ID   TATD1_BOVIN             Reviewed;         297 AA.
AC   Q148G4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Deoxyribonuclease TATDN1;
DE            EC=3.1.21.-;
GN   Name=TATDN1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) 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; BC118354; AAI18355.1; -; mRNA.
DR   RefSeq; NP_001068870.1; NM_001075402.2.
DR   AlphaFoldDB; Q148G4; -.
DR   SMR; Q148G4; -.
DR   STRING; 9913.ENSBTAP00000044772; -.
DR   PaxDb; Q148G4; -.
DR   Ensembl; ENSBTAT00000047576; ENSBTAP00000044772; ENSBTAG00000033446.
DR   GeneID; 509365; -.
DR   KEGG; bta:509365; -.
DR   CTD; 83940; -.
DR   VEuPathDB; HostDB:ENSBTAG00000033446; -.
DR   VGNC; VGNC:35617; TATDN1.
DR   eggNOG; KOG3020; Eukaryota.
DR   GeneTree; ENSGT00940000156272; -.
DR   HOGENOM; CLU_031506_1_0_1; -.
DR   InParanoid; Q148G4; -.
DR   OMA; PNEAPRI; -.
DR   OrthoDB; 1224437at2759; -.
DR   TreeFam; TF324192; -.
DR   Proteomes; UP000009136; Chromosome 14.
DR   Bgee; ENSBTAG00000033446; Expressed in mammary gland fat and 106 other tissues.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0008296; F:3'-5'-exodeoxyribonuclease activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; 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_0000313589"
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"
FT   MOD_RES         27
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P8M1"
FT   MOD_RES         46
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P8M1"
SQ   SEQUENCE   297 AA;  33886 MW;  A91B7CC59C0ED8BA CRC64;
     MSRFKFVDIG INLTDPMFRG IYRGVQKHQD DLQDVIERAV QIGVKKFMIT GGNLQDSKDA
     LHLAQTNDMF FSTVGCHPTR CDEFEKNDPD HYLMELLNLA ESNKGKVVAI GECGLDFDRL
     QFCSKDTQLK YFEKQFELSE QTKLPMFLHC RNSHAEFLDI MRRNRDRCVG GVVHSFDGTK
     EAAAALMDLG LYIGFNGCSL KTEANLEVLK SIPSEKLMIE TDAPWCGVKN THAGSKYIKT
     SFPTKKKWEN GHCLKDRNEP CHIIQILEIM SAVRDEDPLE LANTLYNNTI KIFFPDM