ID D3FPS0_BACPE Unreviewed; 556 AA.
AC D3FPS0;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 01-MAY-2013, entry version 26.
DE RecName: Full=Arginine--tRNA ligase;
DE EC=6.1.1.19;
DE AltName: Full=Arginyl-tRNA synthetase;
GN Name=argS; OrderedLocusNames=BpOF4_07110;
OS Bacillus pseudofirmus (strain OF4).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=398511;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OF4;
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).
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP001878; ADC49480.1; -; Genomic_DNA.
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: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; 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
//
