ID   SYRC_CRIGR              Reviewed;         661 AA.
AC   P37880;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 129.
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, RRS1;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=8224869; DOI=10.1016/0378-1119(93)90201-d;
RA   Lazard M., Mirande M.;
RT   "Cloning and analysis of a cDNA encoding mammalian arginyl-tRNA synthetase,
RT   a component of the multisynthetase complex with a hydrophobic N-terminal
RT   extension.";
RL   Gene 132:237-245(1993).
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Complexed;
CC         IsoId=P37880-1; Sequence=Displayed;
CC       Name=Monomeric; Synonyms=Free;
CC         IsoId=P37880-2; Sequence=VSP_018904;
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   -!- MISCELLANEOUS: [Isoform Monomeric]: The alternative initiation site
CC       Met-74 is uncertain. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; X63415; CAA45012.1; -; mRNA.
DR   RefSeq; XP_007632694.1; XM_007634504.2.
DR   AlphaFoldDB; P37880; -.
DR   SMR; P37880; -.
DR   STRING; 10029.XP_007632694.1; -.
DR   Ensembl; ENSCGRT00001003508; ENSCGRP00001002597; ENSCGRG00001002920. [P37880-1]
DR   eggNOG; KOG4426; Eukaryota.
DR   GeneTree; ENSGT00530000063407; -.
DR   OrthoDB; 463402at2759; -.
DR   SABIO-RK; P37880; -.
DR   GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; ISS:UniProtKB.
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:0004814; F:arginine-tRNA ligase activity; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; ISS:UniProtKB.
DR   CDD; cd00671; ArgRS_core; 1.
DR   Gene3D; 3.30.1360.70; -; 1.
DR   Gene3D; 3.40.50.620; -; 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   PANTHER; PTHR11956; PTHR11956; 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; SSF47323; 1.
DR   SUPFAM; SSF55190; SSF55190; 1.
DR   TIGRFAMs; TIGR00456; argS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative initiation; Aminoacyl-tRNA synthetase;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..661
FT                   /note="Arginine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000035795"
FT   REGION          1..73
FT                   /note="Could be involved in the assembly of the
FT                   multisynthetase complex"
FT   REGION          530..544
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000250|UniProtKB:Q05506"
FT   MOTIF           202..213
FT                   /note="'HIGH' region"
FT   BINDING         201..203
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   BINDING         212
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   BINDING         385
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   BINDING         389
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   BINDING         413
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"
FT   VAR_SEQ         1..73
FT                   /note="Missing (in isoform Monomeric)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_018904"
SQ   SEQUENCE   661 AA;  75602 MW;  12EB1C85655EB8F4 CRC64;
     MDGLVAQCSA RLLQQEKEIK SLTAEIDRLK NCGHLEDSPS LDQLREENLK LKYRLNILQR
     SLQAEKRRRP TKNMININSR LQDVFGCAIK AAYPDLDNPP LVVTPSQQPK FGDYQCNSAM
     GISQMLKAKE QKVNPRGIAE NITKHLPNNE YIDRVEIAGP GFINVHLRKD FVSEQLTNLL
     VNGIQLPALG ENKKVIVDFS SPNIAKEMHV GHLRSTIIGE SMSRLFEFAG YDVLRLNHVG
     DWGTQFGMLI AHLQDQFPDY LTVSPPIGDL QAFYKESKKR FDTEEEFKKR AYQCVVSLQS
     KDPDFIKAWN LICDVSRAEF NKIYDALDIT LIERGESFYQ DRMKDIVKEF EDKGYVQVDD
     GRKIVFVPGC SIPLTIVKSD GGFTYDTSDL AAIKQRLFEE KANKIIYVVD NGQAVHFQTI
     FAAAQMIGWY DPKVTQVTHV GFGVVLGEDK KKFKTRSGET VRLVDLLGEG LKRSMDKLKE
     KERDKVLTEE ELTAAQTSIA YGCIKYADLS HNRLNDYIFS FDKMLDDRGN TAAYLLYAFT
     RIRSIARLAN VDEEMLQKAA RETKIVLDHE KEWKLGRCIL RFPEILQKML DDLFLHTLCD
     YIYELATTFT EFYDSCYCVE KDRQTGKVLK VNMWRMLLCE AVAAVMAKGF DILGIKPVQR
     M