ID   SYR1_BACHK              Reviewed;         562 AA.
AC   Q6HJF5;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Arginine--tRNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_00123};
DE            EC=6.1.1.19 {ECO:0000255|HAMAP-Rule:MF_00123};
DE   AltName: Full=Arginyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_00123};
DE            Short=ArgRS 1 {ECO:0000255|HAMAP-Rule:MF_00123};
GN   Name=argS1 {ECO:0000255|HAMAP-Rule:MF_00123};
GN   OrderedLocusNames=BT9727_1992;
OS   Bacillus thuringiensis subsp. konkukian (strain 97-27).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=281309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=97-27;
RX   PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA   Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA   Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA   Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA   Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA   Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(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; AE017355; AAT59740.1; -; Genomic_DNA.
DR   RefSeq; WP_000384893.1; NC_005957.1.
DR   RefSeq; YP_036321.1; NC_005957.1.
DR   AlphaFoldDB; Q6HJF5; -.
DR   SMR; Q6HJF5; -.
DR   EnsemblBacteria; AAT59740; AAT59740; BT9727_1992.
DR   KEGG; btk:BT9727_1992; -.
DR   PATRIC; fig|281309.8.peg.2096; -.
DR   HOGENOM; CLU_006406_6_1_9; -.
DR   OMA; NKPLHLG; -.
DR   Proteomes; UP000001301; 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.
FT   CHAIN           1..562
FT                   /note="Arginine--tRNA ligase 1"
FT                   /id="PRO_0000241985"
FT   MOTIF           122..132
FT                   /note="'HIGH' region"
SQ   SEQUENCE   562 AA;  64478 MW;  53A98BB71E98264B CRC64;
     MDYKMHFAES LSNIFTNELT QKQILDLIES PKQDEFGDAA FPCFSLAKQY KKAPAIIAKE
     VAQKLSDPFF TKVEAVGPYV NVFFNRETVS DTVLKTILAE KEEYGHNHFG YEKTVVIDYS
     SPNIAKPFSM GHLRSTMIGN SLKHIAEKCG YEVVGINYIG DWGTQFGKLI TAYKKWGNEA
     VVKEDPIREL FKLYVQFHEE VTDDEELEEE GRAWFKKLEE GDEEAVELWN WFRHESLKEF
     SRIYELLGVE FTNFQGEAFY NNLMEDFIGI LEEHDLLEES EGALVVNLEE EGMPPCLIRK
     SDGATIYATR DLTAALYRQN TFGFDKALYV VGPEQSLHFN QFFTVLKKLG YTWVDGMEHV
     PFGFILKDGK KMSTRKGRII LLEEVLEEAI ELAKQNIEEK NPNLKQKDEV AKQVGAGAVI
     FHDLKNERMH NIEFSLENML KFEGETGPYV QYTHARACSI LRKESVEFET CTFTLKDDHS
     WNIVKLLNKF PKVIEAACNK NEPSVISKYV LDVAQSFNKY YGNVRILDEN AEKDSRLALV
     YAVTVVLKEG LRLLGVEAPE EM