ID   SYRC_BOVIN              Reviewed;         660 AA.
AC   A7YW98;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 102.
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 {ECO:0000250|UniProtKB:P54136};
GN   Name=RARS1; Synonyms=RARS {ECO:0000312|EMBL:AAI34469.1};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1] {ECO:0000312|EMBL:AAI34469.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford {ECO:0000312|EMBL:AAI34469.1};
RC   TISSUE=Thymus {ECO:0000312|EMBL:AAI34469.1};
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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   -!- 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:0000255}.
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DR   EMBL; BC134468; AAI34469.1; -; mRNA.
DR   RefSeq; NP_001098808.1; NM_001105338.2.
DR   AlphaFoldDB; A7YW98; -.
DR   SMR; A7YW98; -.
DR   STRING; 9913.ENSBTAP00000019475; -.
DR   PaxDb; 9913-ENSBTAP00000019475; -.
DR   PeptideAtlas; A7YW98; -.
DR   Ensembl; ENSBTAT00000019475.4; ENSBTAP00000019475.3; ENSBTAG00000014626.4.
DR   GeneID; 506305; -.
DR   KEGG; bta:506305; -.
DR   CTD; 5917; -.
DR   VEuPathDB; HostDB:ENSBTAG00000014626; -.
DR   VGNC; VGNC:33733; RARS1.
DR   eggNOG; KOG4426; Eukaryota.
DR   GeneTree; ENSGT00530000063407; -.
DR   HOGENOM; CLU_006406_5_1_1; -.
DR   InParanoid; A7YW98; -.
DR   OMA; CKSMLAW; -.
DR   OrthoDB; 67085at2759; -.
DR   TreeFam; TF106111; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000014626; Expressed in oocyte and 105 other cell types or tissues.
DR   GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
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; 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.
PE   2: Evidence at transcript level;
KW   Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..660
FT                   /note="Arginine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000395433"
FT   REGION          1..72
FT                   /note="Could be involved in the assembly of the
FT                   multisynthetase complex"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
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|UniProtKB:P54136"
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;  75561 MW;  EA5DCB46414C81C1 CRC64;
     MDALVAHCSA RLLQQEKEIK FLTAEVDRLK NYSCSEASAD LEKLREENLK LKYRLNILRK
     SLQAERNKPT KTMININSCL EEVFGCAIKA AYPVLENPPL IVTPSQQPKF GDYQCNSAMG
     ICQMLKTKEQ KVNPREIAEN IVKHLPDNEY IEKVEIAGPG FINIHLRKGF VSQQLTNLLV
     NGVKIPSIGE NKKVIVDFSS PNIAKEMHVG HLRSTIIGES MCRLFEFAGY NVLRLNHVGD
     WGTQFGMLIA HLQDKFPDYL TVSPPIGDLQ AFYKESKKRF DTEEEFKKRA YQCVVLLQSK
     NPDIIKAWKL ICDVSRQEFN KIYEALDISL IERGESFYQD RMHDIVKEFE DRGFVQVDDG
     RKIVFVPGCS VPLTIVKSDG GYTYDTSDLA AIKQRLFEEK ADMIIYVVDN GQSLHFQTVF
     GAAQMIGWYD PAVTRVSHAG FGVVLGEDKK KFKTRSGETV RLIDLLEEGL KRSMDKLKEK
     ERDKVLTTEE LKAAQTSVAY GCIKYADLSH NRLNDYIFSF DKMLDDRGNT AAYLLYAFTR
     IRSIARLANI DEEMLRKAAH ETEIILDHEK EWKLGRCILR FPEVLQKILD DLLLHTLCDY
     IYELATTFTE FYDSCYCVEK DRQSGEVLKV NMWRMLLCEA VAAVMAKGFD ILGIKPVQRM
//