DTD1_DANRE
ID DTD1_DANRE Reviewed; 207 AA.
AC F1QGC8; Q6DH41;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=D-aminoacyl-tRNA deacylase 1 {ECO:0000250|UniProtKB:Q8IIS0};
DE EC=3.1.1.96 {ECO:0000269|PubMed:28362257};
DE AltName: Full=Gly-tRNA(Ala) deacylase 1 {ECO:0000303|PubMed:28362257};
DE AltName: Full=Gly-tRNA(Gly) deacylase 1 {ECO:0000303|PubMed:27224426};
GN Name=dtd1 {ECO:0000312|ZFIN:ZDB-GENE-040801-175};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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: D-aminoacyl-tRNA deacylase, with no observable activity on
CC tRNAs charged with their cognate L-amino acid (By similarity).
CC Hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly)
CC (PubMed:27224426). Deacylates mischarged D.melanogaster and E.coli
CC glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS
CC (PubMed:28362257). Acts via tRNA-based rather than protein-based
CC catalysis; rejects L-amino acids rather than detecting D-amino acids in
CC the active site (By similarity). By recycling D-aminoacyl-tRNA to D-
CC amino acids and free tRNA molecules, this enzyme counteracts the
CC toxicity associated with the formation of D-aminoacyl-tRNA entities in
CC vivo and helps enforce protein L-homochirality (By similarity).
CC {ECO:0000250|UniProtKB:Q8IIS0, ECO:0000269|PubMed:27224426,
CC 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 -!- 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 -!- 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; AL929341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC076141; AAH76141.1; -; mRNA.
DR RefSeq; NP_001003440.1; NM_001003440.1.
DR AlphaFoldDB; F1QGC8; -.
DR SMR; F1QGC8; -.
DR STRING; 7955.ENSDARP00000065565; -.
DR PaxDb; F1QGC8; -.
DR Ensembl; ENSDART00000065566; ENSDARP00000065565; ENSDARG00000044628.
DR Ensembl; ENSDART00000189422; ENSDARP00000147742; ENSDARG00000044628.
DR GeneID; 445046; -.
DR KEGG; dre:445046; -.
DR CTD; 92675; -.
DR ZFIN; ZDB-GENE-040801-175; dtd1.
DR eggNOG; KOG3323; Eukaryota.
DR GeneTree; ENSGT00940000153431; -.
DR HOGENOM; CLU_076901_0_0_1; -.
DR InParanoid; F1QGC8; -.
DR OMA; GVFQAHM; -.
DR OrthoDB; 1411453at2759; -.
DR PhylomeDB; F1QGC8; -.
DR TreeFam; TF314886; -.
DR PRO; PR:F1QGC8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 6.
DR Bgee; ENSDARG00000044628; Expressed in granulocyte and 21 other tissues.
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 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..207
FT /note="D-aminoacyl-tRNA deacylase 1"
FT /id="PRO_0000441700"
FT REGION 142..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 139..140
FT /note="Gly-cisPro motif, important for rejection of L-amino
FT acids"
FT /evidence="ECO:0000250|UniProtKB:Q8IIS0"
FT COMPBIAS 159..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 35
FT /note="V -> A (in Ref. 2; AAH76141)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 207 AA; 23037 MW; F17D80B324745086 CRC64;
MKAIIQRVTR ASVTVGEEQI SSIGRGLCVL LGISVEDTQK DVDYMVRKIL NLRVFEDENG
RAWSRSVMDG ELEVLCVSQF TLQCLLKGNK PDYHAAMPAE LAQPFYNNML EQLRETYKPE
LIKDGQFGAK MQVLIQNDGP VTIQLESPPA PTDPKLLSKQ EKQQQRKEKT RSKGPSDSSR
EKAAQRSKVD PSASSGAEGD VSSEREP
