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ung protein (Idiomarina loihiensis) - STRING interaction network
"ung" - Uracil-DNA-glycosylase in Idiomarina loihiensis
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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ungUracil-DNA-glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine (216 aa)    
Predicted Functional Partners:
dnaN
DNA polymerase sliding clamp subunit; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3’ to 5’ exonuclease activity. The beta chain is required for initiation of replication once it is clamped onto DNA, it slides freely (bidirectional and ATP- independent) along duplex DNA (367 aa)
     
 
  0.941
ndk
Nucleoside diphosphate kinase; Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate (143 aa)
     
 
  0.824
xthA
Exonuclease III (269 aa)
     
  0.788
polA
DNA polymerase I (921 aa)
   
   
  0.757
mutY
A/G-specific DNA glycosylase (346 aa)
 
 
  0.743
mutS
Mismatch repair ATPase; This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity (843 aa)
     
 
  0.708
thyA
Thymidylate synthase; Provides the sole de novo source of dTMP for DNA biosynthesis (283 aa)
   
 
  0.700
dut
Deoxyuridine 5’-triphosphate nucleotidohydrolase; This enzyme is involved in nucleotide metabolism- it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA (151 aa)
   
 
  0.689
nth
Endonuclease III; DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N- glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3’ to the AP site by a beta-elimination, leaving a 3’-terminal unsaturated sugar and a product with a terminal 5’-phosphate (211 aa)
     
 
  0.657
fpg
Formamidopyrimidine DNA glycosylase; Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3’- and 5’-phosphates (270 aa)
         
  0.610
Your Current Organism:
Idiomarina loihiensis
NCBI taxonomy Id: 283942
Other names: I. loihiensis, I. loihiensis L2TR, Idiomarina loihiensis, Idiomarina loihiensis Donachie et al. 2003, Idiomarina loihiensis L2TR, Idiomarina loihiensis str. L2TR, Idiomarina loihiensis strain L2TR
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