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Database: UniProt/TrEMBL
Entry: D3FPS0_BACPE
LinkDB: D3FPS0_BACPE
Original site: D3FPS0_BACPE 
ID   D3FPS0_BACPE            Unreviewed;       556 AA.
AC   D3FPS0;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   29-OCT-2014, entry version 32.
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   ECO:0000313|EMBL:ADC49480.1};
GN   OrderedLocusNames=BpOF4_07110 {ECO:0000313|EMBL:ADC49480.1};
OS   Bacillus pseudofirmus (strain OF4).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=398511 {ECO:0000313|EMBL:ADC49480.1, ECO:0000313|Proteomes:UP000001544};
RN   [1] {ECO:0000313|EMBL:ADC49480.1, ECO:0000313|Proteomes:UP000001544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OF4 {ECO:0000313|EMBL:ADC49480.1,
RC   ECO:0000313|Proteomes:UP000001544};
RX   PubMed=21951522; DOI=10.1111/j.1462-2920.2011.02591.x;
RA   Janto B., Ahmed A., Ito M., Liu J., Hicks D.B., Pagni S.,
RA   Fackelmayer O.J., Smith T.A., Earl J., Elbourne L.D., Hassan K.,
RA   Paulsen I.T., Kolsto A.B., Tourasse N.J., Ehrlich G.D., Boissy R.,
RA   Ivey D.M., Li G., Xue Y., Ma Y., Hu F.Z., Krulwich T.A.;
RT   "Genome of alkaliphilic Bacillus pseudofirmus OF4 reveals adaptations
RT   that support the ability to grow in an external pH range from 7.5 to
RT   11.4.";
RL   Environ. Microbiol. 13:3289-3309(2011).
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; CP001878; ADC49480.1; -; Genomic_DNA.
DR   RefSeq; WP_012960753.1; NC_013791.2.
DR   RefSeq; YP_003426372.1; NC_013791.2.
DR   ProteinModelPortal; D3FPS0; -.
DR   EnsemblBacteria; ADC49480; ADC49480; BpOF4_07110.
DR   GeneID; 8766405; -.
DR   KEGG; bpf:BpOF4_07110; -.
DR   PATRIC; 31945276; VBIBacPse80461_1378.
DR   HOGENOM; HOG000247214; -.
DR   KO; K01887; -.
DR   BioCyc; BPSE398511:GJI9-3844-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:UP000001544};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001544}.
FT   MOTIF       132    142       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00123}.
SQ   SEQUENCE   556 AA;  62487 MW;  65E029570EF8E6D7 CRC64;
     MNSVEQMKQK LKEEIKAAVI SAGLATEDVL PEVVLEAPKD KAHGDYATNM AMQLARIAKK
     APRQIAEELT SQLDKEKASI QKIDIAGPGF INFFMNKSYL REIVPAVLSA KEAYGETNVG
     NGEKIQVEFV SANPTGSLHL GHARGAAVGD ALCNVLSKAG YDVEREYYIN DAGNQINNLA
     LSLEARYFQA LGQDKEMPEE GYRGQDIVDF GKALAEEHGD KYVNVSESER REFFRQYGLQ
     KELDKIKSDL KEFRVEFDNW FSETSLYESN KVIEVLETLD EKGETYEQDG ATWFRSTTYG
     DDKDRVLIKN DGTYTYLTPD IAYHQDKMQR GFDKLINIWG ADHHGYIPRM RAAIQALGYS
     PEQFEVQIIQ MVSLYQGGEK VKMSKRTGKA VTLRDLMDEV GIDAVRYFFA MRSADSQLDF
     DMDLAVSKSN ENPVFYVQYA HARVCSMLRQ GEELGLDYDE NTDLSAVSTE KEYDLLKAIG
     DFPAIVAEAA EKKMPHRITN YAHDLASALH SFYNAERVID SEDQDKSKAR LALMKATQIT
     IQNALSLVGV SAPEKM
//
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