ID   G2PB69_STRVO            Unreviewed;       620 AA.
AC   G2PB69;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   03-APR-2013, entry version 14.
DE   RecName: Full=Aspartate--tRNA ligase;
DE            EC=6.1.1.12;
DE   AltName: Full=Aspartyl-tRNA synthetase;
GN   Name=aspS; ORFNames=Strvi_0333;
OS   Streptomyces violaceusniger Tu 4113.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptomycineae; Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=653045;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tu 4113;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ivanova N., Daligault H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Hagen A.,
RA   Katz L., Fiedler H.-P., Keasling J., Fortman J., Woyke T.;
RT   "Complete sequence of chromosome of Streptomyces violaceusniger Tu
RT   4113.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + L-aspartate + tRNA(Asp) = AMP +
CC       diphosphate + L-aspartyl-tRNA(Asp).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP002994; AEM80121.1; -; Genomic_DNA.
DR   RefSeq; YP_004810401.1; NC_015957.1.
DR   EnsemblBacteria; AEM80121; AEM80121; Strvi_0333.
DR   GeneID; 11088831; -.
DR   KEGG; svl:Strvi_0333; -.
DR   KO; K01876; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:HAMAP.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.1360.30; -; 1.
DR   HAMAP; MF_00044_B; Asp_tRNA_synth_B; 1; -.
DR   InterPro; IPR004364; aa-tRNA-synt_II.
DR   InterPro; IPR018150; aa-tRNA-synt_II-like.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR004524; Asp-tRNA-ligase_IIb_bac/mt.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   InterPro; IPR004115; GAD_dom.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA-helicase.
DR   PANTHER; PTHR22594; PTHR22594; 1.
DR   PANTHER; PTHR22594:SF5; PTHR22594:SF5; 1.
DR   Pfam; PF02938; GAD; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   SUPFAM; SSF50249; Nucleic_acid_OB; 1.
DR   SUPFAM; SSF55261; SSF55261; 1.
DR   TIGRFAMs; TIGR00459; aspS_bact; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
SQ   SEQUENCE   620 AA;  69261 MW;  00A8975FC68B2B6A CRC64;
     MHRYRSHTCG QLRAADVDTD VRLSGWLHNR RNLGGILFID LRDHYGLVQL VVRPDTAANE
     ALSSISKETV VRIDGRVIAR GADNVNPELP TGEIEVEVAD VEVLGAADPL PFTVFPEDGV
     GEERRLEYRF LDLRRERMHR NIMLRSAVIS AIRQKMTAQG FNELATPILS ATSPEGARDF
     LVPSRLHAGK FYALPQAPQQ FKQLLMIAGF DRYFQIAPCF RDEDARADRS PGEFYQLDVE
     MSFVEQEDVF GVIEKVMTEL FEEFGGGRHV TSPFPRIPFR EAMLKYGSDK PDLRAQLELR
     DVSHIFEGSG FKAFADKHVR ALAVPDTADQ PRKFFDQLGE FASLQGAKGL AWVRIGEDAK
     LTGPIAKFLN HEDVEKLITE VQGKPGTSIF FGAGEFDEVS KIMGAVRVEA AKRTGHFEEG
     VFRFCWIVDF PMFERNEDTG QIEFSHNPFS MPQGGLEALE TKDPLDILAW QYDIVCNGVE
     LSSGAIRNHE PDVMYKAFAL AGYDRDEVER EFGGMLRAFH FGAPPHGGIA PGVDRIVMLL
     ADEPNIRETI AFPLNGNAQD LLMGAPSEVD EARLRELHLS VRKPPQVKKA ETSEKAETSE
     KAEKADKAEK TAAEAEKPAE
//