ID   TYDP1_CAEEL             Reviewed;         451 AA.
AC   Q9TXV7;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Probable tyrosyl-DNA phosphodiesterase;
DE            Short=Tyr-DNA phosphodiesterase;
DE            EC=3.1.4.- {ECO:0000250|UniProtKB:Q9NUW8};
GN   ORFNames=F52C12.1;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: DNA repair enzyme that can remove a variety of covalent
CC       adducts from DNA through hydrolysis of a 3'-phosphodiester bond, giving
CC       rise to DNA with a free 3' phosphate. Catalyzes the hydrolysis of dead-
CC       end complexes between DNA and the topoisomerase I active site tyrosine
CC       residue. Hydrolyzes 3'-phosphoglycolates on protruding 3' ends on DNA
CC       double-strand breaks due to DNA damage by radiation and free radicals.
CC       Acts on blunt-ended double-strand DNA breaks and on single-stranded
CC       DNA. May have low 3'exonuclease activity and may be able to remove a
CC       single nucleoside from the 3'end of DNA and RNA molecules with
CC       3'hydroxyl groups. Has no exonuclease activity towards DNA or RNA with
CC       a 3'phosphate (By similarity). {ECO:0000250|UniProtKB:Q9NUW8}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NUW8}.
CC   -!- SIMILARITY: Belongs to the tyrosyl-DNA phosphodiesterase family.
CC       {ECO:0000305}.
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DR   EMBL; FO081438; CCD71624.1; -; Genomic_DNA.
DR   PIR; A88641; A88641.
DR   RefSeq; NP_500149.1; NM_067748.4.
DR   AlphaFoldDB; Q9TXV7; -.
DR   SMR; Q9TXV7; -.
DR   STRING; 6239.F52C12.1a; -.
DR   EPD; Q9TXV7; -.
DR   PaxDb; Q9TXV7; -.
DR   PeptideAtlas; Q9TXV7; -.
DR   EnsemblMetazoa; F52C12.1a.1; F52C12.1a.1; WBGene00018678.
DR   GeneID; 176996; -.
DR   KEGG; cel:CELE_F52C12.1; -.
DR   UCSC; F52C12.1; c. elegans.
DR   CTD; 176996; -.
DR   WormBase; F52C12.1a; CE19434; WBGene00018678; -.
DR   eggNOG; KOG2031; Eukaryota.
DR   InParanoid; Q9TXV7; -.
DR   OMA; HDMSSAN; -.
DR   OrthoDB; 1295967at2759; -.
DR   PhylomeDB; Q9TXV7; -.
DR   PRO; PR:Q9TXV7; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00018678; Expressed in germ line (C elegans) and 4 other tissues.
DR   ExpressionAtlas; Q9TXV7; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0017005; F:3'-tyrosyl-DNA phosphodiesterase activity; IBA:GO_Central.
DR   GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR   GO; GO:0000012; P:single strand break repair; IBA:GO_Central.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   InterPro; IPR010347; Tdp1.
DR   PANTHER; PTHR12415; PTHR12415; 1.
DR   Pfam; PF06087; Tyr-DNA_phospho; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA repair; Exonuclease; Hydrolase; Nuclease; Nucleus;
KW   Reference proteome; Repeat.
FT   CHAIN           1..451
FT                   /note="Probable tyrosyl-DNA phosphodiesterase"
FT                   /id="PRO_0000212488"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          266..269
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NUW8"
FT   ACT_SITE        131
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NUW8"
FT   ACT_SITE        356
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NUW8"
FT   BINDING         133
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NUW8"
FT   BINDING         358
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NUW8"
FT   SITE            379
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NUW8"
SQ   SEQUENCE   451 AA;  51058 MW;  02C81CB96FC90C2C CRC64;
     MKRTIQETPG PSSTTVPPPK KLNSQRNGSN LEPGSIYFTP IGGISVPRQE SESSRSLDEI
     LADIRPINSL HFSFMLDFEF LIGSYPPSLR EYPITLVVGA PDAPDLLKCT KNQKLVTVVG
     ASLPIPFGTH HTKMSILEDE DGRFHVIVST ANLVPDDWEF KTQQFYYNFG VKIASGTVPR
     SDFQDDLLEY LSMYRNQLDT WKQLLQKVDF SQISDRLIFS TPGYHTDPPT QRPGHPRLFR
     ILSEKFPFDA SYEHTERCTF VAQCSSIGSL GSAPINWFRG QFLQSLEGAN PSPKQKPAKM
     YLVFPSVEDV RTSCQGYAGG CSVPYRNSVH ARQKWLQGNM CKWRSNAKRR TNAVPHCKTY
     VKYDKKVAIW QLLTSANLSK AAWGEVSFNK SKNVEQLMIR SWEMGVLITD PSRFNIPFDY
     PLVPYSATDE PFVTDKKHEK PDILGCIWTP P