ID   SYR_CLOD6               Reviewed;         566 AA.
AC   Q189Q7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=CD630_07110;
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(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; AM180355; CAJ67544.1; -; Genomic_DNA.
DR   RefSeq; WP_003436885.1; NZ_CP010905.2.
DR   RefSeq; YP_001087187.1; NC_009089.1.
DR   AlphaFoldDB; Q189Q7; -.
DR   SMR; Q189Q7; -.
DR   STRING; 272563.CD630_07110; -.
DR   EnsemblBacteria; CAJ67544; CAJ67544; CD630_07110.
DR   GeneID; 66353213; -.
DR   KEGG; cdf:CD630_07110; -.
DR   KEGG; pdc:CDIF630_00826; -.
DR   PATRIC; fig|272563.120.peg.731; -.
DR   eggNOG; COG0018; Bacteria.
DR   OMA; NKPLHLG; -.
DR   PhylomeDB; Q189Q7; -.
DR   BioCyc; PDIF272563:G12WB-821-MON; -.
DR   Proteomes; UP000001978; 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; 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..566
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000198887"
FT   MOTIF           123..133
FT                   /note="'HIGH' region"
SQ   SEQUENCE   566 AA;  64990 MW;  767922C7C06F0B64 CRC64;
     MQDFKVAISN CLKEKIEDLS KEEIEALIEV PPNKDMGDYA FPCFKLAKVF RKAPNMIASE
     LAESIEPSGE ITKVIQLGGY VNFFVNKSQL AETVIKKVLD EKENYGHSDF GKDKTVIVEY
     SSPNIAKPFH IGHIRTTVIG NALYKIYDSQ GYKTIRINHL GDYGTQFGKL IVAFKKWGEK
     EVVESNPIPE LLKLYVRFHD EAEQHPEMED EARAWFNKLE NGDEEAQELW QWFRNESLKE
     FNRVYKLLDI EFDSLAGESF YSDKMNRVIE LLEEKNLLKE SKGARIVDLE EYKMPPALIT
     KNDGSTLYMT RDLAAAIYRK ETYDFDKCIY VVGSQQNLHF QQWFKVIELM GYDWAKDLIH
     VGFGMVALEE GTMSTRKGRV VFLEDALNQA IDKTKEIILA KNPNAKNVDE ISKQVGVGAV
     VFQELSNSRI KDYTFSWERT LSFDGETGPY VQYTHARCCA VLRKAEVEVT SDIDYSLLAD
     EDSAEVLRVI ESFNKNILLA LKKNEPHIVT RFMLDLAQAF NKFYHDNPIL VENLEIRKAR
     LALVLATKQT LENSLKLLGM HAPERM