ID   G0IMA4_BACAM            Unreviewed;       556 AA.
AC   G0IMA4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   03-APR-2013, entry version 13.
DE   RecName: Full=Arginine--tRNA ligase;
DE            EC=6.1.1.19;
DE   AltName: Full=Arginyl-tRNA synthetase;
GN   Name=argS; ORFNames=BAXH7_03869;
OS   Bacillus amyloliquefaciens XH7.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1034836;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=XH7;
RX   PubMed=21914895; DOI=10.1128/JB.05880-11;
RA   Yang H., Liao Y., Wang B., Lin Y., Pan L.;
RT   "Complete Genome Sequence of Bacillus amyloliquefaciens XH7, Which
RT   Exhibits Production of Purine Nucleosides.";
RL   J. Bacteriol. 193:5593-5594(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=XH7;
RA   Yang H.L., Liao Y.L., Lin Y., Pan L.;
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002927; AEK90979.1; -; Genomic_DNA.
DR   RefSeq; YP_005551827.1; NC_017191.1.
DR   ProteinModelPortal; G0IMA4; -.
DR   EnsemblBacteria; AEK90979; AEK90979; BAXH7_03869.
DR   GeneID; 12197518; -.
DR   KEGG; bxh:BAXH7_03869; -.
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;  62566 MW;  0E8619619FD95F7F CRC64;
     MNIAEQMKDV LKEEIKAAVL KAGLAEESQI PSVLLETPKD KTHGDYSTNM AMQLARIAKK
     APRQIAEEIV AAFDKGKASI EKMDIAGPGF INFYMNNGYL TKLIPSVLEA GEHYGETNVG
     QGEKIQVEFV SANPTGDLHL GHARGAAVGD VLCSVLSKAG YDVSREYYIN DAGNQINNLA
     LSVEVRYFEA LGLEKPMPED GYRGEDIIAI GKKLAEDFGD RFVHEEESER QAFFREYGLK
     YELDKLRSDL ENFRVPFDVW YSETSLYENG KIDQALEALR EKGHVYEEDG ATWFRSTTFG
     DDKDRVLIKK DGSYTYLLPD IAYHKDKLDR GFDKLINVWG ADHHGYIPRM KAAIEALGYK
     KGTLEVEIIQ LVHLYKNGEK MKMSKRTGKA VTMRDLIEEV GLDAVRYFFA MRSADTHMDF
     DLDLAVSTSN ENPVYYAQYA HARICSMLRQ GEEQGLKPAA DLDFSHIQSE KEYDLLKTIG
     GFPEAVAEAA EKRIPHRITN YIYDLASALH SFYNAEKVID PENKEKSRAR LALMKATQIT
     LNNALQLIGV SAPEKM
//