(data stored in ACNUC7421 zone)

SWISSPROT: C5BCB0_EDWI9

ID   C5BCB0_EDWI9            Unreviewed;       260 AA.
AC   C5BCB0;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   30-AUG-2017, entry version 51.
DE   RecName: Full=3'-5' ssDNA/RNA exonuclease TatD {ECO:0000256|HAMAP-Rule:MF_00901};
DE            EC=3.1.11.- {ECO:0000256|HAMAP-Rule:MF_00901};
DE            EC=3.1.13.- {ECO:0000256|HAMAP-Rule:MF_00901};
DE   AltName: Full=DNase TatD {ECO:0000256|HAMAP-Rule:MF_00901};
GN   Name=tatD {ECO:0000256|HAMAP-Rule:MF_00901};
GN   OrderedLocusNames=NT01EI_0146 {ECO:0000313|EMBL:ACR67401.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67401.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: 3'-5' exonuclease that prefers single-stranded DNA and
CC       RNA. May play a role in the H(2)O(2)-induced DNA damage repair.
CC       {ECO:0000256|HAMAP-Rule:MF_00901}.
CC   -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in the 3'- to 5'-
CC       direction to yield nucleoside 5'-phosphates. {ECO:0000256|HAMAP-
CC       Rule:MF_00901}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00901};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00901}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00901}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. TatD-type hydrolase family. TatD subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00901}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001600; ACR67401.1; -; Genomic_DNA.
DR   RefSeq; WP_015869617.1; NC_012779.2.
DR   ProteinModelPortal; C5BCB0; -.
DR   STRING; 634503.NT01EI_0146; -.
DR   EnsemblBacteria; ACR67401; ACR67401; NT01EI_0146.
DR   GeneID; 7958746; -.
DR   KEGG; eic:NT01EI_0146; -.
DR   PATRIC; fig|634503.3.peg.137; -.
DR   eggNOG; ENOG4105F8V; Bacteria.
DR   eggNOG; COG0084; LUCA.
DR   HOGENOM; HOG000201523; -.
DR   KO; K03424; -.
DR   OMA; SPYLTPH; -.
DR   OrthoDB; POG091H012B; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016888; F:endodeoxyribonuclease activity, producing 5'-phosphomonoesters; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008310; F:single-stranded DNA 3'-5' exodeoxyribonuclease activity; IEA:UniProtKB-HAMAP.
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_family.
DR   PANTHER; PTHR10060; PTHR10060; 1.
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;
DR   PRODOM; C5BCB0.
DR   SWISS-2DPAGE; C5BCB0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00901};
KW   Exonuclease {ECO:0000256|HAMAP-Rule:MF_00901};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00901,
KW   ECO:0000313|EMBL:ACR67401.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00901};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00901};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_00901};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485}.
FT   METAL        92     92       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_00901}.
FT   METAL       128    128       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_00901}.
FT   METAL       153    153       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_00901}.
SQ   SEQUENCE   260 AA;  28839 MW;  4DC99C472271F3EB CRC64;
     MLDIGVNLTN SQFAGDVPQV IARARQAGLN GMIITGTNLT ESAQALCLAQ AYPDFCWATA
     GVHPHDAHRW NENSTAALEP LLHSPTVVAV GECGLDFARN FSTPAQQEAA FEAQLTLAAR
     IGKPVFLHCR EAHARFIALL RPWLSSLPGA VLHCFTGTRD ELDACLSLGL YIGITGWICD
     ERRGMPQRAL LPHIPAERLL LETDAPYLLP RNIQPKPKSR RNEPCFLPHI AEQVARWRQQ
     DASWLRQVTE NNARQLFRLA
//

If you have problems or comments...

PBIL Back to PBIL home page