ID   TATD1_ENTBH             Reviewed;         274 AA.
AC   B7XJI2;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Putative deoxyribonuclease TATDN1 homolog;
DE            EC=3.1.21.-;
GN   ORFNames=EBI_25826;
OS   Enterocytozoon bieneusi (strain H348) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Enterocytozoonidae;
OC   Enterocytozoon.
OX   NCBI_TaxID=481877;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H348;
RX   PubMed=18060071; DOI=10.1371/journal.pone.0001277;
RA   Corradi N., Akiyoshi D.E., Morrison H.G., Feng X., Weiss L.M., Tzipori S.,
RA   Keeling P.J.;
RT   "Patterns of genome evolution among the microsporidian parasites
RT   Encephalitozoon cuniculi, Antonospora locustae and Enterocytozoon
RT   bieneusi.";
RL   PLoS ONE 2:E1277-E1277(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H348;
RX   PubMed=19132089; DOI=10.1371/journal.ppat.1000261;
RA   Akiyoshi D.E., Morrison H.G., Lei S., Feng X., Zhang Q., Corradi N.,
RA   Mayanja H., Tumwine J.K., Keeling P.J., Weiss L.M., Tzipori S.;
RT   "Genomic survey of the non-cultivatable opportunistic human pathogen,
RT   Enterocytozoon bieneusi.";
RL   PLoS Pathog. 5:E1000261-E1000261(2009).
CC   -!- FUNCTION: Putative deoxyribonuclease. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC       Note=Binds 2 divalent metal cations per subunit. {ECO:0000250};
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; ABGB01000029; EED43915.1; -; Genomic_DNA.
DR   RefSeq; XP_002650160.1; XM_002650114.1.
DR   AlphaFoldDB; B7XJI2; -.
DR   SMR; B7XJI2; -.
DR   STRING; 481877.B7XJI2; -.
DR   EnsemblFungi; EED43915; EED43915; EBI_25826.
DR   VEuPathDB; MicrosporidiaDB:EBI_25826; -.
DR   HOGENOM; CLU_031506_1_1_1; -.
DR   InParanoid; B7XJI2; -.
DR   Proteomes; UP000001742; Unassembled WGS sequence.
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   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Nuclease; Nucleus; Reference proteome.
FT   CHAIN           1..274
FT                   /note="Putative deoxyribonuclease TATDN1 homolog"
FT                   /id="PRO_0000388426"
FT   BINDING         105
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         139
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         208
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   274 AA;  31862 MW;  95D21E60C8266D4A CRC64;
     MSISYNVFDI AVNPTYYSFE KLKLIVEKAK ELKILPLFIG LDMETNIQVI HLSKMQQTLC
     YCGIHPTHIN TLYKENNIWN ILDIVQADLK QLFVENSEYI IAIGECGLDY YRNQLKIEQQ
     RIFKMQLELS YLNIPYFLHM RNAFDDFYNI IKNYTNVTGV IHSFDGTVDQ ALALINLGFY
     IGINGCSLKN NIDLVKNIPI DKILVETDSP FCLIRKSYAG AEYGKVLKVK ENEPVYILNL
     IEIISNIKQM PIQQLIHQFK LNTIKCFPQL KKFQ