DTD_DROME
ID DTD_DROME Reviewed; 158 AA.
AC Q9VGP0; Q4V4U7; Q4V6L2;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=D-aminoacyl-tRNA deacylase {ECO:0000250|UniProtKB:Q8IIS0};
DE EC=3.1.1.96 {ECO:0000269|PubMed:28362257};
DE AltName: Full=Gly-tRNA(Ala) deacylase {ECO:0000303|PubMed:28362257};
DE AltName: Full=Gly-tRNA(Gly) deacylase {ECO:0000303|PubMed:27224426};
GN Name=Dtd {ECO:0000312|FlyBase:FBgn0037898};
GN ORFNames=CG18643 {ECO:0000312|FlyBase:FBgn0037898};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J.,
RA Park S., Wan K., Yu C., Celniker S.;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND SUBSTRATE SPECIFICITY.
RX PubMed=27224426; DOI=10.1371/journal.pbio.1002465;
RA Routh S.B., Pawar K.I., Ahmad S., Singh S., Suma K., Kumar M., Kuncha S.K.,
RA Yadav K., Kruparani S.P., Sankaranarayanan R.;
RT "Elongation factor Tu prevents misediting of Gly-tRNA(Gly) caused by the
RT design behind the chiral proofreading site of D-aminoacyl-tRNA deacylase.";
RL PLoS Biol. 14:E1002465-E1002465(2016).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=28362257; DOI=10.7554/elife.24001;
RA Pawar K.I., Suma K., Seenivasan A., Kuncha S.K., Routh S.B.,
RA Kruparani S.P., Sankaranarayanan R.;
RT "Role of D-aminoacyl-tRNA deacylase beyond chiral proofreading as a
RT cellular defense against glycine mischarging by AlaRS.";
RL Elife 6:0-0(2017).
CC -!- FUNCTION: An aminoacyl-tRNA editing enzyme that deacylates mischarged
CC D-aminoacyl-tRNAs (By similarity). Hydrolyzes correctly charged,
CC achiral, glycyl-tRNA(Gly) (PubMed:27224426). Deacylates mischarged
CC endogenous and E.coli glycyl-tRNA(Ala), protecting cells against
CC glycine mischarging by AlaRS (PubMed:28362257). Acts via tRNA-based
CC rather than protein-based catalysis; rejects L-amino acids rather than
CC detecting D-amino acids in the active site (By similarity). By
CC recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules,
CC this enzyme counteracts the toxicity associated with the formation of
CC D-aminoacyl-tRNA entities in vivo and helps enforce protein L-
CC homochirality (By similarity). {ECO:0000250|UniProtKB:Q8IIS0,
CC ECO:0000269|PubMed:27224426, ECO:0000269|PubMed:28362257}.
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:0000269|PubMed:28362257};
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:0000269|PubMed:28362257};
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; AE014297; AAF54636.2; -; Genomic_DNA.
DR EMBL; BT022294; AAY54710.1; -; mRNA.
DR EMBL; BT022909; AAY55325.1; -; mRNA.
DR EMBL; KX531645; ANY27455.1; -; mRNA.
DR RefSeq; NP_650072.2; NM_141815.2.
DR AlphaFoldDB; Q9VGP0; -.
DR SMR; Q9VGP0; -.
DR STRING; 7227.FBpp0290123; -.
DR PaxDb; Q9VGP0; -.
DR DNASU; 41371; -.
DR EnsemblMetazoa; FBtr0300901; FBpp0290123; FBgn0037898.
DR GeneID; 41371; -.
DR KEGG; dme:Dmel_CG18643; -.
DR UCSC; CG18643-RA; d. melanogaster.
DR CTD; 41371; -.
DR FlyBase; FBgn0037898; Dtd.
DR VEuPathDB; VectorBase:FBgn0037898; -.
DR eggNOG; KOG3323; Eukaryota.
DR GeneTree; ENSGT00940000153431; -.
DR HOGENOM; CLU_076901_0_4_1; -.
DR InParanoid; Q9VGP0; -.
DR OMA; GVFQAHM; -.
DR PhylomeDB; Q9VGP0; -.
DR BioGRID-ORCS; 41371; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41371; -.
DR PRO; PR:Q9VGP0; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0037898; Expressed in oviduct (Drosophila) and 26 other tissues.
DR ExpressionAtlas; Q9VGP0; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0051500; F:D-tyrosyl-tRNA(Tyr) deacylase activity; IBA:GO_Central.
DR GO; GO:0106026; F:Gly-tRNA(Ala) hydrolase activity; IDA:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
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 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 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Reference proteome; RNA-binding; tRNA-binding.
FT CHAIN 1..158
FT /note="D-aminoacyl-tRNA deacylase"
FT /id="PRO_0000441701"
FT MOTIF 138..139
FT /note="Gly-cisPro motif, important for rejection of L-amino
FT acids"
FT /evidence="ECO:0000250|UniProtKB:Q8IIS0"
FT CONFLICT 93
FT /note="L -> S (in Ref. 3; AAY55325)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="T -> S (in Ref. 3; AAY55325)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 158 AA; 17889 MW; 0594949F3D09F6B4 CRC64;
MRAVIQRVKA AKVTVLDELV SSIGPGLCVL VGIKASDTAK DVEYLVRKIL ALRLFEEEGK
RWQKSVKDLN LELLCVSQFT LYHRLKGNKP DFLAAMKGEE AQELYNQFLD RLGQSYDSTK
IKDGKFGAYM QVHIENDGPV TINLESPEQK DTDREVDK
