TATD_CITK8
ID TATD_CITK8 Reviewed; 260 AA.
AC A8ACY8;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 72.
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=CKO_00182;
OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=290338;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG The Citrobacter koseri Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (AUG-2007) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABV11351.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000822; ABV11351.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_024130103.1; NC_009792.1.
DR AlphaFoldDB; A8ACY8; -.
DR SMR; A8ACY8; -.
DR STRING; 290338.CKO_00182; -.
DR EnsemblBacteria; ABV11351; ABV11351; CKO_00182.
DR GeneID; 45134473; -.
DR KEGG; cko:CKO_00182; -.
DR HOGENOM; CLU_031506_1_2_6; -.
DR OrthoDB; 915852at2; -.
DR Proteomes; UP000008148; 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;
KW Reference proteome.
FT CHAIN 1..260
FT /note="3'-5' ssDNA/RNA exonuclease TatD"
FT /id="PRO_0000412730"
FT BINDING 91
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00901"
FT BINDING 127
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00901"
FT BINDING 152
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00901"
SQ SEQUENCE 260 AA; 29127 MW; 69B2958565EEF1A4 CRC64;
MFDIGVNLTS SQFVKDRDDV VTRALAAGVS GMLLTGTNLH ESQQAQKLAQ RYACCWSTAG
VHPHDSSQWQ SETEDAIVAL ARQPDVVAIG ECGLDFNRNF STPQEQERAF QAQLRIAAEL
QMPVFMHCRD AHARFLALLE PWLDKLPGAV LHCFTGTREE MQECIDRGLY IGITGWVCDE
RRGLELRELL PFIPAEKLLI ETDAPYLLPR DLTPKPASRR NEPAHLAHIL ARVAHWRGED
PQWLAATTDA NVKTLFGIAF