ID   SYR_STRT1               Reviewed;         563 AA.
AC   Q5M1Z3;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 102.
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=str0047;
OS   Streptococcus thermophilus (strain CNRZ 1066).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=299768;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNRZ 1066;
RX   PubMed=15543133; DOI=10.1038/nbt1034;
RA   Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA   Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA   Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA   Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT   "Complete sequence and comparative genome analysis of the dairy bacterium
RT   Streptococcus thermophilus.";
RL   Nat. Biotechnol. 22:1554-1558(2004).
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; CP000024; AAV61664.1; -; Genomic_DNA.
DR   RefSeq; WP_011226739.1; NC_006449.1.
DR   AlphaFoldDB; Q5M1Z3; -.
DR   SMR; Q5M1Z3; -.
DR   KEGG; stc:str0047; -.
DR   HOGENOM; CLU_006406_6_1_9; -.
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; cd07956; Anticodon_Ia_Arg; 1.
DR   CDD; cd00671; ArgRS_core; 1.
DR   Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   NCBIfam; TIGR00456; argS; 1.
DR   PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR   PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF55190; Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..563
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000242102"
FT   MOTIF           121..131
FT                   /note="'HIGH' region"
SQ   SEQUENCE   563 AA;  62893 MW;  83CAFCAD12D2E2B3 CRC64;
     MNTKELIAAE IAKVVPELEQ ENIQNLLEIP KNADMGDLAF PAFSLAKVLR KAPQMIAADI
     AEKIDASNFE KVEAVGPYIN IFLDKSKISA DVLGQVIAQG SHYADQNIGN GRNIAFDMSS
     PNIAKPFSIG HLRSTVIADA LANIVAKQGY KPVRINHLGD WGKQFGMLIV AYKKWGSEEA
     VKANPINELL QLYVRINAEA EEDPSVDEEA REWFRKLEAG DEEATALWQW FRDESLVEFN
     RLYDELGVSF DSYNGEAFYN DKMDEVVDIL TEKGLLQESQ GAQVVNLEKY GIEHPALIKK
     SDGATLYITR DLAAALYRKR TYDFAKAIYV VGNEQSAHFK QLKAVLKEMG YNWSDDMTHV
     AFGLVTKNGK KLSTRKGNVI LLEPTIAEAV NRAQAQIEAK NPNLPNKEAI AHAVGVGAIK
     FYDLKTDRMN GYDFDLDAMV SFEGETGPYV QYAHARIQSI LRKADFTPSA DATYSLNDVE
     SWEIIKLLQD FPRIINRASD NFEPSIVAKF AISLAQAFNK YYAHTRILDE SPERDSRLAL
     CYATATVLKE ALRLLGVEAP DEM
//