ID   SYR_XANOM               Reviewed;         562 AA.
AC   Q2P8B1;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Arginine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00123};
DE            EC=6.1.1.19 {ECO:0000255|HAMAP-Rule:MF_00123};
DE   AltName: Full=Arginyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00123};
DE            Short=ArgRS {ECO:0000255|HAMAP-Rule:MF_00123};
GN   Name=argS {ECO:0000255|HAMAP-Rule:MF_00123}; OrderedLocusNames=XOO0461;
OS   Xanthomonas oryzae pv. oryzae (strain MAFF 311018).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=342109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 311018;
RA   Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
RT   "Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of
RT   large numbers of effector genes and insertion sequences to its race
RT   diversity.";
RL   Jpn. Agric. Res. Q. 39:275-287(2005).
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:0000255|HAMAP-Rule:MF_00123};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00123}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00123}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00123}.
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DR   EMBL; AP008229; BAE67216.1; -; Genomic_DNA.
DR   RefSeq; WP_011407446.1; NC_007705.1.
DR   AlphaFoldDB; Q2P8B1; -.
DR   SMR; Q2P8B1; -.
DR   KEGG; xom:XOO0461; -.
DR   HOGENOM; CLU_006406_0_1_6; -.
DR   OMA; NKPLHLG; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..562
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000242126"
FT   MOTIF           129..139
FT                   /note="'HIGH' region"
SQ   SEQUENCE   562 AA;  62016 MW;  C41CE9B3546FCE81 CRC64;
     MKALLRALIG QGIEALRANG TLPGDTLPPD FVVERPKTRE HGDFATNAAM LLAKAARSNP
     RALAQALLTA LPDSNDVTKV EIAGPGFINF HLAPTAYQRE VAHVIKQGHD YGRGLAGNGR
     SVGVEYVSAN PTGPLHVGHG RAAAIGDSLA RVLDANGWNV KREFYYNDAG VQIENLALSV
     QARAQGLTPD SAGWPENGYR GDYIADVANA YLAGDTVDME GHLVTGTKDP ADLESIRRFA
     VAYLRNEQNH DLAAFRVDFD IYFLESSLYK DGKVEEAVQK LIASGHTYEE GGALWLKSTD
     FGDDKDRVMR KSDGTYTYFV PDVAYHLTKW QRGYERAITE LGADHHGSLT RVRAGLQAME
     LGIPQGWPEY VLHQMVTVMR DGEEVKLGKR AGGYVTLRDL IEETSADAVR WFLIARKPDS
     QLTFDIDLAR AQSNDNPVFY VQYAHARVCS VLRQAQEKGY KYDQVHGLAE LARLDDEHSL
     AVMLELSRYP EVVEIAGQTL EPYQIAQYLR ELAHAFHTWY HNSKVLVDDA AERDAKLTLA
     VATQQVLANG LELLGVSAPE KM