ID   SYR_STRP1               Reviewed;         563 AA.
AC   Q99XL5; Q48W49;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 143.
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=SPy_2151, M5005_Spy1808;
OS   Streptococcus pyogenes serotype M1.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=301447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX   PubMed=11296296; DOI=10.1073/pnas.071559398;
RA   Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA   Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA   Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA   Clifton S.W., Roe B.A., McLaughlin R.E.;
RT   "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX   PubMed=16088826; DOI=10.1086/432514;
RA   Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA   Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA   Musser J.M.;
RT   "Evolutionary origin and emergence of a highly successful clone of serotype
RT   M1 group A Streptococcus involved multiple horizontal gene transfer
RT   events.";
RL   J. Infect. Dis. 192:771-782(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAZ52426.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE004092; AAK34788.1; -; Genomic_DNA.
DR   EMBL; CP000017; AAZ52426.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_270067.1; NC_002737.2.
DR   AlphaFoldDB; Q99XL5; -.
DR   SMR; Q99XL5; -.
DR   STRING; 1314.HKU360_01921; -.
DR   PaxDb; Q99XL5; -.
DR   EnsemblBacteria; AAK34788; AAK34788; SPy_2151.
DR   KEGG; spy:SPy_2151; -.
DR   KEGG; spz:M5005_Spy1808; -.
DR   PATRIC; fig|160490.10.peg.1863; -.
DR   HOGENOM; CLU_006406_6_1_9; -.
DR   OMA; NKPLHLG; -.
DR   Proteomes; UP000000750; Chromosome.
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; 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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..563
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151620"
FT   MOTIF           121..131
FT                   /note="'HIGH' region"
SQ   SEQUENCE   563 AA;  63121 MW;  E0F2CAC28D03B613 CRC64;
     MDTKTLIASE IAKVVPELEQ DAIFNLLETP KNSDMGDLAF PAFSLAKVLR KAPQMIASEL
     AEQIDESQFE KVVAVGPYIN FFLDKAKISS QVLEQVITAG SDYAQQDEGQ GRNVAIDMSS
     PNIAKPFSIG HLRSTVIGDS LAHIFAKMGY KPVKINHLGD WGKQFGMLIV AYKKWGDEAA
     VQAHPIDELL KLYVRINAEA ETDPTVDEEA REWFRKLEDG DKEATELWQW FRDESLLEFN
     RLYDQLHVTF DSYNGEAFYN DKMDEVLDLL EAKNLLVESK GAQVVNLEKY GIEHPALIKK
     SDGATLYITR DLAAALYRKR TYDFAKSVYV VGNEQAAHFK QLKAVLKEMG YDWSDDMTHV
     AFGLVTKGGA KLSTRKGNVI LLEPTVAEAI NRAASQIEAK NPNLADKEAV AHAVGVGAIK
     FYDLKTDRMN GYDFDLEAMV SFEGETGPYV QYAHARIQSI LRKADFTPSA TTTYSLADAE
     SWEIIKLIQD FPRIIKRTSD NFEPSIMAKF AINLAQSFNK YYAHTRILDD NSERDNRLAL
     CYATATVLKE ALRLLGVDAP NEM