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Database: UniProt/TrEMBL
Entry: A7GVA6_BACCN
LinkDB: A7GVA6_BACCN
Original site: A7GVA6_BACCN 
ID   A7GVA6_BACCN            Unreviewed;       556 AA.
AC   A7GVA6;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   19-FEB-2014, entry version 51.
DE   RecName: Full=Arginine--tRNA ligase;
DE            EC=6.1.1.19;
DE   AltName: Full=Arginyl-tRNA synthetase;
GN   Name=argS; OrderedLocusNames=Bcer98_3878;
OS   Bacillus cereus subsp. cytotoxis (strain NVH 391-98).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315749;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NVH 391-98;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B.,
RA   Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.H.,
RA   Sanchis V., Nguen-The C., Lereclus D., Richardson P., Wincker P.,
RA   Weissenbach J., Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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; CP000764; ABS24064.1; -; Genomic_DNA.
DR   RefSeq; YP_001377059.1; NC_009674.1.
DR   ProteinModelPortal; A7GVA6; -.
DR   STRING; 315749.Bcer98_3878; -.
DR   EnsemblBacteria; ABS24064; ABS24064; Bcer98_3878.
DR   GeneID; 5347434; -.
DR   KEGG; bcy:Bcer98_3878; -.
DR   PATRIC; 18936497; VBIBacCyt128034_4063.
DR   eggNOG; COG0018; -.
DR   HOGENOM; HOG000247214; -.
DR   KO; K01887; -.
DR   OMA; YNARENG; -.
DR   OrthoDB; EOG6JB13C; -.
DR   ProtClustDB; PRK01611; -.
DR   BioCyc; BCYT315749:GH2A-4012-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:UniProtKB-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; 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; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   MOTIF       132    142       "HIGH" region (By similarity).
SQ   SEQUENCE   556 AA;  62585 MW;  A07E2627672AC4E1 CRC64;
     MNSLEQVKEL IKEEIKAAVL KAELATEEQI PNVILETPKD KTHGDFSTNM AMQLARVAKK
     APRMIAEELI TNFNKEKASI EKIEIAGPGF INFHMDNSYL TDLIPTIVKA GEAYGETNTG
     KGEKIQVEFV SANPTGDLHL GHARGAAVGD TLCNVLAKAG YDVSREYYIN DAGNQIHNLA
     LSVEARYMQA LGLEKEMPED GYHGADIMEI GKRLAEEFGD RYVKADEKES YEFYRQYGLK
     YELAKLQKDL DSFRVKFDVW FSETSLYKNG KIDAALAVLK ERNEIFEEGG ATWFRSTAYG
     DDKDRVLIKK DGSYTYLTPD IAYHRDKLER GFDKLINIWG ADHHGYIPRM KAAIQALGYE
     KETLEVEIIQ MVQLYQNGEK VKMSKRTGKA VTLRELMEEV GVDAMRYFFA MRSGDSHLDF
     DMDLAVSKSN ENPVYYAQYA HARVCSILRQ GEELGLHAGG DVNYKLVASE KEIDLLKKLG
     EFPAAVAEAA QKRLPHRITS YAFELAAALH SFYNAEKVLN QDNLELSKAR YELMKAVRIT
     LQNALALVGV SAPEKM
//
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