ID D9TIN1_CALOO Unreviewed; 594 AA.
AC D9TIN1;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-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=COB47_0545;
OS Caldicellulosiruptor obsidiansis (strain ATCC BAA-2073 / strain OB47).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacterales Family III. Incertae Sedis;
OC Caldicellulosiruptor.
OX NCBI_TaxID=608506;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2073 / strain OB47;
RX PubMed=20851897; DOI=10.1128/JB.00950-10;
RA Elkins J.G., Lochner A., Hamilton-Brehm S.D., Davenport K.W.,
RA Podar M., Brown S.D., Land M.L., Hauser L.J., Klingeman D.M.,
RA Raman B., Goodwin L.A., Tapia R., Meincke L.J., Detter J.C.,
RA Bruce D.C., Han C.S., Palumbo A.V., Cottingham R.W., Keller M.,
RA Graham D.E.;
RT "Complete genome sequence of the cellulolytic thermophile
RT Caldicellulosiruptor obsidiansis OB47T.";
RL J. Bacteriol. 192:6099-6100(2010).
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.
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; CP002164; ADL41863.1; -; Genomic_DNA.
DR RefSeq; YP_003839849.1; NC_014392.1.
DR EnsemblBacteria; ADL41863; ADL41863; COB47_0545.
DR GeneID; 9604972; -.
DR KEGG; cob:COB47_0545; -.
DR PATRIC; 42228265; VBICalObs143161_0605.
DR HOGENOM; HOG000275159; -.
DR KO; K01876; -.
DR BioCyc; COBS608506:GH1S-555-MONOMER; -.
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 594 AA; 67839 MW; F663761FDE4BA84F CRC64;
MESIKDFKRT KYCGEVSLED VGKEVVLTGW VDTRRDLGGI IFVDLRDRTG IVQVVFDEKM
GEELLDKADS LRSEYCIGIR GIVEKRPPET INPKIKTGEV EVRAQELRIF SKSETPPFPI
EEGINVNEAV RLKYRYLDLR RPDMQKNLMF RHKLYQVVRN FLSQNGFIEI ETPMLTKSTP
EGARDYLVPS RIFPGKFFAL PQSPQLFKQL LMVAGFDRYF QIVKCFRDED LRADRQPEFT
QIDIEMSFVD VDDVIEINER LLQTIFGEML GIDLKLPLPR LTYKEAMERF GSDKPDTRFG
MELVNLTDIA KNCEFKVFAD AANKGGSVRA INAKGCAITF SRREIDALVE YAKNFGAKGL
AWIAVESDGL KSPIVKFLKE EEINEILKRL GAEVGDLLLF SADKDEIVFD VLGNIRLEIA
RKLNLLDKSK FNLLWVTEFP LFEYSEEEGR YVAKHHPFTS PMDEDIEFLE TDPAKVRSKA
YDIVLNGTEI GGGSIRIHST ELQKRMFKAL GFTEERAQDR FGFLLEAFKY GTPPHGGIAY
GFDRLCMLLL GLDSIRDTIA FPKVKDSSCP LTDAPSEVEP KQLRELHIKV DVVK
//
