SYRC_RAT
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 03-AUG-2022, entry version 122.
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; P40329; -.
DR PRIDE; P40329; -.
DR Ensembl; ENSRNOT00000010252; ENSRNOP00000010252; ENSRNOG00000007739.
DR GeneID; 287191; -.
DR KEGG; rno:287191; -.
DR UCSC; RGD:1309215; rat.
DR CTD; 5917; -.
DR RGD; 1309215; Rars.
DR eggNOG; KOG4426; Eukaryota.
DR GeneTree; ENSGT00530000063407; -.
DR HOGENOM; CLU_006406_5_1_1; -.
DR InParanoid; P40329; -.
DR OMA; NKPLHLG; -.
DR OrthoDB; 463402at2759; -.
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 tissues.
DR Genevisible; P40329; RN.
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; -; 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 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
