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mugUracil-DNA glycosylase superfamily; Excises ethenocytosine and uracil, which can arise by alkylation or deamination of cytosine, respectively, from the corresponding mispairs with guanine in ds-DNA. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and the mispaired base. The complementary strand guanine functions in substrate recognition. Required for DNA damage lesion repair in stationary-phase cells; Belongs to the uracil-DNA glycosylase (UDG) superfamily. TDG/mug family. (168 aa)    
Predicted Functional Partners:
ADO48838.1
Manually curated; TIGRFAM: exodeoxyribonuclease III; exodeoxyribonuclease III Xth; KEGG: efe:EFER_1316 exonuclease III; PFAM: Endonuclease/exonuclease/phosphatase.
    
 0.440
ADO46734.1
TIGRFAM: diguanylate cyclase; PFAM: GGDEF domain containing protein; EAL domain protein; KEGG: kva:Kvar_0439 diguanylate cyclase/phosphodiesterase; SMART: EAL domain protein; GGDEF domain containing protein.
  
     0.428
Your Current Organism:
Enterobacter lignolyticus
NCBI taxonomy Id: 701347
Other names: Enterobacter lignolyticus SCF1, [. lignolyticus SCF1, [Enterobacter] lignolyticus SCF1
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