ID   SYR_STAA8               Reviewed;         553 AA.
AC   Q2G0F8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 96.
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};
GN   OrderedLocusNames=SAOUHSC_00611;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
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; CP000253; ABD29749.1; -; Genomic_DNA.
DR   RefSeq; WP_001021145.1; NZ_LS483365.1.
DR   RefSeq; YP_499174.1; NC_007795.1.
DR   AlphaFoldDB; Q2G0F8; -.
DR   SMR; Q2G0F8; -.
DR   STRING; 1280.SAXN108_0673; -.
DR   EnsemblBacteria; ABD29749; ABD29749; SAOUHSC_00611.
DR   GeneID; 3918930; -.
DR   KEGG; sao:SAOUHSC_00611; -.
DR   PATRIC; fig|93061.5.peg.547; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_0_1_9; -.
DR   OMA; YEFKWER; -.
DR   PRO; PR:Q2G0F8; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..553
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000018126"
FT   MOTIF           130..140
FT                   /note="'HIGH' region"
SQ   SEQUENCE   553 AA;  62381 MW;  9B10AAB5C212E30C CRC64;
     MNIIDQVKQT LVEEIAASIN KAGLADEIPD IKIEVPKDTK NGDYATNIAM VLTKIAKRNP
     REIAQAIVDN LDTEKAHVKQ IDIAGPGFIN FYLDNQYLTA IIPEAIEKGD QFGHVNESKG
     QNVLLEYVSA NPTGDLHIGH ARNAAVGDAL ANILTAAGYN VTREYYINDA GNQITNLARS
     IETRFFEALG DNSYSMPEDG YNGKDIIEIG KDLAEKHPEI KDYSEEARLK EFRKLGVEYE
     MAKLKNDLAE FNTHFDNWFS ETSLYEKGEI LEVLAKMKEL GYTYEADGAT WLRTTDFKDD
     KDRVLIKNDG TYTYFLPDIA YHFDKVKRGN DILIDLFGAD HHGYINRLKA SLETFGVDSN
     RLEIQIMQMV RLMENGKEVK MSKRTGNAIT LREIMDEVGV DAARYFLTMR SPDSHFDFDM
     ELAKEQSQDN PVYYAQYAHA RICSILKQAK EQGIEVTAAN DFTTITNEKA IELLKKVADF
     EPTIESAAEH RSAHRITNYI QDLASHFHKF YNAEKVLTDD IEKTKAHVAM IEAVRITLKN
     ALAMVGVSAP ESM