TATD_ERWAE
ID TATD_ERWAE Reviewed; 259 AA.
AC D4ICL5;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 52.
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=EAM_0208;
OS Erwinia amylovora (strain ATCC 49946 / CCPPB 0273 / Ea273 / 27-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=716540;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49946 / CCPPB 0273 / Ea273 / 27-3;
RX PubMed=20118253; DOI=10.1128/jb.00022-10;
RA Sebaihia M., Bocsanczy A.M., Biehl B.S., Quail M.A., Perna N.T.,
RA Glasner J.D., DeClerck G.A., Cartinhour S., Schneider D.J., Bentley S.D.,
RA Parkhill J., Beer S.V.;
RT "Complete genome sequence of the plant pathogen Erwinia amylovora strain
RT ATCC 49946.";
RL J. Bacteriol. 192:2020-2021(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; FN666575; CBJ44883.1; -; Genomic_DNA.
DR RefSeq; WP_004154961.1; NC_013971.1.
DR AlphaFoldDB; D4ICL5; -.
DR SMR; D4ICL5; -.
DR PRIDE; D4ICL5; -.
DR GeneID; 8914066; -.
DR KEGG; eay:EAM_0208; -.
DR HOGENOM; CLU_031506_1_2_6; -.
DR OMA; PNEAPRI; -.
DR BioCyc; EAMY716540:EAM_RS01095-MON; -.
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..259
FT /note="3'-5' ssDNA/RNA exonuclease TatD"
FT /id="PRO_0000412739"
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 259 AA; 28691 MW; 3A506E2B805AA52C CRC64;
MFDIGVNLTS TQFAKDRDKV VKRAREAGIS GMLITGTNAL ESQQALSLAR QHANYCWSTA
GVHPHHASEW SAETAATLRR LAESPLVVAI GECGLDFNRN FSQPEQQVYA FNAQLALAAE
LSLPVFLHCR EAHERFITIL KPWLPSLKAA VLHCFTGARA ELESCLAEGL SIGITGWICD
ERRGQELREL VPLIPADRLL LETDAPWLLP RDMRPRPPSR RNEPCFLPHI VQQVALLRGD
DVDELAAQTA LNARALFGL
