ID   SYRM_PONAB              Reviewed;         578 AA.
AC   Q5REH3;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 79.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR857556; CAH89834.1; -; mRNA.
DR   RefSeq; NP_001128754.1; NM_001135282.1.
DR   AlphaFoldDB; Q5REH3; -.
DR   SMR; Q5REH3; -.
DR   STRING; 9601.ENSPPYP00000018841; -.
DR   GeneID; 100189650; -.
DR   KEGG; pon:100189650; -.
DR   CTD; 57038; -.
DR   eggNOG; KOG1195; Eukaryota.
DR   InParanoid; Q5REH3; -.
DR   OrthoDB; 463402at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
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_0000250733"
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;  65533 MW;  17F28D28E8805284 CRC64;
     MACGFRRAIA CQLSRVLNLP PENLITSISA VPISQKEEVA DFQLSVDSLL EKDNDHSRPD
     IQVQAKRLAE KLRCDTVVSE ISTGQRTVNF KINRELLTKT VLQQVIEDGS KYGLKSELFS
     GLPQKKIVVE FSSPNVAKKF HVGHLRSTII GNFIANLKEA LGHQVIRINY LGDWGMQFGL
     LGTGFQLFGY EEKLQSNPLQ HLFEVYVQVN KEAADDKSVA KAAQEFFQRL ELGDVQALSL
     WQKFRDLSIE EYIRVYKRLG VYFDEYSGES FYREKSQEVL KLLESKGLLL RTIKGTAVVD
     LSGNGDPSSI CTVMRSDGTS LYATRDLAAA IDRMDKYNFD TMIYVTDKGQ KKHFQQVFQM
     LKIMGYDWAE RCQHVPFGVV QGMKTRRGDV TFLEDVLNEI QLRMLQNMAS IKTTKELKNP
     QETAERVGLA ALIIQDFKGL LLSDYKFSWD RVFQSRGDTG VFLQYTHARL HSLEETFGCG
     YLNDFNTACL QEPQSVSILQ HLLRFDEVLY KSSQDFQPRH IVSYLLTLSH LAAVAHKTLQ
     IKDSPPEVAG ARLHLFKAVR SVLANGMKLL GITPVCRM