| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| DM42_4667 | WI67_04835 | DM42_4667 | DM42_827 | alkA N-terminal domain protein | Dnaq- exonuclease, DNA polymerase III, epsilon subunit family domain protein | 0.625 |
| DM42_4667 | mutM | DM42_4667 | DM42_2272 | alkA N-terminal domain protein | 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 | 0.589 |
| DM42_4667 | mutY | DM42_4667 | DM42_2273 | alkA N-terminal domain protein | mutY- A/G-specific adenine glycosylase | 0.649 |
| DM42_4667 | nth | DM42_4667 | DM42_2731 | alkA N-terminal domain protein | 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 | 0.669 |
| DM42_4667 | polA | DM42_4667 | DM42_4183 | alkA N-terminal domain protein | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity | 0.842 |
| WI67_04835 | DM42_4667 | DM42_827 | DM42_4667 | Dnaq- exonuclease, DNA polymerase III, epsilon subunit family domain protein | alkA N-terminal domain protein | 0.625 |
| WI67_04835 | dnaN | DM42_827 | DM42_1785 | Dnaq- exonuclease, DNA polymerase III, epsilon subunit family domain protein | Beta sliding clamp; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3’-5’ exonuclease proofreading activity. The beta chain is required for initiation of replication as [...] | 0.963 |
| WI67_04835 | mutL | DM42_827 | DM42_1072 | Dnaq- exonuclease, DNA polymerase III, epsilon subunit family domain protein | DNA mismatch repair protein MutL; This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a "molecular matchmaker", a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex | 0.622 |
| WI67_04835 | mutM | DM42_827 | DM42_2272 | Dnaq- exonuclease, DNA polymerase III, epsilon subunit family domain protein | 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 | 0.623 |
| WI67_04835 | mutY | DM42_827 | DM42_2273 | Dnaq- exonuclease, DNA polymerase III, epsilon subunit family domain protein | mutY- A/G-specific adenine glycosylase | 0.683 |
| WI67_04835 | nth | DM42_827 | DM42_2731 | Dnaq- exonuclease, DNA polymerase III, epsilon subunit family domain protein | 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 | 0.726 |
| WI67_04835 | polA | DM42_827 | DM42_4183 | Dnaq- exonuclease, DNA polymerase III, epsilon subunit family domain protein | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity | 0.968 |
| WI67_04835 | ung | DM42_827 | DM42_1314 | Dnaq- exonuclease, DNA polymerase III, epsilon subunit family domain protein | Uracil-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 | 0.732 |
| WI67_12710 | mutY | DM42_2716 | DM42_2273 | hypoxanDNAglyco- DNA-deoxyinosine glycosylase | mutY- A/G-specific adenine glycosylase | 0.784 |
| WL94_14045 | mutM | DM42_2271 | DM42_2272 | annotation not available | 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 | 0.689 |
| WL94_14045 | mutY | DM42_2271 | DM42_2273 | annotation not available | mutY- A/G-specific adenine glycosylase | 0.694 |
| WL94_14045 | polA | DM42_2271 | DM42_4183 | annotation not available | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity | 0.798 |
| dnaN | WI67_04835 | DM42_1785 | DM42_827 | Beta sliding clamp; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3’-5’ exonuclease proofreading activity. The beta chain is required for initiation of replication as [...] | Dnaq- exonuclease, DNA polymerase III, epsilon subunit family domain protein | 0.963 |
| dnaN | mutL | DM42_1785 | DM42_1072 | Beta sliding clamp; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3’-5’ exonuclease proofreading activity. The beta chain is required for initiation of replication as [...] | DNA mismatch repair protein MutL; This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a "molecular matchmaker", a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex | 0.670 |
| dnaN | mutM | DM42_1785 | DM42_2272 | Beta sliding clamp; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3’-5’ exonuclease proofreading activity. The beta chain is required for initiation of replication as [...] | 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 | 0.625 |
