ID   G7VX06_PAETH            Unreviewed;       559 AA.
AC   G7VX06;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   03-APR-2013, entry version 10.
DE   RecName: Full=Arginine--tRNA ligase;
DE            EC=6.1.1.19;
DE   AltName: Full=Arginyl-tRNA synthetase;
GN   Name=argS; OrderedLocusNames=HPL003_08105;
OS   Paenibacillus terrae (strain HPL-003).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=985665;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPL-003;
RA   Shin S.H., Kim S., Kim J.Y.;
RT   "Complete sequence of Paenibacillus terrae HPL-003.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HPL-003;
RA   Shin S.H., Kim S., Kim J.Y.;
RL   Submitted (NOV-2011) 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; CP003107; AET58384.1; -; Genomic_DNA.
DR   RefSeq; YP_005074607.1; NC_016641.1.
DR   EnsemblBacteria; AET58384; AET58384; HPL003_08105.
DR   GeneID; 11588055; -.
DR   KEGG; pta:HPL003_08105; -.
DR   KO; K01887; -.
DR   OMA; NGEKVKM; -.
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       134    144       "HIGH" region (By similarity).
SQ   SEQUENCE   559 AA;  62570 MW;  9355A4588CEA99A7 CRC64;
     MTSNPLELIN QKVISAIEAA VLAAGIVSRE ELPTITLEVP KDKSHGDLAT NAAMQLTRIA
     KKNPRQIAED LIANMDLAAA SIESAEIAGP GFINFRLNKS YLYDVIKQVQ EQGADYGRVQ
     EGAGKKVQIE FVSANPTGSL HLGHARGAAV GDALCNVLDY AGYKVTREYY INDAGNQIYN
     MSRSIEARYL QELGQPAEMP EDGYHGEDII GFAKELVAEK SDSLLSLTPG DRAAYFRDYG
     LEKELNKIKR DLELFRVPFD SWFSETSLYE NGEVLKALNE LRDREEIYEK DGATWLNTTK
     YGDDKDRVLI KNDGTYTYLT PDIAYHRDKY ARGYDTIINI WGADHHGYIP RMKAAMEALG
     NDPDKLKVLI AQMVSLFQNG EKVKMSKRTG KAVTMEDLME EVGVDAIRYF FTMRSMDSHL
     DFDMDLAIST SNENPVFYVQ YAHARACSVY RQAEEQGIAV LPLAEVDLSK LTAEHEYDLL
     RKIGELPEEV SVAAANFAPH RMIRYVYELA SLFHSYYKAE RVITEDAAQT QARLALFGAV
     RTTIANVLKL VGVSAPERM
//