DTD_DICDI
ID DTD_DICDI Reviewed; 151 AA.
AC Q54EY1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=D-aminoacyl-tRNA deacylase {ECO:0000250|UniProtKB:Q8IIS0};
DE Short=DTD;
DE EC=3.1.1.96 {ECO:0000250|UniProtKB:Q8IIS0};
DE AltName: Full=Gly-tRNA(Ala) deacylase {ECO:0000250|UniProtKB:Q8IIS0};
GN Name=dtd; ORFNames=DDB_G0291273;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: An aminoacyl-tRNA editing enzyme that deacylates mischarged
CC D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala),
CC protecting cells against glycine mischarging by AlaRS. Acts via tRNA-
CC based rather than protein-based catalysis; rejects L-amino acids rather
CC than detecting D-amino acids in the active site. By recycling D-
CC aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme
CC counteracts the toxicity associated with the formation of D-aminoacyl-
CC tRNA entities in vivo and helps enforce protein L-homochirality.
CC {ECO:0000250|UniProtKB:Q8IIS0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala);
CC Xref=Rhea:RHEA:53744, Rhea:RHEA-COMP:9657, Rhea:RHEA-COMP:13640,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78522; EC=3.1.1.96;
CC Evidence={ECO:0000250|UniProtKB:Q8IIS0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA +
CC H(+); Xref=Rhea:RHEA:13953, Rhea:RHEA-COMP:10123, Rhea:RHEA-
CC COMP:10124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:59871,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:79333; EC=3.1.1.96;
CC Evidence={ECO:0000250|UniProtKB:Q8IIS0};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8IIS0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8IIS0}.
CC -!- DOMAIN: A Gly-cisPro motif from one monomer fits into the active site
CC of the other monomer to allow specific chiral rejection of L-amino
CC acids. {ECO:0000250|UniProtKB:Q8IIS0}.
CC -!- SIMILARITY: Belongs to the DTD family. {ECO:0000305}.
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DR EMBL; AAFI02000177; EAL61620.1; -; Genomic_DNA.
DR RefSeq; XP_635109.1; XM_630017.1.
DR AlphaFoldDB; Q54EY1; -.
DR SMR; Q54EY1; -.
DR STRING; 44689.DDB0266900; -.
DR PaxDb; Q54EY1; -.
DR EnsemblProtists; EAL61620; EAL61620; DDB_G0291273.
DR GeneID; 8628056; -.
DR KEGG; ddi:DDB_G0291273; -.
DR dictyBase; DDB_G0291273; dtd.
DR eggNOG; KOG3323; Eukaryota.
DR HOGENOM; CLU_076901_0_4_1; -.
DR InParanoid; Q54EY1; -.
DR OMA; GVFQAHM; -.
DR PhylomeDB; Q54EY1; -.
DR PRO; PR:Q54EY1; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0051500; F:D-tyrosyl-tRNA(Tyr) deacylase activity; ISS:dictyBase.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0019478; P:D-amino acid catabolic process; ISS:dictyBase.
DR GO; GO:0006399; P:tRNA metabolic process; IBA:GO_Central.
DR CDD; cd00563; Dtyr_deacylase; 1.
DR Gene3D; 3.50.80.10; -; 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 Cytoplasm; Hydrolase; Reference proteome; RNA-binding; tRNA-binding.
FT CHAIN 1..151
FT /note="D-aminoacyl-tRNA deacylase"
FT /id="PRO_0000328259"
FT MOTIF 140..141
FT /note="Gly-cisPro motif, important for rejection of L-amino
FT acids"
FT /evidence="ECO:0000250|UniProtKB:Q8IIS0"
SQ SEQUENCE 151 AA; 17400 MW; 5C25C1537BFE966E CRC64;
MKAIIQRVKS SSVTVEGEVI SEIKQGLMCL IGIGRDDTKE DAEYITRKIL NLRLWKNEDG
TKNWDRSVQQ MDYEILFVSQ FTLFAQLKGN KQSYHLAMAP ELSKQFYLDF LENAKKSYKP
EKIKDGRFGA MMDVQLINDG PVTIQLDSKE K
