SYRC_BOVIN
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 03-AUG-2022, entry version 95.
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; A7YW98; -.
DR PeptideAtlas; A7YW98; -.
DR PRIDE; A7YW98; -.
DR Ensembl; ENSBTAT00000019475; ENSBTAP00000019475; ENSBTAG00000014626.
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; NKPLHLG; -.
DR OrthoDB; 463402at2759; -.
DR TreeFam; TF106111; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000014626; Expressed in oocyte and 105 other tissues.
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; 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
