ID A7GVA6_BACCN Unreviewed; 556 AA.
AC A7GVA6;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 29-MAY-2013, entry version 47.
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; NGEKVKM; -.
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: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; 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
//
