ID   TATD_ERWBE              Reviewed;         261 AA.
AC   D8MKW4;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=EbC_02390;
OS   Erwinia billingiae (strain Eb661).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=634500;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eb661;
RX   PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA   Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA   Knaust F., Geider K., Reinhardt R.;
RT   "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT   tasmaniensis with the pear pathogen E. pyrifoliae.";
RL   BMC Genomics 11:393-393(2010).
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; FP236843; CAX57770.1; -; Genomic_DNA.
DR   RefSeq; WP_013200277.1; NC_014306.1.
DR   AlphaFoldDB; D8MKW4; -.
DR   SMR; D8MKW4; -.
DR   STRING; 634500.EbC_02390; -.
DR   EnsemblBacteria; CAX57770; CAX57770; EbC_02390.
DR   KEGG; ebi:EbC_02390; -.
DR   eggNOG; COG0084; Bacteria.
DR   HOGENOM; CLU_031506_1_2_6; -.
DR   OMA; NEPCALP; -.
DR   OrthoDB; 915852at2; -.
DR   Proteomes; UP000008793; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; Exonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW   Reference proteome.
FT   CHAIN           1..261
FT                   /note="3'-5' ssDNA/RNA exonuclease TatD"
FT                   /id="PRO_0000412740"
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   261 AA;  28754 MW;  9BBFD590B2F768AD CRC64;
     MFDIGVNLTS TQFAKDRDQV VKRAKDAGIT GLLITGTNAL ESQQAQSLAT RRPGYCWSTA
     GVHPHHASEW SGETAATLKR LAESPEVVAI GECGLDFNRN ISEPEQQVYA FNAQLELAAE
     LAMPVFLHCR DAHDRFLAVL TPWLPTLPGA VVHCFTGTRE ELEACLAAGL SIGITGWVCD
     ERRGVELREL MPLIPADRLL LETDAPYLLP RDMRPRPPSR RNEPCFLPHI VQVVAGLRGE
     EPEALGRQCD ANARKLFRLP A