ID   TATD_EDWTE              Reviewed;         260 AA.
AC   D0Z9R0;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=3'-5' ssDNA/RNA exonuclease TatD {ECO:0000255|HAMAP-Rule:MF_00901};
DE            EC=3.1.11.- {ECO:0000255|HAMAP-Rule:MF_00901};
DE            EC=3.1.13.- {ECO:0000255|HAMAP-Rule:MF_00901};
DE   AltName: Full=DNase TatD {ECO:0000255|HAMAP-Rule:MF_00901};
GN   Name=tatD {ECO:0000255|HAMAP-Rule:MF_00901}; OrderedLocusNames=ETAE_0153;
OS   Edwardsiella tarda (strain EIB202).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=498217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EIB202;
RX   PubMed=19865481; DOI=10.1371/journal.pone.0007646;
RA   Wang Q., Yang M., Xiao J., Wu H., Wang X., Lv Y., Xu L., Zheng H., Wang S.,
RA   Zhao G., Liu Q., Zhang Y.;
RT   "Genome sequence of the versatile fish pathogen Edwardsiella tarda provides
RT   insights into its adaptation to broad host ranges and intracellular
RT   niches.";
RL   PLoS ONE 4:E7646-E7646(2009).
CC   -!- FUNCTION: 3'-5' exonuclease that prefers single-stranded DNA and RNA.
CC       May play a role in the H(2)O(2)-induced DNA damage repair.
CC       {ECO:0000255|HAMAP-Rule:MF_00901}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00901};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00901}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00901}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       TatD-type hydrolase family. TatD subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00901}.
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DR   EMBL; CP001135; ACY83000.1; -; Genomic_DNA.
DR   RefSeq; WP_012847033.1; NC_013508.1.
DR   AlphaFoldDB; D0Z9R0; -.
DR   SMR; D0Z9R0; -.
DR   EnsemblBacteria; ACY83000; ACY83000; ETAE_0153.
DR   KEGG; etr:ETAE_0153; -.
DR   HOGENOM; CLU_031506_1_2_6; -.
DR   OMA; PNEAPRI; -.
DR   OrthoDB; 915852at2; -.
DR   Proteomes; UP000002634; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008310; F:single-stranded DNA 3'-5' exodeoxyribonuclease activity; IEA:UniProtKB-UniRule.
DR   CDD; cd01310; TatD_DNAse; 1.
DR   HAMAP; MF_00901; TatD_exonuclease; 1.
DR   InterPro; IPR018228; DNase_TatD-rel_CS.
DR   InterPro; IPR024918; Exonuc_TatD.
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   Cytoplasm; Exonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease.
FT   CHAIN           1..260
FT                   /note="3'-5' ssDNA/RNA exonuclease TatD"
FT                   /id="PRO_0000412735"
FT   BINDING         92
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00901"
FT   BINDING         128
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00901"
FT   BINDING         153
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00901"
SQ   SEQUENCE   260 AA;  28816 MW;  EA76BE5B8D362C43 CRC64;
     MLDIGVNLTN GQFSGDVPQV VARARQAGLN GMIITGTNLT ESAQALHLAQ AYPDFCWATA
     GVHPHDAHRW NENSAADLEP LLRSPAVVAV GECGLDFARN FSTPAQQEAA FEAQLALAAQ
     IGKPVFLHCR EAHARFIALL RPWLSRLPGA VLHCFTGTRD ELDACLSLGL YIGITGWICD
     ERRGMPLRAL LPHIPAERLL LETDAPYLLP RDIQPKPKSR RNEPCFLPHI AEQAARWRQQ
     DANWLKQVTE NNARQLFRLA