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   27-MAR-2024, entry version 106.
DE   RecName: Full=Probable arginine--tRNA ligase, mitochondrial;
DE            EC=6.1.1.19 {ECO:0000250|UniProtKB:Q5T160};
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   -!- FUNCTION: Catalyzes the attachment of arginine to tRNA(Arg) in a two-
CC       step reaction: arginine is first activated by ATP to form Arg-AMP and
CC       then transferred to the acceptor end of tRNA(Arg).
CC       {ECO:0000250|UniProtKB:Q5T160}.
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:Q5T160};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC       {ECO:0000250|UniProtKB:Q5T160}.
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.ENSBTAP00000058548; -.
DR   PaxDb; 9913-ENSBTAP00000022568; -.
DR   Ensembl; ENSBTAT00000084438.1; ENSBTAP00000057024.1; ENSBTAG00000016967.6.
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   TreeFam; TF300888; -.
DR   Proteomes; UP000009136; Chromosome 9.
DR   Bgee; ENSBTAG00000016967; Expressed in oocyte and 110 other cell types or tissues.
DR   ExpressionAtlas; Q0P5H7; baseline and differential.
DR   GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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; 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; Arginyl tRNA synthetase N-terminal domain; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   NCBIfam; TIGR00456; argS; 1.
DR   PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR   PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 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; 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; Ligase; Membrane;
KW   Mitochondrion; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome; 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
//