ID   SYR_SALTS               Reviewed;         577 AA.
AC   E1WGF0; P74871;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Arginine--tRNA ligase;
DE            EC=6.1.1.19;
DE   AltName: Full=Arginyl-tRNA synthetase;
DE            Short=ArgRS;
GN   Name=argS; OrderedLocusNames=SL1344_1844;
OS   Salmonella typhimurium (strain SL1344).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=216597;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL1344;
RX   PubMed=22538806; DOI=10.1073/pnas.1201061109;
RA   Kroger C., Dillon S.C., Cameron A.D., Papenfort K., Sivasankaran S.K.,
RA   Hokamp K., Chao Y., Sittka A., Hebrard M., Handler K., Colgan A.,
RA   Leekitcharoenphon P., Langridge G.C., Lohan A.J., Loftus B., Lucchini S.,
RA   Ussery D.W., Dorman C.J., Thomson N.R., Vogel J., Hinton J.C.;
RT   "The transcriptional landscape and small RNAs of Salmonella enterica
RT   serovar Typhimurium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:E1277-E1286(2012).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 491-577.
RC   STRAIN=SL1344;
RX   PubMed=8930920; DOI=10.1046/j.1365-2958.1996.00120.x;
RA   Valdivia R.H., Falkow S.;
RT   "Bacterial genetics by flow cytometry: rapid isolation of Salmonella
RT   typhimurium acid-inducible promoters by differential fluorescence
RT   induction.";
RL   Mol. Microbiol. 22:367-378(1996).
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;
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FQ312003; CBW17938.1; -; Genomic_DNA.
DR   EMBL; U62714; AAC44610.1; -; Genomic_DNA.
DR   RefSeq; WP_001025361.1; NZ_QASL01000015.1.
DR   AlphaFoldDB; E1WGF0; -.
DR   SMR; E1WGF0; -.
DR   KEGG; sey:SL1344_1844; -.
DR   PATRIC; fig|216597.6.peg.2047; -.
DR   HOGENOM; CLU_006406_5_1_6; -.
DR   BioCyc; SENT216597:SL1344_RS09550-MONOMER; -.
DR   Proteomes; UP000008962; 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; 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; 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   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.
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..577
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000406087"
FT   MOTIF           122..132
FT                   /note="'HIGH' region"
FT   CONFLICT        491
FT                   /note="D -> H (in Ref. 2; AAC44610)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        498
FT                   /note="A -> D (in Ref. 2; AAC44610)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        555
FT                   /note="A -> V (in Ref. 2; AAC44610)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        569
FT                   /note="L -> S (in Ref. 2; AAC44610)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        574
FT                   /note="V -> A (in Ref. 2; AAC44610)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   577 AA;  64275 MW;  842D46DD38EB44B7 CRC64;
     MNIQALLSEK VSQAMIAAGA PADCEPQVRQ SAKVQFGDYQ ANGMMAVAKK LGMAPRQLAE
     QVLTHLDLSG IASKVEIAGP GFINIFLEPA FLAEQVQQAL ASDRLGVSQP TRQTIVVDYS
     APNVAKEMHV GHLRSTIIGD AAVRTLEFLG HHVIRANHVG DWGTQFGMLI AWLEKQQQEN
     AGDMALADLE GFYRDAKKHY DEDEAFAERA RNYVVKLQSG DTYFREMWRK LVDITMTQNQ
     ITYDRLNVTL TRDDVMGESL YNPMLPGIVA DLKAKGLAVE SEGATVVFLD EFKNKEGDPM
     GVIIQKKDGG YLYTTTDIAC AKYRYETLHA DRVLYYIDSR QHQHLMQAWT IVRKAGYVPD
     SVPLEHHMFG MMLGKDGKPF KTRAGGTVKL ADLLDEALER ARRLVAEKNP DMPADELEKL
     ANAVGIGAVK YADLSKNRTT DYIFDWDNML AFEGNTAPYM QYAYTRVLSV FRKANIDEQA
     LASAPVIISE DREAQLAARL LQFEETLTVV AREGTPHVMC AYLYDVAGLF SGFYEHCPIL
     SAENDAVRNS RLKLAQLTAK TLKLGLDTLG IETVERM
//