ID D5DWK2_BACMQ Unreviewed; 556 AA.
AC D5DWK2;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 01-MAY-2013, entry version 22.
DE RecName: Full=Arginine--tRNA ligase;
DE EC=6.1.1.19;
DE AltName: Full=Arginyl-tRNA synthetase;
GN Name=argS; OrderedLocusNames=BMQ_5189;
OS Bacillus megaterium (strain ATCC 12872 / QMB1551).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=545693;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12872 / QMB1551;
RA Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K.,
RA Riley D.R., Creasy H.H., Koenig S.S.K., Galens K., Orvis J.,
RA Creasy T., Biedendieck R., Braun C., Grayburn S., Jahn D., Ravel J.,
RA Vary P.S.;
RT "Genome sequences of the industrial vitamin B12-producers B.
RT megaterium QM B1551 and DSM319 reveal new insights into the Bacillus
RT genome evolution and pan-genome structure.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
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; CP001983; ADE72167.1; -; Genomic_DNA.
DR RefSeq; YP_003565601.1; NC_014019.1.
DR ProteinModelPortal; D5DWK2; -.
DR EnsemblBacteria; ADE72167; ADE72167; BMQ_5189.
DR GeneID; 8989627; -.
DR KEGG; bmq:BMQ_5189; -.
DR PATRIC; 35487170; VBIBacMeg35839_5215.
DR HOGENOM; HOG000247214; -.
DR KO; K01887; -.
DR BioCyc; BMEG545693:GHSY-5570-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; 62438 MW; 495AFFF0BA467AE4 CRC64;
MNIVEQVQQK LKAEIQDAVV KAGLAEKAEL PEVLLETPKD KTHGDYSTNM AMQLARIAKK
APRVIAEELV ANFDKSQASI EKIDIAGPGF INFYMNNSYL AELIPTIVKA GEAYGQTNVG
NGQKVQVEFV SANPTGDLHL GHARGAAVGD SLCNVLEKAG YDVSREYYIN DAGNQINNLA
YSVEARYMQA LGLEKEMPAD GYHGADIINI GKELAKEHGD KYANASEEER FEFFRQYGLD
YELAKLKRDL EQFRVKFDVW YSETSLYKND KISIALETLK KQGHVYEEEG ATWFRSTTFG
DDKDRVLIKN DGSFTYLTPD IAYHQDKIQR GFDKLINIWG ADHHGYIPRM KAAIQALGYE
KDTLEVEIIQ MVQLYQNGEK MKMSKRTGKA VTMRDLVEEV GLDATRYFFA MRSADTHLDF
DLDLAVSQSN ENPVYYAQYA HARICSILRQ GEEMGIQSTS GADLSLISAE KEMELLKKIG
EFPQAVAEAA TKRIPHRITN YVFDLASTFH SFYNAEKVLD SDNVETSKAR IELVKAVQVT
LQNSLKLIGV SAPEKM
//
