| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EEX35899.1 | nfo | VIB_002211 | VIB_001935 | Inosose dehydratase. | Endonuclease IV; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to produce new 5'-ends that are base-free deoxyribose 5-phosphate residues. It preferentially attacks modified AP sites created by bleomycin and neocarzinostatin. | 0.640 |
| EEX36732.1 | nfo | VIB_000838 | VIB_001935 | Superoxide dismutase [Fe]; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. | Endonuclease IV; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to produce new 5'-ends that are base-free deoxyribose 5-phosphate residues. It preferentially attacks modified AP sites created by bleomycin and neocarzinostatin. | 0.545 |
| EEX36850.1 | EEX37325.1 | VIB_000957 | VIB_001445 | Exodeoxyribonuclease III. | DNA polymerase II. | 0.708 |
| EEX36850.1 | EEX37626.1 | VIB_000957 | VIB_001751 | Exodeoxyribonuclease III. | D-glycero-D-manno-heptose 1,7-bisphosphate phosphatase. | 0.547 |
| EEX36850.1 | hisB | VIB_000957 | VIB_001082 | Exodeoxyribonuclease III. | Histidinol-phosphatase/imidazoleglycerol- phosphate dehydratase; In the N-terminal section; belongs to the histidinol- phosphatase family. | 0.701 |
| EEX36850.1 | nfo | VIB_000957 | VIB_001935 | Exodeoxyribonuclease III. | Endonuclease IV; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to produce new 5'-ends that are base-free deoxyribose 5-phosphate residues. It preferentially attacks modified AP sites created by bleomycin and neocarzinostatin. | 0.964 |
| EEX36850.1 | nth | VIB_000957 | VIB_001689 | Exodeoxyribonuclease III. | Predicted EndoIII-related endonuclease; 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. | 0.970 |
| EEX36850.1 | ung | VIB_000957 | VIB_001934 | Exodeoxyribonuclease III. | 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. | 0.793 |
| EEX37325.1 | EEX36850.1 | VIB_001445 | VIB_000957 | DNA polymerase II. | Exodeoxyribonuclease III. | 0.708 |
| EEX37325.1 | dinB | VIB_001445 | VIB_000642 | DNA polymerase II. | DNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. | 0.980 |
| EEX37325.1 | nfo | VIB_001445 | VIB_001935 | DNA polymerase II. | Endonuclease IV; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to produce new 5'-ends that are base-free deoxyribose 5-phosphate residues. It preferentially attacks modified AP sites created by bleomycin and neocarzinostatin. | 0.592 |
| EEX37325.1 | nth | VIB_001445 | VIB_001689 | DNA polymerase II. | Predicted EndoIII-related endonuclease; 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. | 0.413 |
| EEX37626.1 | EEX36850.1 | VIB_001751 | VIB_000957 | D-glycero-D-manno-heptose 1,7-bisphosphate phosphatase. | Exodeoxyribonuclease III. | 0.547 |
| EEX37626.1 | nfo | VIB_001751 | VIB_001935 | D-glycero-D-manno-heptose 1,7-bisphosphate phosphatase. | Endonuclease IV; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to produce new 5'-ends that are base-free deoxyribose 5-phosphate residues. It preferentially attacks modified AP sites created by bleomycin and neocarzinostatin. | 0.497 |
| EEX37805.1 | nfo | VIB_001933 | VIB_001935 | Hypothetical protein. | Endonuclease IV; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to produce new 5'-ends that are base-free deoxyribose 5-phosphate residues. It preferentially attacks modified AP sites created by bleomycin and neocarzinostatin. | 0.466 |
| EEX37805.1 | ung | VIB_001933 | VIB_001934 | Hypothetical 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. | 0.587 |
| dinB | EEX37325.1 | VIB_000642 | VIB_001445 | DNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. | DNA polymerase II. | 0.980 |
| dinB | nfo | VIB_000642 | VIB_001935 | DNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. | Endonuclease IV; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to produce new 5'-ends that are base-free deoxyribose 5-phosphate residues. It preferentially attacks modified AP sites created by bleomycin and neocarzinostatin. | 0.517 |
| dinB | nth | VIB_000642 | VIB_001689 | DNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. | Predicted EndoIII-related endonuclease; 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. | 0.454 |
| hisB | EEX36850.1 | VIB_001082 | VIB_000957 | Histidinol-phosphatase/imidazoleglycerol- phosphate dehydratase; In the N-terminal section; belongs to the histidinol- phosphatase family. | Exodeoxyribonuclease III. | 0.701 |