node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
A0A0L8G0J7 | A0A0L8GJF6 | A0A0L8G0J7 | A0A0L8GJF6 | DNA mismatch repair protein; Component of the post-replicative DNA mismatch repair system (MMR). | DNA-(apurinic or apyrimidinic site) lyase; Belongs to the DNA repair enzymes AP/ExoA family. | 0.606 |
A0A0L8G0J7 | A0A0L8GLQ9 | A0A0L8G0J7 | A0A0L8GLQ9 | DNA mismatch repair protein; Component of the post-replicative DNA mismatch repair system (MMR). | DNA-(apurinic or apyrimidinic site) lyase; Belongs to the DNA repair enzymes AP/ExoA family. | 0.428 |
A0A0L8G0J7 | A0A0L8HN68 | A0A0L8G0J7 | A0A0L8HN68 | DNA mismatch repair protein; Component of the post-replicative DNA mismatch repair system (MMR). | ENDO3c domain-containing protein. | 0.775 |
A0A0L8G0J7 | A0A0L8I334 | A0A0L8G0J7 | A0A0L8I334 | DNA mismatch repair protein; Component of the post-replicative DNA mismatch repair system (MMR). | UmuC domain-containing protein. | 0.632 |
A0A0L8G0J7 | NTH1 | A0A0L8G0J7 | A0A0L8HSE5 | DNA mismatch repair protein; Component of the post-replicative DNA mismatch repair system (MMR). | Endonuclease III homolog; Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines; Belongs to the Nth/MutY family. | 0.587 |
A0A0L8G4B4 | A0A0L8HN68 | A0A0L8G4B4 | A0A0L8HN68 | Uncharacterized protein. | ENDO3c domain-containing protein. | 0.898 |
A0A0L8GJF6 | A0A0L8G0J7 | A0A0L8GJF6 | A0A0L8G0J7 | DNA-(apurinic or apyrimidinic site) lyase; Belongs to the DNA repair enzymes AP/ExoA family. | DNA mismatch repair protein; Component of the post-replicative DNA mismatch repair system (MMR). | 0.606 |
A0A0L8GJF6 | A0A0L8GLQ9 | A0A0L8GJF6 | A0A0L8GLQ9 | DNA-(apurinic or apyrimidinic site) lyase; Belongs to the DNA repair enzymes AP/ExoA family. | DNA-(apurinic or apyrimidinic site) lyase; Belongs to the DNA repair enzymes AP/ExoA family. | 0.918 |
A0A0L8GJF6 | A0A0L8HN68 | A0A0L8GJF6 | A0A0L8HN68 | DNA-(apurinic or apyrimidinic site) lyase; Belongs to the DNA repair enzymes AP/ExoA family. | ENDO3c domain-containing protein. | 0.894 |
A0A0L8GJF6 | A0A0L8I334 | A0A0L8GJF6 | A0A0L8I334 | DNA-(apurinic or apyrimidinic site) lyase; Belongs to the DNA repair enzymes AP/ExoA family. | UmuC domain-containing protein. | 0.722 |
A0A0L8GJF6 | NTH1 | A0A0L8GJF6 | A0A0L8HSE5 | DNA-(apurinic or apyrimidinic site) lyase; Belongs to the DNA repair enzymes AP/ExoA family. | Endonuclease III homolog; Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines; Belongs to the Nth/MutY family. | 0.933 |
A0A0L8GLQ9 | A0A0L8G0J7 | A0A0L8GLQ9 | A0A0L8G0J7 | DNA-(apurinic or apyrimidinic site) lyase; Belongs to the DNA repair enzymes AP/ExoA family. | DNA mismatch repair protein; Component of the post-replicative DNA mismatch repair system (MMR). | 0.428 |
A0A0L8GLQ9 | A0A0L8GJF6 | A0A0L8GLQ9 | A0A0L8GJF6 | DNA-(apurinic or apyrimidinic site) lyase; Belongs to the DNA repair enzymes AP/ExoA family. | DNA-(apurinic or apyrimidinic site) lyase; Belongs to the DNA repair enzymes AP/ExoA family. | 0.918 |
A0A0L8GLQ9 | A0A0L8HN68 | A0A0L8GLQ9 | A0A0L8HN68 | DNA-(apurinic or apyrimidinic site) lyase; Belongs to the DNA repair enzymes AP/ExoA family. | ENDO3c domain-containing protein. | 0.774 |
A0A0L8GLQ9 | A0A0L8I334 | A0A0L8GLQ9 | A0A0L8I334 | DNA-(apurinic or apyrimidinic site) lyase; Belongs to the DNA repair enzymes AP/ExoA family. | UmuC domain-containing protein. | 0.405 |
A0A0L8GLQ9 | NTH1 | A0A0L8GLQ9 | A0A0L8HSE5 | DNA-(apurinic or apyrimidinic site) lyase; Belongs to the DNA repair enzymes AP/ExoA family. | Endonuclease III homolog; Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines; Belongs to the Nth/MutY family. | 0.885 |
A0A0L8GWV9 | A0A0L8HEY5 | A0A0L8GWV9 | A0A0L8HEY5 | 5_nucleotid_C domain-containing protein; Belongs to the 5'-nucleotidase family. | Uncharacterized protein; Belongs to the 5'-nucleotidase family. | 0.912 |
A0A0L8GWV9 | A0A0L8HM87 | A0A0L8GWV9 | A0A0L8HM87 | 5_nucleotid_C domain-containing protein; Belongs to the 5'-nucleotidase family. | Purine nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. | 0.965 |
A0A0L8GWV9 | A0A0L8HN68 | A0A0L8GWV9 | A0A0L8HN68 | 5_nucleotid_C domain-containing protein; Belongs to the 5'-nucleotidase family. | ENDO3c domain-containing protein. | 0.791 |
A0A0L8GWV9 | A0A0L8IBL0 | A0A0L8GWV9 | A0A0L8IBL0 | 5_nucleotid_C domain-containing protein; Belongs to the 5'-nucleotidase family. | S-methyl-5'-thioadenosine phosphorylase; Catalyzes the reversible phosphorylation of S-methyl-5'- thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates. | 0.663 |