ID   TATD_PANSA              Reviewed;         260 AA.
AC   E6WHK1;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   03-AUG-2022, entry version 58.
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=Pat9b_0188;
OS   Pantoea sp. (strain At-9b).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea; unclassified Pantoea.
OX   NCBI_TaxID=592316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=At-9b;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pinto A., Currie C., Woyke T.;
RT   "Complete sequence chromosome of Pantoea sp. At-9b.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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; CP002433; ADU67514.1; -; Genomic_DNA.
DR   RefSeq; WP_013507383.1; NC_014837.1.
DR   AlphaFoldDB; E6WHK1; -.
DR   SMR; E6WHK1; -.
DR   STRING; 592316.Pat9b_0188; -.
DR   EnsemblBacteria; ADU67514; ADU67514; Pat9b_0188.
DR   KEGG; pao:Pat9b_0188; -.
DR   eggNOG; COG0084; Bacteria.
DR   HOGENOM; CLU_031506_1_2_6; -.
DR   OMA; NEPCALP; -.
DR   OrthoDB; 915852at2; -.
DR   Proteomes; UP000001624; 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; PS01090; TATD_2; 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_0000412746"
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;  29113 MW;  E9ADE5CF171E2E83 CRC64;
     MFDIGVNLTS TQFAKDREQV VARARDAGVT GLLITGTNAL ESQQAQRLAE WHPGYCWSTA
     GVHPHHASAW SAETANTLRR LAESEQVVAI GECGLDFNRN FSAHDQQEYA FDAQLQLAAE
     LQLPVFLHCR EAHDRFAAIL QPWLPKLVGA VAHCFTGTRE ELEACLAMGL SIGITGWVCD
     ERRGMELREL LPLIPAERLL LETDAPWLLP RDMHPRPTSR RNEPCFLPHI VQQVALWRNE
     AAETLGAQVD HNARQLFRLA