ID   TATD_PECPW              Reviewed;         260 AA.
AC   D0KC77;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=Pecwa_4241;
OS   Pectobacterium parmentieri (strain WPP163) (Pectobacterium wasabiae (strain
OS   WPP163)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WPP163;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium wasabiae WPP163.";
RL   Submitted (OCT-2009) 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; CP001790; ACX89965.1; -; Genomic_DNA.
DR   RefSeq; WP_015731429.1; NC_013421.1.
DR   AlphaFoldDB; D0KC77; -.
DR   SMR; D0KC77; -.
DR   KEGG; pwa:Pecwa_4241; -.
DR   eggNOG; COG0084; Bacteria.
DR   HOGENOM; CLU_031506_1_2_6; -.
DR   OMA; NEPCALP; -.
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_0000412749"
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;  28967 MW;  234DC30A27D631E1 CRC64;
     MFDIGVNLTS SQFEQDREQV VIRAKQAGVS GILITGTNAQ ESHQAMLLAQ AYPDYCWSTA
     GVHPHDASQW NGDIAEQVHH MANAACVVAI GECGLDFNRN FSTPEEQERA FSAQLAIAAE
     LSMPVFLHCR DAHPRFISLL TPWLGQLPAA VVHCFTGNRQ ELDACLAVGL TIGITGWVCD
     ERRGLELRAL LPHIPADRLL VETDAPYLLP RDLRPKPASR RNEPCYLPHI IRQIAEWRGE
     DATWLGQITD ENARRIFRLA