ID   TATD1_DANRE             Reviewed;         298 AA.
AC   Q6GML7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Deoxyribonuclease TATDN1;
DE            EC=3.1.21.-;
GN   Name=tatdn1; ORFNames=zgc:92362;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP   ASP-222.
RX   PubMed=23187801; DOI=10.4161/cc.22886;
RA   Yang H., Liu C., Jamsen J., Wu Z., Wang Y., Chen J., Zheng L., Shen B.;
RT   "The DNase domain-containing protein TATDN1 plays an important role in
RT   chromosomal segregation and cell cycle progression during zebrafish eye
RT   development.";
RL   Cell Cycle 11:4626-4632(2012).
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 (PubMed:23187801). Plays an important
CC       role in chromosomal segregation and cell cycle progression during eye
CC       development probably via its DNA decatenation activity
CC       (PubMed:23187801). {ECO:0000269|PubMed:23187801}.
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   -!- DEVELOPMENTAL STAGE: Predominantly expressed in the eye during
CC       embryonic development. {ECO:0000269|PubMed:23187801}.
CC   -!- DISRUPTION PHENOTYPE: Morpholino knockdown in the embryo results in an
CC       abnormal cell cycle progression, formation of polyploidy and aberrant
CC       chromatin structures (PubMed:23187801). Consequently, the morphants
CC       have disordered eye cell layers and significantly smaller eyes compared
CC       to the wild-type counterpart (PubMed:23187801).
CC       {ECO:0000269|PubMed:23187801}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       TatD-type hydrolase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC074027; AAH74027.1; -; mRNA.
DR   RefSeq; NP_001002213.1; NM_001002213.1.
DR   AlphaFoldDB; Q6GML7; -.
DR   SMR; Q6GML7; -.
DR   GeneID; 100151626; -.
DR   KEGG; dre:100151626; -.
DR   CTD; 83940; -.
DR   ZFIN; ZDB-GENE-040704-56; tatdn1.
DR   InParanoid; Q6GML7; -.
DR   OrthoDB; 1224437at2759; -.
DR   PhylomeDB; Q6GML7; -.
DR   PRO; PR:Q6GML7; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008296; F:3'-5'-exodeoxyribonuclease activity; IBA:GO_Central.
DR   GO; GO:0004530; F:deoxyribonuclease I activity; IDA:ZFIN.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IMP:ZFIN.
DR   GO; GO:0001654; P:eye development; IMP:ZFIN.
DR   GO; GO:0010842; P:retina layer formation; IMP:ZFIN.
DR   CDD; cd01310; TatD_DNAse; 1.
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.
PE   1: Evidence at protein level;
KW   Hydrolase; Metal-binding; Nuclease; Nucleus; Reference proteome.
FT   CHAIN           1..298
FT                   /note="Deoxyribonuclease TATDN1"
FT                   /id="PRO_0000313592"
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   MUTAGEN         222
FT                   /note="D->A: Loss of deoxyribonuclease and DNA decatenation
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:23187801"
SQ   SEQUENCE   298 AA;  33667 MW;  E267692FFE99AA53 CRC64;
     MTNFRFIDIG INLTDPMFRG VYRGTQKHED DFAEVVERAL QVGVQKFIIT GGNLEDSRAA
     LTLTHTREQF FSTVGCHPTR CSEFDDQGSD QYLSSLLDLT VSNTQKVVAV GECGLDFDRL
     EFCPKETQLR YFQLQFDLAE ASGLPMFLHC RNAHTEFIDI MRRNRQRCVG GVVHSFDGSQ
     QDAAALLDLD LYIGINGCSL KTAENLEVMK SIPSDRLMIE TDAPWCGIKN THAGAKLIKT
     SFPTKKKWET GHCVKDRNEP CHIIQVLEVM AAVREEDPLD LAETIFNNTD TLFFKNRS