TATD_PECCP
ID TATD_PECCP Reviewed; 260 AA.
AC C6DI71;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=PC1_4050;
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1;
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., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-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; CP001657; ACT15065.1; -; Genomic_DNA.
DR RefSeq; WP_015842142.1; NC_012917.1.
DR AlphaFoldDB; C6DI71; -.
DR SMR; C6DI71; -.
DR STRING; 561230.PC1_4050; -.
DR EnsemblBacteria; ACT15065; ACT15065; PC1_4050.
DR KEGG; pct:PC1_4050; -.
DR eggNOG; COG0084; Bacteria.
DR HOGENOM; CLU_031506_1_2_6; -.
DR OMA; NEPCALP; -.
DR OrthoDB; 915852at2; -.
DR Proteomes; UP000002736; 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_0000412748"
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; 29170 MW; 4215F0BA5BE62913 CRC64;
MFDIGVNLTS SQFEKDREQV VIRAKQAGVS GILITGTNAQ ESQQAMLLAQ AYPDYCWSTA
GVHPHDASQW NDAVAEQIHH MASADCVVAI GECGLDFNRN FSTPEEQERA FSAQLAIAAE
RSMPVFLHCR DAHSRFISFL TPWLNRLPAA VVHCFTGNRH ELDECLAAGL MVGITGWVCD
ERRGLELRAL LPHIPADRLL VETDAPYLLP RDLRPKPASR RNEPCYLPHI IRQIAEWRGE
DATWLGQTTD ENARRVFRLA