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Database: UniProt/TrEMBL
Entry: B7JHI5_BACC0
LinkDB: B7JHI5_BACC0
Original site: B7JHI5_BACC0 
ID   B7JHI5_BACC0            Unreviewed;       556 AA.
AC   B7JHI5;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   29-OCT-2014, entry version 44.
DE   RecName: Full=Arginine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00123};
DE            EC=6.1.1.19 {ECO:0000256|HAMAP-Rule:MF_00123};
DE   AltName: Full=Arginyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00123};
GN   Name=argS {ECO:0000256|HAMAP-Rule:MF_00123};
GN   Synonyms=argS2 {ECO:0000313|EMBL:ACK91045.1};
GN   OrderedLocusNames=BCAH820_5455 {ECO:0000313|EMBL:ACK91045.1};
OS   Bacillus cereus (strain AH820).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405535 {ECO:0000313|EMBL:ACK91045.1, ECO:0000313|Proteomes:UP000001363};
RN   [1] {ECO:0000313|EMBL:ACK91045.1, ECO:0000313|Proteomes:UP000001363}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AH820 {ECO:0000313|EMBL:ACK91045.1,
RC   ECO:0000313|Proteomes:UP000001363};
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus AH820.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + L-arginine + tRNA(Arg) = AMP +
CC       diphosphate + L-arginyl-tRNA(Arg). {ECO:0000256|HAMAP-
CC       Rule:MF_00123}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00123}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00123}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00123,
CC       ECO:0000256|RuleBase:RU003489}.
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DR   EMBL; CP001283; ACK91045.1; -; Genomic_DNA.
DR   RefSeq; YP_002454375.1; NC_011773.1.
DR   ProteinModelPortal; B7JHI5; -.
DR   STRING; 405535.BCAH820_5455; -.
DR   EnsemblBacteria; ACK91045; ACK91045; BCAH820_5455.
DR   GeneID; 7189808; -.
DR   KEGG; bcu:BCAH820_5455; -.
DR   PATRIC; 18847917; VBIBacCer122868_5437.
DR   eggNOG; COG0018; -.
DR   HOGENOM; HOG000247214; -.
DR   KO; K01887; -.
DR   OMA; LCNVLAK; -.
DR   OrthoDB; EOG6JB13C; -.
DR   BioCyc; BCER405535:GHSL-5470-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; 1.10.730.10; -; 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; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR001278; Arg-tRNA-ligase.
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 {ECO:0000256|HAMAP-Rule:MF_00123,
KW   ECO:0000256|RuleBase:RU003489};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00123,
KW   ECO:0000256|RuleBase:RU003489};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001363};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00123};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00123,
KW   ECO:0000256|RuleBase:RU003489};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00123,
KW   ECO:0000256|RuleBase:RU003489};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00123,
KW   ECO:0000256|RuleBase:RU003489}.
FT   MOTIF       132    142       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00123}.
SQ   SEQUENCE   556 AA;  62472 MW;  907C27F1AAD2F5D2 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 YAFELAAALH SFYNAEKVLN QDNLELSKAR YELMKAVRTT
     LQNALAIVGV SAPEKM
//
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