| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| BARCL_0367 | BARCL_0368 | BARCL_0367 | BARCL_0368 | Homologs of previously reported genes of unknown function. | Homologs of previously reported genes of unknown function. | 0.691 |
| BARCL_0367 | mutY | BARCL_0367 | BARCL_0366 | Homologs of previously reported genes of unknown function. | A/G-specific adenine glycosylase MutY; Adenine glycosylase active on G-A mispairs. | 0.621 |
| BARCL_0368 | BARCL_0367 | BARCL_0368 | BARCL_0367 | Homologs of previously reported genes of unknown function. | Homologs of previously reported genes of unknown function. | 0.691 |
| BARCL_0368 | mutY | BARCL_0368 | BARCL_0366 | Homologs of previously reported genes of unknown function. | A/G-specific adenine glycosylase MutY; Adenine glycosylase active on G-A mispairs. | 0.524 |
| BARCL_0368 | polA | BARCL_0368 | BARCL_0007 | Homologs of previously reported genes of unknown function. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.550 |
| BARCL_0397 | mutM | BARCL_0397 | BARCL_0191 | Methyltranferase. | 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. | 0.507 |
| BARCL_0397 | mutY | BARCL_0397 | BARCL_0366 | Methyltranferase. | A/G-specific adenine glycosylase MutY; Adenine glycosylase active on G-A mispairs. | 0.597 |
| BARCL_0397 | polA | BARCL_0397 | BARCL_0007 | Methyltranferase. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.751 |
| BARCL_0397 | ruvA | BARCL_0397 | BARCL_1231 | Methyltranferase. | Holliday junction ATP-dependent DNA helicase ruvA; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB. | 0.494 |
| BARCL_0397 | xthA | BARCL_0397 | BARCL_0943 | Methyltranferase. | Exodeoxyribonuclease III. | 0.599 |
| BARCL_0397 | xthA-2 | BARCL_0397 | BARCL_1292 | Methyltranferase. | Exodeoxyribonuclease III. | 0.599 |
| dnaN | mutY | BARCL_0132 | BARCL_0366 | DNA polymerase III, beta chain; 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 r [...] | A/G-specific adenine glycosylase MutY; Adenine glycosylase active on G-A mispairs. | 0.795 |
| dnaN | polA | BARCL_0132 | BARCL_0007 | DNA polymerase III, beta chain; 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 r [...] | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.994 |
| dnaN | secD | BARCL_0132 | BARCL_0578 | DNA polymerase III, beta chain; 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 r [...] | Protein-export membrane protein; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA; Belongs to the SecD/SecF family. SecD subfamily. | 0.561 |
| dnaN | xthA | BARCL_0132 | BARCL_0943 | DNA polymerase III, beta chain; 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 r [...] | Exodeoxyribonuclease III. | 0.832 |
| dnaN | xthA-2 | BARCL_0132 | BARCL_1292 | DNA polymerase III, beta chain; 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 r [...] | Exodeoxyribonuclease III. | 0.832 |
| mutM | BARCL_0397 | BARCL_0191 | BARCL_0397 | 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. | Methyltranferase. | 0.507 |
| mutM | mutY | BARCL_0191 | BARCL_0366 | 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 MutY; Adenine glycosylase active on G-A mispairs. | 0.537 |
| mutM | polA | BARCL_0191 | BARCL_0007 | 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 I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.826 |
| mutM | ruvA | BARCL_0191 | BARCL_1231 | 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. | Holliday junction ATP-dependent DNA helicase ruvA; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB. | 0.617 |