ID   TATD1_XENLA             Reviewed;         297 AA.
AC   Q640V9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Deoxyribonuclease TATDN1;
DE            EC=3.1.21.-;
GN   Name=tatdn1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Deoxyribonuclease which catalyzes (in vitro) the decatenation
CC       of kinetoplast DNA, which are circular DNA catenated to each other,
CC       producing linear DNA molecules (By similarity). Plays an important role
CC       in chromosomal segregation and cell cycle progression during eye
CC       development probably via its DNA decatenation activity (By similarity).
CC       {ECO:0000250|UniProtKB:Q6GML7}.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250|UniProtKB:Q17R31};
CC       Note=Binds 2 divalent metal cations per subunit.
CC       {ECO:0000250|UniProtKB:Q17R31};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       TatD-type hydrolase family. {ECO:0000305}.
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DR   EMBL; BC082480; AAH82480.1; -; mRNA.
DR   RefSeq; NP_001087965.1; NM_001094496.1.
DR   AlphaFoldDB; Q640V9; -.
DR   SMR; Q640V9; -.
DR   MaxQB; Q640V9; -.
DR   DNASU; 494648; -.
DR   GeneID; 494648; -.
DR   KEGG; xla:494648; -.
DR   CTD; 494648; -.
DR   Xenbase; XB-GENE-945965; tatdn1.L.
DR   OrthoDB; 1224437at2759; -.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 494648; Expressed in testis and 19 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR   CDD; cd01310; TatD_DNAse; 1.
DR   InterPro; IPR018228; DNase_TatD-rel_CS.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR001130; TatD-like.
DR   Pfam; PF01026; TatD_DNase; 1.
DR   PIRSF; PIRSF005902; DNase_TatD; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   PROSITE; PS01091; TATD_3; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Metal-binding; Nuclease; Nucleus; Reference proteome.
FT   CHAIN           1..297
FT                   /note="Deoxyribonuclease TATDN1"
FT                   /id="PRO_0000313593"
FT   BINDING         112
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R31"
FT   BINDING         112
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R31"
FT   BINDING         149
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R31"
FT   BINDING         174
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R31"
FT   BINDING         222
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R31"
SQ   SEQUENCE   297 AA;  33863 MW;  02A0DB7B3A630AAD CRC64;
     MSLYRFIDIG INLTDPMFRG LYRGTRKHQD DFADIIERAV RTGVQKFMIT GGNLHESKEA
     IQLAQSNDRF YSTVGCHPTR CGEFEQGDPD QYLAELQNLL EDNKGKVVAV GECGLDFDRL
     EFCSKETQLK YFEKQFDLAE RSRLPMFLHC RNAHKEFLEI MQRNRDRCVG GVVHSFDGTK
     EDAEAIIALD LYIGINGCSL KTESNLDVLK SIPSERLMIE TDAPWCGVKN THAGSKLVKT
     TFPTKKKWES GHCLKDRNEP CHIIQVLEIM ASAREEEPLE LSKTLYNNTL KLFFPAA