TATD_RAHSY
ID TATD_RAHSY Reviewed; 263 AA.
AC E8XYF5;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 56.
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=Rahaq_4155;
OS Rahnella sp. (strain Y9602).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Rahnella.
OX NCBI_TaxID=2703885;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y9602;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Ovchinnikova G., Pagani I., Sobecky P.A., Martinez R.J.,
RA Woyke T.;
RT "Complete sequence of chromosome of Rahnella sp. Y9602.";
RL Submitted (JAN-2011) 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; CP002505; ADW75743.1; -; Genomic_DNA.
DR RefSeq; WP_013577430.1; NC_015061.1.
DR AlphaFoldDB; E8XYF5; -.
DR SMR; E8XYF5; -.
DR STRING; 741091.Rahaq_4155; -.
DR EnsemblBacteria; ADW75743; ADW75743; Rahaq_4155.
DR KEGG; rah:Rahaq_4155; -.
DR eggNOG; COG0084; Bacteria.
DR HOGENOM; CLU_031506_1_2_6; -.
DR OMA; NEPCALP; -.
DR OrthoDB; 915852at2; -.
DR Proteomes; UP000007257; 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.
FT CHAIN 1..263
FT /note="3'-5' ssDNA/RNA exonuclease TatD"
FT /id="PRO_0000412750"
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 263 AA; 29438 MW; BEF46C8015146AD6 CRC64;
MFEIGINLTS SQFDKDRLQV VERARTAGLS GMLITGTSAQ ESVEAQKMAD EHPDFCWSTA
GVHPHQASHW NAQVEAGIRE LAVLPNVVAI GECGLDFNRN FSPADRQEAA FTAQLALAKE
LQLPVFLHCR DAGERFATLL KPWLSDLPGG VVHCFTGTRQ ELELYLSLGL SIGITGWVCD
ERRGLELRDM LPLIPADRLM LETDAPYLLP RDMENKPKNR RNEPAFLPHI VKQVALWRGE
DPQWLADITD DNARKLFALS ARR