ID   SYR_STRMU               Reviewed;         563 AA.
AC   Q8DRW2;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 111.
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=SMU_2098;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AE014133; AAN59692.1; -; Genomic_DNA.
DR   RefSeq; NP_722386.1; NC_004350.2.
DR   RefSeq; WP_002262405.1; NC_004350.2.
DR   AlphaFoldDB; Q8DRW2; -.
DR   SMR; Q8DRW2; -.
DR   STRING; 210007.SMU_2098; -.
DR   PRIDE; Q8DRW2; -.
DR   EnsemblBacteria; AAN59692; AAN59692; SMU_2098.
DR   KEGG; smu:SMU_2098; -.
DR   PATRIC; fig|210007.7.peg.1868; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_6_2_9; -.
DR   OMA; NKPLHLG; -.
DR   PhylomeDB; Q8DRW2; -.
DR   Proteomes; UP000002512; 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_0000151617"
FT   MOTIF           121..131
FT                   /note="'HIGH' region"
SQ   SEQUENCE   563 AA;  63573 MW;  312C7691C9B3B385 CRC64;
     MNHNRLIAKE IAAIVPALEQ ETILNLLEKP KKSSMGDLAF PTFSLAKTMR KAPQIIASEL
     VGQINNSYFE KVEAVGPYIN FFLNKSEISA QVLKEVIKKR EDYAQAAIGQ GHNIVIDLSS
     PNIAKPFSIG HLRSTVIGDA LSNIFQKLGY ETVKINHLGD WGKQFGMLIV AYKKWGSEEA
     VRAHPIDELL KIYVRINAET KNHPELDEEA REWFRKLENN DEEALALWQW FRDESLMEFN
     RLYAELGIDF DSYNGEAFYN DKMEEVVQLL AEKGLLEESK GAQVVNLEKY GIEHPALIKK
     SDGATLYITR DLAAAIYRKR TYDFAKAIYV VGQEQTAHFK QLKAVLAEMG YAWSKDIQHV
     SFGLVTKNGQ KLSTRKGNVI LLEPTIAEAV KRSLAQIDTK NPDLVNKEAV AHAVGVGAIK
     FYDLKTDRTN GYDFDLEAMV SFEGETGPYV QYAHARIQSI LRKADFQPQA TENYQLNDTE
     SWEIIKLIQD FPNTIVRAAD NFEPSLIARF AIHLAQSFNK YYAHTRILDN SPERDSRLAL
     SYATATVLKE ALALLGVEAP NEM