54136};
CC   -!- SUBUNIT: Interacts (via N-terminus) with AIMP1 (via N-terminus); this
CC       stimulates its catalytic activity. Interacts (via N-terminus) with
CC       LARS2 (via C-terminus). Monomer. Part of a multisubunit complex that
CC       groups tRNA ligases for Arg (RARS1), Asp (DARS1), Gln (QARS1), Ile
CC       (IARS1), Leu (LARS1), Lys (KARS1), Met (MARS1) the bifunctional ligase
CC       for Glu and Pro (EPRS1) and the auxiliary subunits AIMP1/p43, AIMP2/p38
CC       and EEF1E1/p18. Interacts with QARS1. Part of a complex composed of
CC       RARS1, QARS1 and AIMP1. {ECO:0000250|UniProtKB:P54136}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P54136}.
CC       Cytoplasm, cytosol {ECO:0000250|UniProtKB:P54136}.
CC   -!- TISSUE SPECIFICITY: Detected in dorsal root ganglion.
CC       {ECO:0000269|PubMed:25467976}.
CC   -!- DOMAIN: The alpha-helical N-terminus (residues 1-72) mediates
CC       interaction with AIMP1 and thereby contributes to the assembly of the
CC       multisynthetase complex. {ECO:0000250|UniProtKB:P54136}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; BC161929; AAI61929.1; -; mRNA.
DR   PIR; A35857; A35857.
DR   RefSeq; NP_001099247.2; NM_001105777.2.
DR   AlphaFoldDB; P40329; -.
DR   SMR; P40329; -.
DR   BioGRID; 252058; 1.
DR   STRING; 10116.ENSRNOP00000010252; -.
DR   iPTMnet; P40329; -.
DR   PhosphoSitePlus; P40329; -.
DR   jPOST; P40329; -.
DR   PaxDb; 10116-ENSRNOP00000010252; -.
DR   Ensembl; ENSRNOT00000010252.7; ENSRNOP00000010252.4; ENSRNOG00000007739.7.
DR   Ensembl; ENSRNOT00055004721; ENSRNOP00055003492; ENSRNOG00055003032.
DR   Ensembl; ENSRNOT00060004779; ENSRNOP00060003440; ENSRNOG00060002943.
DR   Ensembl; ENSRNOT00065015631; ENSRNOP00065011800; ENSRNOG00065009729.
DR   GeneID; 287191; -.
DR   KEGG; rno:287191; -.
DR   UCSC; RGD:1309215; rat.
DR   AGR; RGD:1309215; -.
DR   CTD; 5917; -.
DR   RGD; 1309215; Rars1.
DR   eggNOG; KOG4426; Eukaryota.
DR   GeneTree; ENSGT00530000063407; -.
DR   HOGENOM; CLU_006406_5_1_1; -.
DR   InParanoid; P40329; -.
DR   OMA; CKSMLAW; -.
DR   OrthoDB; 67085at2759; -.
DR   PhylomeDB; P40329; -.
DR   TreeFam; TF106111; -.
DR   BRENDA; 6.1.1.19; 5301.
DR   PRO; PR:P40329; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000007739; Expressed in jejunum and 20 other cell types or tissues.
DR   GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IDA:CAFA.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0034618; F:arginine binding; IDA:RGD.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IDA:RGD.
DR   GO; GO:0005524; F:ATP binding; IDA:RGD.
DR   GO; GO:0000049; F:tRNA binding; IDA:RGD.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IDA:RGD.
DR   CDD; cd00671; ArgRS_core; 1.
DR   Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00123; Arg_tRNA_synth; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR001278; Arg-tRNA-ligase.
DR   InterPro; IPR005148; Arg-tRNA-synth_N.
DR   InterPro; IPR036695; Arg-tRNA-synth_N_sf.
DR   InterPro; IPR035684; ArgRS_core.
DR   InterPro; IPR008909; DALR_anticod-bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   NCBIfam; TIGR00456; argS; 1.
DR   PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR   PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF03485; Arg_tRNA_synt_N; 1.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF00750; tRNA-synt_1d; 1.
DR   PRINTS; PR01038; TRNASYNTHARG.
DR   SMART; SM01016; Arg_tRNA_synt_N; 1.
DR   SMART; SM00836; DALR_1; 1.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF55190; Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR   Genevisible; P40329; RN.
PE   1: Evidence at protein level;
KW   Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW   Direct protein sequencing; Ligase; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..660
FT                   /note="Arginine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000151660"
FT   REGION          1..72
FT                   /note="Could be involved in the assembly of the
FT                   multisynthetase complex"
FT                   /evidence="ECO:0000250"
FT   REGION          529..543
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000250|UniProtKB:Q05506"
FT   MOTIF           201..212
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000250"
FT   BINDING         200..202
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   BINDING         211
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   BINDING         384
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   BINDING         388
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   BINDING         412
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
SQ   SEQUENCE   660 AA;  75810 MW;  3C2D718AECDC4655 CRC64;
     MDGLVAQCSA RLLQQEKEIK SLTAEIDRLK NCSYLEASPS LEQLREENLK LKYRLNILRR
     SLQAERKRPT KNMININSRL QELFGCAIKA AYPDLENPPL VVTPSQQPKF GDYQCNSAMG
     ISQMLKAKEQ KVSPREIAEN ITKHLPNNEY IDRVEIAGPG FINVHLRKDF VSEQLTNLLV
     NGVQLPVLGE NEKVIVDFSS PNIAKEMHVG HLRSTIIGES MSRLFEFAGY NVLRLNHVGD
     WGTQFGMLIA HLQDKFPDYL TVSPPIGDLQ AFYKESKKRF DTEEEFKKRA YECVVLLQSK
     NPDIMKAWNL ICDVSREEFN KIYDALDITL IERGESFYQD RMKDIVKEFE DKGFVQVDDG
     RKIVFVPGCS VPLTIVKSDG GYTYDTSDLA AIKQRLFEEK ANKIIYVVDN GQATHFQTVF
     AAAQMIGWYD PKVTRVAHVG FGVVLGEDKK KFKTRSGETV RLMDLLEEGL RRSMDKLKEK
     ERDKVLTEEE LKAAQTSVAY GCIKYADLSH NRLNDYVFSF DKMLDDRGNT AAYLLYAFTR
     IRSIARLANI DEEMLQRAAR ETKIILDHEK EWKLGRCILR FPEILQKILD DLFLHTLCDY
     IYELATTFTE FYDSCYCVEK DRQTGKVLKV NMWRMLLCEA VAAVMAKGFD ILGIKPVQRM
//