ID   SYRM_BOVIN              Reviewed;         578 AA.
AC   Q0P5H7;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Probable arginine--tRNA ligase, mitochondrial;
DE            EC=6.1.1.19;
DE   AltName: Full=Arginyl-tRNA synthetase;
DE            Short=ArgRS;
DE   Flags: Precursor;
GN   Name=RARS2; Synonyms=RARSL;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; BC120020; AAI20021.1; -; mRNA.
DR   RefSeq; NP_001069346.1; NM_001075878.1.
DR   AlphaFoldDB; Q0P5H7; -.
DR   SMR; Q0P5H7; -.
DR   STRING; 9913.ENSBTAP00000022568; -.
DR   PaxDb; Q0P5H7; -.
DR   PRIDE; Q0P5H7; -.
DR   Ensembl; ENSBTAT00000084438; ENSBTAP00000057024; ENSBTAG00000016967.
DR   GeneID; 525894; -.
DR   KEGG; bta:525894; -.
DR   CTD; 57038; -.
DR   VEuPathDB; HostDB:ENSBTAG00000016967; -.
DR   VGNC; VGNC:33734; RARS2.
DR   eggNOG; KOG1195; Eukaryota.
DR   GeneTree; ENSGT00530000063407; -.
DR   HOGENOM; CLU_006406_6_2_1; -.
DR   InParanoid; Q0P5H7; -.
DR   OMA; YEFKWER; -.
DR   OrthoDB; 463402at2759; -.
DR   TreeFam; TF300888; -.
DR   Proteomes; UP000009136; Chromosome 9.
DR   Bgee; ENSBTAG00000016967; Expressed in oocyte and 110 other tissues.
DR   ExpressionAtlas; Q0P5H7; baseline and differential.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IBA:GO_Central.
DR   GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR   CDD; cd00671; ArgRS_core; 1.
DR   Gene3D; 3.30.1360.70; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR001278; Arg-tRNA-ligase.
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; PF05746; DALR_1; 1.
DR   Pfam; PF00750; tRNA-synt_1d; 1.
DR   PRINTS; PR01038; TRNASYNTHARG.
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; Ligase; Mitochondrion;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..16
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..578
FT                   /note="Probable arginine--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000284070"
FT   MOTIF           133..144
FT                   /note="'HIGH' region"
FT   BINDING         133..135
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   BINDING         144
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   BINDING         322
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   BINDING         326
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   BINDING         350
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   MOD_RES         568
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3U186"
SQ   SEQUENCE   578 AA;  65631 MW;  1CFCBDCA6492CB42 CRC64;
     MACGFRRSIA SQLSRVLDLP PENLIKSISA VPISRKEEVA DFQLSVDSLL ENNNDHSRPD
     IQIQAMRLAE KLKCDTVVSE ISTGQGTVNF KINRELLTKT VLQQVIEDGS KYGLKSELFS
     GLPKKRIVVE FSSPNVAKKF HVGHLRSTII GNFIANLKEA LGHQVTRINY LGDWGMQFGL
     LGTGFQLFGY EEKLQSSPLQ HLFEVYVQVN KEAADDKNVA KSAHEFFQRL ELGDMQALAL
     WQKFRDLSID EYMRIYQRLG VHFDEYSGES FYREKSQEVL KLLDSKGLLQ KTLKGTAVVD
     LSGNGDPSSV CTVMRSDGTS LYATRDLAAA IDRMEKYNFD KMIYVTDKGQ KKHFQQVFQI
     LQIMGYDWAE RCQHVPFGVV QGMKTRRGDV TFLEDVLNEI RLRMLQNMAS IKTTKELENP
     EETAEQVGLA ALIIQDFRGF LLSDYQFSWD RVFQSRGDTG VFLQYTHARL HSLEETFGCG
     YLNDFNTACL QEPQSVSILQ HLLRFDEVLY RSSQDLQPRH IVSYLLTLSH LAAVAHRTLH
     VRNSPPEVAG ARLHLFRAVR SVLANGMKLL GITPVCRM