DTD1_LEIMA
ID DTD1_LEIMA Reviewed; 152 AA.
AC Q4Q1E7;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 96.
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; ORFNames=LMJF_36_2730 {ECO:0000312|EMBL:CAJ09232.1};
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin;
RX PubMed=16020728; DOI=10.1126/science.1112680;
RA Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA Ciarloni L., Clayton C., Coulson R.M.R., Cronin A., Cruz A.K., Davies R.M.,
RA De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA Masuy D., Matthews K., Michaeli S., Mottram J.C., Mueller-Auer S.,
RA Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA Rutter S., Saunders D., Schaefer M., Schein J., Schwartz D.C., Seeger K.,
RA Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA Barrell B.G., Myler P.J.;
RT "The genome of the kinetoplastid parasite, Leishmania major.";
RL Science 309:436-442(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin;
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
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: 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 D.melanogaster 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 recycling D-aminoacyl-
CC tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts
CC the toxicity associated with the formation of D-aminoacyl-tRNA entities
CC in 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=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; FR796432; CAJ09232.1; -; Genomic_DNA.
DR RefSeq; XP_001686851.1; XM_001686799.1.
DR AlphaFoldDB; Q4Q1E7; -.
DR SMR; Q4Q1E7; -.
DR STRING; 5664.LmjF.36.2730; -.
DR EnsemblProtists; CAJ09232; CAJ09232; LMJF_36_2730.
DR GeneID; 5655562; -.
DR KEGG; lma:LMJF_36_2730; -.
DR VEuPathDB; TriTrypDB:LmjF.36.2730; -.
DR VEuPathDB; TriTrypDB:LMJLV39_360036200; -.
DR VEuPathDB; TriTrypDB:LMJSD75_360036100; -.
DR eggNOG; KOG3323; Eukaryota.
DR HOGENOM; CLU_076901_0_4_1; -.
DR InParanoid; Q4Q1E7; -.
DR OMA; GVFQAHM; -.
DR Proteomes; UP000000542; Chromosome 36.
DR GO; GO:0005737; C:cytoplasm; ISO:GeneDB.
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 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..152
FT /note="D-aminoacyl-tRNA deacylase 1"
FT /id="PRO_0000441702"
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 152 AA; 16994 MW; 2EB074B4C941C1F6 CRC64;
MKAVIQRVLS GSVTSEGEVV GSIQKGLAVL VGIARDDTAD DTEYILRKIL GVRVWSNEDG
SKMWCRNVKE IDGEVLLISQ FTLMHVMKGN KPDFHNAMPP EDALKVFNAL RDKLRCEYAP
HKIATGNFQH YMNIHLSNDG PVTLILDSKK RS
