ID   SYR1_BACCZ              Reviewed;         562 AA.
AC   Q63C01;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
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}; OrderedLocusNames=BCE33L1974;
OS   Bacillus cereus (strain ZK / E33L).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=288681;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZK / E33L;
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}.
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; CP000001; AAU18282.1; -; Genomic_DNA.
DR   RefSeq; WP_000385003.1; NZ_CP009968.1.
DR   AlphaFoldDB; Q63C01; -.
DR   SMR; Q63C01; -.
DR   EnsemblBacteria; AAU18282; AAU18282; BCE33L1974.
DR   KEGG; bcz:BCE33L1974; -.
DR   PATRIC; fig|288681.22.peg.3550; -.
DR   OMA; NKPLHLG; -.
DR   Proteomes; UP000002612; 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_0000241981"
FT   MOTIF           122..132
FT                   /note="'HIGH' region"
SQ   SEQUENCE   562 AA;  64425 MW;  35EBD962DE643E09 CRC64;
     MDYKTQFAES LSNIFTNELT QKQILDLIET PKQDEFGDAA FPCFSLAKQY KKSPAIIAKE
     VAEKLSDPFF TKVEAVGPYV NVFFNRDTVS DAVLKTILAE KEEYGQNHFG CEKTVVIDYS
     SPNIAKPFSM GHLRSTMIGN SLKHIAEKCG YEVVGINYIG DWGTQFGKLI TAYKKWGNEA
     VVKEDPIREL FKLYVQFHEE IKDDEELEEE GRAWFKKLEE GDEEAVELWN WFRHESLKEF
     SRIYELLGVE FTNFQGEAFY NNLMEDFIGI LEEHDLLEES EGALVVNLEE EGMPPCLIRK
     SDGATIYATR DLTAALYRQN TFGFDKALYV VGPEQSLHFN QFFTVLKKLG YTWVDGMEHV
     PFGFILKDGK KMSTRKGRVI LLEEVLEEAI ELAKQNIEEK NPNLKQKEEV AKQVGAGAVI
     FHDLKNERMH NIEFSLENML KFEGETGPYV QYTHARACSI LRKESVEFET CTFTLKDDYS
     WNIVKLLNKF PEVIEAACNK NEPSVISKYV LDVAQSFNKY YGNVRILDEN AEKDSRLALV
     YAVTVVLKEG LRLLGVEAPE EM