DTD2_CHICK
ID DTD2_CHICK Reviewed; 167 AA.
AC E1C762;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 2.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=D-aminoacyl-tRNA deacylase 2 {ECO:0000305};
DE EC=3.1.1.96 {ECO:0000269|PubMed:29410408};
DE AltName: Full=Animalia-specific tRNA deacylase {ECO:0000303|PubMed:29410408};
DE Short=ATD {ECO:0000303|PubMed:29410408};
DE AltName: Full=D-tyrosyl-tRNA(Tyr) deacylase 2;
DE AltName: Full=L-alanyl-tRNA deacylase {ECO:0000305|PubMed:29410408};
GN Name=DTD2 {ECO:0000312|Ensembl:ENSGALP00000031950};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000312|Proteomes:UP000000539};
RN [1] {ECO:0000312|Proteomes:UP000000539}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl {ECO:0000312|Proteomes:UP000000539};
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [2] {ECO:0000305}
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=29410408; DOI=10.1038/s41467-017-02204-w;
RA Kuncha S.K., Mazeed M., Singh R., Kattula B., Routh S.B.,
RA Sankaranarayanan R.;
RT "A chiral selectivity relaxed paralog of DTD for proofreading tRNA
RT mischarging in Animalia.";
RL Nat. Commun. 9:511-511(2018).
CC -!- FUNCTION: Deacylates mischarged D-aminoacyl-tRNAs (By similarity). Also
CC deacylates mischarged glycyl-tRNA(Ala), protecting cells against
CC glycine mischarging by AlaRS (By similarity). Probably acts by
CC rejecting L-amino acids from its binding site rather than specific
CC recognition of D-amino acids (By similarity). Catalyzes the hydrolysis
CC of D-tyrosyl-tRNA(Tyr), has no activity on correctly charged L-tyrosyl-
CC tRNA(Tyr) (By similarity). By recycling D-aminoacyl-tRNA to D-amino
CC acids and free tRNA molecules, this enzyme counteracts the toxicity
CC associated with the formation of D-aminoacyl-tRNA entities in vivo and
CC helps enforce protein L-homochirality. In contrast to DTD1, deacylates
CC L-Ala mischarged on tRNA(Thr)(G4.U69) by alanine-tRNA ligase AARS
CC (PubMed:29410408). Can deacylate L-Ala due to a relaxed specificity for
CC substrate chirality caused by the trans conformation of the Gly-Pro
CC motif in the active site (PubMed:29410408). Also hydrolyzes correctly
CC charged, achiral, glycyl-tRNA(Gly) in vitro, although in vivo
CC EEF1A1/EF-Tu may protect cognate achiral glycyl-tRNA(Gly) from DTD2-
CC mediated deacetylation (By similarity). {ECO:0000250|UniProtKB:Q8BHA3,
CC ECO:0000269|PubMed:29410408}.
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:29410408};
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:29410408};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-tyrosyl-tRNA(Tyr) + H2O = D-tyrosine + tRNA(Tyr);
CC Xref=Rhea:RHEA:25347, Rhea:RHEA-COMP:9707, Rhea:RHEA-COMP:9872,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:58570, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78723; Evidence={ECO:0000250|UniProtKB:Q8BHA3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-alanyl-tRNA(Thr) = H(+) + L-alanine + tRNA(Thr);
CC Xref=Rhea:RHEA:17793, Rhea:RHEA-COMP:9670, Rhea:RHEA-COMP:14576,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78497;
CC Evidence={ECO:0000269|PubMed:29410408};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8BHA3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: A Gly-transPro motif from one monomer fits into the active site
CC of the other monomer to allow specific chiral rejection of most L-amino
CC acids except L-Ala. The trans conformation of the motif is maintained
CC by Arg-150. {ECO:0000250|UniProtKB:Q8BHA3}.
CC -!- SIMILARITY: Belongs to the DTD family. {ECO:0000305}.
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DR EMBL; AADN04000014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_001234140.2; XM_001234139.4.
DR AlphaFoldDB; E1C762; -.
DR SMR; E1C762; -.
DR STRING; 9031.ENSGALP00000031950; -.
DR PaxDb; E1C762; -.
DR Ensembl; ENSGALT00000032587; ENSGALP00000031950; ENSGALG00000009978.
DR GeneID; 770817; -.
DR KEGG; gga:770817; -.
DR CTD; 112487; -.
DR VEuPathDB; HostDB:geneid_770817; -.
DR eggNOG; KOG3323; Eukaryota.
DR GeneTree; ENSGT00940000153431; -.
DR HOGENOM; CLU_076118_1_0_1; -.
DR InParanoid; E1C762; -.
DR OMA; NAKCMEA; -.
DR OrthoDB; 1170114at2759; -.
DR PhylomeDB; E1C762; -.
DR TreeFam; TF329119; -.
DR PRO; PR:E1C762; -.
DR Proteomes; UP000000539; Chromosome 5.
DR Bgee; ENSGALG00000009978; Expressed in heart and 14 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0106105; F:Ala-tRNA(Thr) hydrolase activity; IDA:UniProtKB.
DR GO; GO:0051500; F:D-tyrosyl-tRNA(Tyr) deacylase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0106074; P:aminoacyl-tRNA metabolism involved in translational fidelity; IDA:UniProtKB.
DR GO; GO:0006399; P:tRNA metabolic process; IBA:GO_Central.
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.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Reference proteome; RNA-binding; tRNA-binding.
FT CHAIN 1..167
FT /note="D-aminoacyl-tRNA deacylase 2"
FT /id="PRO_0000444310"
FT MOTIF 159..160
FT /note="Gly-transPro motif, allows the protein to recognize
FT chirality of D-amino acids"
FT /evidence="ECO:0000250|UniProtKB:Q8BHA3"
SQ SEQUENCE 167 AA; 18653 MW; CB61EC794A2264E2 CRC64;
MAAARPVLAR ALLQQCLFAR LQVKPPEHGA EAEWEEIQRG LVIYICFFKG ADEDLVPKIV
NVLLNVKLSE DENGEYVSVL DLPGNVLIIP QATLGGKLKG RKMQYHTNIE KEKGMELYSQ
FVSLCEKELA ANPKCMEAGV LVKHGTYGNR QVLKLDTNGP YTHLVEF
