ID   DTD2_LEIMA              Reviewed;         181 AA.
AC   P84066;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 2.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Putative D-tyrosyl-tRNA(Tyr) deacylase 2;
DE            EC=3.1.-.-;
OS   Leishmania major.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5664;
RN   [1] {ECO:0000305, ECO:0000312|PDB:1TC5}
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS), AND SUBUNIT.
RA   Robein M.A., Hol W.G.J.;
RT   "Structural analysis of a probable eukaryotic D-amino acid tRNA
RT   deacylase.";
RL   Submitted (JUN-2004) to the PDB data bank.
CC   -!- FUNCTION: May hydrolyze D-tyrosyl-tRNA(Tyr) into D-tyrosine and free
CC       tRNA(Tyr). Could be a defense mechanism against a harmful effect of D-
CC       tyrosine (By similarity). {ECO:0000250|UniProtKB:P32147}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DTD family. Highly divergent. {ECO:0000305}.
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DR   PDB; 1TC5; X-ray; 1.93 A; A/B/C/D=1-181.
DR   PDBsum; 1TC5; -.
DR   AlphaFoldDB; P84066; -.
DR   SMR; P84066; -.
DR   STRING; 5664.LmjF.34.3360; -.
DR   VEuPathDB; TriTrypDB:LmjF.34.3360; -.
DR   VEuPathDB; TriTrypDB:LMJLV39_340039400; -.
DR   VEuPathDB; TriTrypDB:LMJSD75_340039700; -.
DR   eggNOG; KOG3323; Eukaryota.
DR   EvolutionaryTrace; P84066; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051499; F:D-aminoacyl-tRNA deacylase activity; IEA:InterPro.
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   3D-structure; Cytoplasm; Hydrolase.
FT   CHAIN           1..181
FT                   /note="Putative D-tyrosyl-tRNA(Tyr) deacylase 2"
FT                   /id="PRO_0000164628"
FT   STRAND          1..11
FT                   /evidence="ECO:0007829|PDB:1TC5"
FT   STRAND          13..16
FT                   /evidence="ECO:0007829|PDB:1TC5"
FT   STRAND          18..21
FT                   /evidence="ECO:0007829|PDB:1TC5"
FT   STRAND          23..32
FT                   /evidence="ECO:0007829|PDB:1TC5"
FT   HELIX           42..54
FT                   /evidence="ECO:0007829|PDB:1TC5"
FT   STRAND          80..85
FT                   /evidence="ECO:0007829|PDB:1TC5"
FT   HELIX           87..90
FT                   /evidence="ECO:0007829|PDB:1TC5"
FT   STRAND          92..94
FT                   /evidence="ECO:0007829|PDB:1TC5"
FT   STRAND          97..99
FT                   /evidence="ECO:0007829|PDB:1TC5"
FT   HELIX           106..123
FT                   /evidence="ECO:0007829|PDB:1TC5"
FT   STRAND          135..139
FT                   /evidence="ECO:0007829|PDB:1TC5"
FT   HELIX           140..142
FT                   /evidence="ECO:0007829|PDB:1TC5"
FT   STRAND          146..148
FT                   /evidence="ECO:0007829|PDB:1TC5"
FT   STRAND          156..158
FT                   /evidence="ECO:0007829|PDB:1TC5"
FT   STRAND          167..172
FT                   /evidence="ECO:0007829|PDB:1TC5"
FT   STRAND          177..181
FT                   /evidence="ECO:0007829|PDB:1TC5"
SQ   SEQUENCE   181 AA;  20114 MW;  406E11C5B03123A1 CRC64;
     MLQAMDQGHL LVNNVDKYVR AGRGVMVYIA FLSDRDSAPI TDEALRHAVG VLLHTKIFTH
     FSPEKMINQP QSLEECPEMD ILIVPQASLG GKVKGRSVQF HQLVAKDVGA ALYDRFCHFV
     RVARGVDESR VDANGAPRSE GDAPKAEGWI KYNSRVISGT FGNRQGLRFE SEGPFTHMFD
     I