ID DTD_THENN Reviewed; 149 AA. AC B9KAP7; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 24-MAR-2009, sequence version 1. DT 27-MAY-2015, entry version 41. DE RecName: Full=D-aminoacyl-tRNA deacylase {ECO:0000255|HAMAP-Rule:MF_00518}; DE EC=3.1.1.96 {ECO:0000255|HAMAP-Rule:MF_00518}; DE AltName: Full=D-tyrosyl-tRNA(Tyr) deacylase; GN Name=dtd {ECO:0000255|HAMAP-Rule:MF_00518}; GN OrderedLocusNames=CTN_1854; OS Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NS-E). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=309803; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49049 / DSM 4359 / NS-E; RA Lim S.K., Kim J.S., Cha S.H., Park B.C., Lee D.S., Tae H.S., RA Kim S.-J., Kim J.J., Park K.J., Lee S.Y.; RT "The genome sequence of the hyperthermophilic bacterium Thermotoga RT neapolitana."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: D-aminoacyl-tRNA deacylase with broad substrate CC specificity. By recycling D-aminoacyl-tRNA to D-amino acids and CC free tRNA molecules, this enzyme counteracts the toxicity CC associated with the formation of D-aminoacyl-tRNA entities in CC vivo. {ECO:0000255|HAMAP-Rule:MF_00518}. CC -!- CATALYTIC ACTIVITY: A D-aminoacyl-tRNA + H(2)O = a D-amino acid + CC tRNA. {ECO:0000255|HAMAP-Rule:MF_00518}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00518}. CC -!- SIMILARITY: Belongs to the DTD family. {ECO:0000255|HAMAP- CC Rule:MF_00518}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000916; ACM24030.1; -; Genomic_DNA. DR RefSeq; WP_015920266.1; NC_011978.1. DR RefSeq; YP_002535396.1; NC_011978.1. DR STRING; 309803.CTN_1854; -. DR EnsemblBacteria; ACM24030; ACM24030; CTN_1854. DR KEGG; tna:CTN_1854; -. DR PATRIC; 23942550; VBITheNea118396_1849. DR eggNOG; COG1490; -. DR HOGENOM; HOG000113981; -. DR KO; K07560; -. DR OMA; ENDGPFT; -. DR OrthoDB; EOG6C2WM2; -. DR BioCyc; TNEA309803:GJFG-1905-MONOMER; -. DR Proteomes; UP000000445; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:UniProtKB-HAMAP. DR GO; GO:0019478; P:D-amino acid catabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.50.80.10; -; 1. DR HAMAP; MF_00518; Deacylase_Dtd; 1. DR InterPro; IPR003732; Daa-tRNA_deacyls_DTD. DR InterPro; IPR023509; DTD-like_dom. DR PANTHER; PTHR10472; PTHR10472; 1. DR Pfam; PF02580; Tyr_Deacylase; 1. DR SUPFAM; SSF69500; SSF69500; 1. DR TIGRFAMs; TIGR00256; TIGR00256; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase. FT CHAIN 1 149 D-aminoacyl-tRNA deacylase. FT /FTId=PRO_1000146219. FT ACT_SITE 80 80 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00518}. SQ SEQUENCE 149 AA; 16589 MW; ED6505109AC134B7 CRC64; MRAVVQRVNE AKVIVDEKVV GAIGKGLLVF VGVGKDDTEK DCEWLAEKVS GLRIFEDEEG KMNLSIMDVG GEVLVVSQFT LYGDCRRGKR PSFTEAAPPE KGKELYEKFV DLLEKKGLKV EKGIFRAHMH VHLVNDGPVT LLLDSSRLF //