ID   D5X852_THEPJ            Unreviewed;       595 AA.
AC   D5X852;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   01-MAY-2013, entry version 23.
DE   RecName: Full=Aspartate--tRNA ligase;
DE            EC=6.1.1.12;
DE   AltName: Full=Aspartyl-tRNA synthetase;
GN   Name=aspS; OrderedLocusNames=TherJR_1923;
OS   Thermincola potens (strain JR).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Thermincola.
OX   NCBI_TaxID=635013;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JR;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Hazen T.C., Woyke T.;
RT   "Complete sequence of Thermincola sp. JR.";
RL   Submitted (MAY-2010) 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; CP002028; ADG82772.1; -; Genomic_DNA.
DR   RefSeq; YP_003640673.1; NC_014152.1.
DR   EnsemblBacteria; ADG82772; ADG82772; TherJR_1923.
DR   GeneID; 9149613; -.
DR   KEGG; tjr:TherJR_1923; -.
DR   PATRIC; 38275535; VBITheSp141296_2064.
DR   HOGENOM; HOG000275159; -.
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; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
SQ   SEQUENCE   595 AA;  67419 MW;  0932E2DDA2ECFF77 CRC64;
     MTASLKGLKR THHCGELRKT NIGEEVVLMG WVQRRRDHGG LIFVDLRDRS GLVQVVFSPD
     VDKEAFAKAE IIRSEYVLAV RGQVVARPEG TVNENLPTGE IDVNCLEVRI LNKAKTPPFY
     IEEDIDVDEN LRLKYRYLDL RRPDMQRNMI LRHKTTMAIR EFLDKAGFLE IETPMLTKST
     PEGARDYLVP SRVNPGKFYA LPQSPQIFKQ ILMVAGMEKY FQIVRCFRDE DLRADRQPEF
     TQVDMEMSFV DIDDVLALTE EMLAHAFRAA GIEITTPFER LTYKEAIDRY GSDKPDLRFG
     LELKDFTDIV KDSDFKVFAS VAAGGGQVKG INAKGCAGFS RKEIDDLTQF VGIYGAKGLA
     YIVVTEDGLK SPILKFFKEE EIKVILERFE AEPGDLLFFV ADKPSIVADA LGHLRVELAR
     RLNLIDDKVF KFVWIVEFPL LEYDEEERRY VAIHHPFTSP MDEDIPLLDS DPLVVRAKAY
     DVVLNGVELG GGSIRIHSRQ VQEKMFTLLG LSPEEAIEKF GFMLEAFEYG TPPHGGIAFG
     LDRMVMLMAG RDSIRDVIAF PKTQSATDLM TQAPSEVTAK QLRELHIKLN VVAPK
//