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 28-MAR-2018, entry version 54. DE RecName: Full=D-aminoacyl-tRNA deacylase {ECO:0000255|HAMAP-Rule:MF_00518}; DE Short=DTD {ECO:0000255|HAMAP-Rule:MF_00518}; DE EC=3.1.1.96 {ECO:0000255|HAMAP-Rule:MF_00518}; DE AltName: Full=Gly-tRNA(Ala) deacylase {ECO:0000255|HAMAP-Rule:MF_00518}; DE EC=3.1.1.- {ECO:0000255|HAMAP-Rule:MF_00518}; 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: An aminoacyl-tRNA editing enzyme that deacylates CC mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl- CC tRNA(Ala), protecting cells against glycine mischarging by AlaRS. CC Acts via tRNA-based rather than protein-based catalysis; rejects CC L-amino acids rather than detecting D-amino acids in the active CC site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA CC molecules, this enzyme counteracts the toxicity associated with CC the formation of D-aminoacyl-tRNA entities in vivo and helps CC enforce protein L-homochirality. {ECO:0000255|HAMAP- CC Rule:MF_00518}. CC -!- CATALYTIC ACTIVITY: Glycyl-tRNA(Ala) + H(2)O = glycine + CC tRNA(Ala). {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 -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00518}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00518}. CC -!- DOMAIN: A Gly-cisPro motif from one monomer fits into the active CC site of the other monomer to allow specific chiral rejection of L- CC amino acids. {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 SMR; B9KAP7; -. DR STRING; 309803.CTN_1854; -. DR EnsemblBacteria; ACM24030; ACM24030; CTN_1854. DR KEGG; tna:CTN_1854; -. DR eggNOG; ENOG4108YYA; Bacteria. DR eggNOG; COG1490; LUCA. DR HOGENOM; HOG000113981; -. DR KO; K07560; -. DR OMA; GVFQAHM; -. DR OrthoDB; POG091H02D0; -. DR Proteomes; UP000000445; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051499; F:D-aminoacyl-tRNA deacylase activity; IEA:UniProtKB-EC. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR CDD; cd00563; Dtyr_deacylase; 1. 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_sf. 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; RNA-binding; tRNA-binding. FT CHAIN 1 149 D-aminoacyl-tRNA deacylase. FT /FTId=PRO_1000146219. FT MOTIF 137 138 Gly-cisPro motif, important for rejection FT of L-amino acids. {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 //