ID   G8UA90_BACCE            Unreviewed;       556 AA.
AC   G8UA90;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   03-APR-2013, entry version 11.
DE   RecName: Full=Arginine--tRNA ligase;
DE            EC=6.1.1.19;
DE   AltName: Full=Arginyl-tRNA synthetase;
GN   Name=argS; ORFNames=bcf_26925;
OS   Bacillus cereus F837/76.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=347495;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=F837/76;
RX   PubMed=22374959; DOI=10.1128/JB.06719-11;
RA   Auger S., Galleron N., Segurens B., Dossat C., Bolotin A., Wincker P.,
RA   Sorokin A.;
RT   "Complete Genome Sequence of the Highly Hemolytic Strain Bacillus
RT   cereus F837/76.";
RL   J. Bacteriol. 194:1630-1630(2012).
CC   -!- CATALYTIC ACTIVITY: ATP + L-arginine + tRNA(Arg) = AMP +
CC       diphosphate + L-arginyl-tRNA(Arg).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP003187; AEW58478.1; -; Genomic_DNA.
DR   RefSeq; YP_005121991.1; NC_016779.1.
DR   ProteinModelPortal; G8UA90; -.
DR   EnsemblBacteria; AEW58478; AEW58478; bcf_26925.
DR   GeneID; 11681084; -.
DR   KEGG; bcf:bcf_26925; -.
DR   KO; K01887; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:HAMAP.
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_Ia.
DR   InterPro; IPR015945; Arg-tRNA-synth_Ia_core.
DR   InterPro; IPR005148; Arg-tRNA-synth_N.
DR   InterPro; IPR008909; DALR_anticod-bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_1a_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; SSF55190; Arg-tRNA-synth_Ic_N; 1.
DR   SUPFAM; SSF47323; tRNAsyn_1a_bind; 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.
FT   MOTIF       132    142       "HIGH" region (By similarity).
SQ   SEQUENCE   556 AA;  62502 MW;  8ACC27EB1AD2F5D2 CRC64;
     MNSLEQVKGL IKEEIQAAVL KAELATEEQI PNVVLESPKD KTNGDFSTNM AMQLARVAKK
     APRMIAEELV ANFDKAKASI EKIEIAGPGF INFYMDNSYL TDLIPTIVNA GEAYGETNTG
     KGEKVQVEFV SANPTGDLHL GHARGAAVGD TLCNLLAKAG YDVSREYYIN DAGNQIHNLA
     LSVEARYMQA LGLEKEMPED GYHGADIIGI GKRLAEEFGD RYAKADEKES YEFYREYGLK
     YELAKLQKDL ESFRVKFDVW FSETSLYKNG KIDQALAVLK ERDEIFEEDG ATWFRSMTYG
     DDKNRVLIKN DGSYTYLTPD IAYHRDKLER GFDKLINIWG ADHHGYIPRM KAAIQALGYD
     KETLEVEIIQ MVQLYQNGEK MKMSKRTGKA VTLRELMEEV GVDAMRYFFA MRSGDSHLDF
     DMDLAVSKSN ENPVYYAQYA HARVCSILRQ GEELGLATGG DVNYKLVTSE KEVELLKKLG
     EFPAVVADAA QKRLPHRITN YAFELAATLH SFYNAEKVLN QDNLELSKAR YELMKAVRTT
     LQNALAIVGV SAPEKM
//