| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CMS0227 | CMS2872 | CMS0227 | CMS2872 | Putative exonuclease. | Putative nuclease. | 0.976 |
| CMS0227 | mutY | CMS0227 | CMS1841 | Putative exonuclease. | A/G-specific adenine glycosylase. | 0.605 |
| CMS1839 | mutY | CMS1839 | CMS1841 | Putative oxidoreductase; Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid. | A/G-specific adenine glycosylase. | 0.583 |
| CMS1840 | mutY | CMS1840 | CMS1841 | Hypothetical protein. | A/G-specific adenine glycosylase. | 0.569 |
| CMS2872 | CMS0227 | CMS2872 | CMS0227 | Putative nuclease. | Putative exonuclease. | 0.976 |
| CMS2872 | mutY | CMS2872 | CMS1841 | Putative nuclease. | A/G-specific adenine glycosylase. | 0.605 |
| dinB | mutM | CMS1522 | CMS0747 | 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. | 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. | 0.508 |
| dinB | mutY | CMS1522 | CMS1841 | 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. | A/G-specific adenine glycosylase. | 0.484 |
| dinB | uvrB | CMS1522 | CMS1994 | 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. | ABC excision nuclease subunit B; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissoc [...] | 0.677 |
| hemN | mutY | CMS1742 | CMS1841 | Putative oxygen-independent coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | A/G-specific adenine glycosylase. | 0.509 |
| mutM | dinB | CMS0747 | CMS1522 | 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. | 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. | 0.508 |
| mutM | mutY | CMS0747 | CMS1841 | 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. | A/G-specific adenine glycosylase. | 0.715 |
| mutM | recO | CMS0747 | CMS1725 | 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. | DNA repair protein RecO; Involved in DNA repair and RecF pathway recombination. | 0.654 |
| mutM | uvrB | CMS0747 | CMS1994 | 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. | ABC excision nuclease subunit B; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissoc [...] | 0.663 |
| mutY | CMS0227 | CMS1841 | CMS0227 | A/G-specific adenine glycosylase. | Putative exonuclease. | 0.605 |
| mutY | CMS1839 | CMS1841 | CMS1839 | A/G-specific adenine glycosylase. | Putative oxidoreductase; Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid. | 0.583 |
| mutY | CMS1840 | CMS1841 | CMS1840 | A/G-specific adenine glycosylase. | Hypothetical protein. | 0.569 |
| mutY | CMS2872 | CMS1841 | CMS2872 | A/G-specific adenine glycosylase. | Putative nuclease. | 0.605 |
| mutY | dinB | CMS1841 | CMS1522 | A/G-specific adenine glycosylase. | 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. | 0.484 |
| mutY | hemN | CMS1841 | CMS1742 | A/G-specific adenine glycosylase. | Putative oxygen-independent coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.509 |