ID   SYRM_XENLA              Reviewed;         580 AA.
AC   Q6GQJ7;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
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   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-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; BC072745; AAH72745.1; -; mRNA.
DR   RefSeq; NP_001085437.1; NM_001091968.1.
DR   AlphaFoldDB; Q6GQJ7; -.
DR   SMR; Q6GQJ7; -.
DR   IntAct; Q6GQJ7; 2.
DR   PRIDE; Q6GQJ7; -.
DR   DNASU; 443863; -.
DR   GeneID; 443863; -.
DR   KEGG; xla:443863; -.
DR   CTD; 443863; -.
DR   Xenbase; XB-GENE-976893; rars2.S.
DR   OrthoDB; 463402at2759; -.
DR   Proteomes; UP000186698; Chromosome 5S.
DR   Bgee; 443863; Expressed in egg cell and 19 other tissues.
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   TIGRFAMs; TIGR00456; argS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   2: Evidence at transcript level;
KW   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..580
FT                   /note="Probable arginine--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000250734"
FT   MOTIF           136..147
FT                   /note="'HIGH' region"
FT   BINDING         136..138
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   BINDING         147
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   BINDING         324
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   BINDING         328
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   BINDING         352
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
SQ   SEQUENCE   580 AA;  65426 MW;  5927ED86B0DA6F64 CRC64;
     MAWHFRRVIA EQVSRVLGLP SESCSRVAQC IQTVPVHRKH ESPDFQLFMT SLSEGGPNGT
     FSNQEERAEQ LAGKLVCDSV ISDIGTTRGS VTFKINRDLL TRNVLQQISK DGSLYGLNTE
     LFSELSRRKT IVEYSSPNIA KKFHVGHLRS TIIGNFIANL KQAVGNEVVR INYLGDWGLQ
     FGLLGAGFSS FGSKEKLLAN PLQHLFEVYV KVNTAAEKDN GIKLSAQEFL RRLEGGDPHA
     LSLWMHFRDI SIQEYAKIYK RLGAHFDDYS GESFYKEKSQ EVLKQLESKG LLLKTDKGTV
     IDLSEEGNLS SYSTVMRSDG TSLYITRDMA AAVDRMERYN FDEMIYVTDK SQKNHFQQLF
     KILKIMGKDQ ADRCQHVPFG LVQGMKTRRG EVVFLEDVLD EARSRMLQNM AASETSKQLD
     DPSDTAEKIG IAALIVQDFK GQLVSDYHFD WDQALQSTGD TGVFLQYTHA RLHSLQALRC
     PRDTEDFEIA SLREPCVIAT LQHLLRYDEV IYKCLEDLQP RYLVTYLLSL GHLANVAHRT
     LQVKGSSSEA AHARLLFFKN VQMVLGNGMK LLGITPVNNM