| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Mettu_0058 | Mettu_1953 | Mettu_0058 | Mettu_1953 | Helicase c2 | DNA polymerase III subunit beta ; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3’ to 5’ exonuclease activity. The beta chain is required for initiation of replication once it is clamped onto DNA, it slides freely (bidirectional and ATP- independent) along duplex DNA | 0.827 |
| Mettu_0058 | Mettu_2187 | Mettu_0058 | Mettu_2187 | Helicase c2 | DNA polymerase I | 0.977 |
| Mettu_0058 | Mettu_2609 | Mettu_0058 | Mettu_2609 | Helicase c2 | Nuclease SbcCD subunit C ; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3’->5’ double strand exonuclease that can open hairpins. It also has a 5’ single-strand endonuclease activity | 0.700 |
| Mettu_0058 | Mettu_2674 | Mettu_0058 | Mettu_2674 | Helicase c2 | ATP-dependent DNA helicase RecQ | 0.760 |
| Mettu_0058 | recA | Mettu_0058 | Mettu_4087 | Helicase c2 | Recombinase A ; Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage | 0.633 |
| Mettu_0058 | sbcD | Mettu_0058 | Mettu_2608 | Helicase c2 | Nuclease SbcCD subunit D ; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3’->5’ double strand exonuclease that can open hairpins. It also has a 5’ single-strand endonuclease activity | 0.626 |
| Mettu_0058 | topA | Mettu_0058 | Mettu_3784 | Helicase c2 | DNA topoisomerase I ; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5’-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3’-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] | 0.599 |
| Mettu_1042 | Mettu_2187 | Mettu_1042 | Mettu_2187 | Single-stranded-DNA-specific exonuclease RecJ | DNA polymerase I | 0.859 |
| Mettu_1042 | Mettu_2609 | Mettu_1042 | Mettu_2609 | Single-stranded-DNA-specific exonuclease RecJ | Nuclease SbcCD subunit C ; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3’->5’ double strand exonuclease that can open hairpins. It also has a 5’ single-strand endonuclease activity | 0.695 |
| Mettu_1042 | Mettu_2674 | Mettu_1042 | Mettu_2674 | Single-stranded-DNA-specific exonuclease RecJ | ATP-dependent DNA helicase RecQ | 0.878 |
| Mettu_1042 | recA | Mettu_1042 | Mettu_4087 | Single-stranded-DNA-specific exonuclease RecJ | Recombinase A ; Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage | 0.836 |
| Mettu_1042 | recB | Mettu_1042 | Mettu_1851 | Single-stranded-DNA-specific exonuclease RecJ | Helicase/nuclease RecBCD subunit RecB ; A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3’ direction. Cuts ssDNA a few nucleotides 3’ to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3’-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and [...] | 0.864 |
| Mettu_1042 | topA | Mettu_1042 | Mettu_3784 | Single-stranded-DNA-specific exonuclease RecJ | DNA topoisomerase I ; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5’-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3’-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] | 0.455 |
| Mettu_1953 | Mettu_0058 | Mettu_1953 | Mettu_0058 | DNA polymerase III subunit beta ; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3’ to 5’ exonuclease activity. The beta chain is required for initiation of replication once it is clamped onto DNA, it slides freely (bidirectional and ATP- independent) along duplex DNA | Helicase c2 | 0.827 |
| Mettu_1953 | Mettu_2187 | Mettu_1953 | Mettu_2187 | DNA polymerase III subunit beta ; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3’ to 5’ exonuclease activity. The beta chain is required for initiation of replication once it is clamped onto DNA, it slides freely (bidirectional and ATP- independent) along duplex DNA | DNA polymerase I | 0.999 |
| Mettu_1953 | Mettu_2609 | Mettu_1953 | Mettu_2609 | DNA polymerase III subunit beta ; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3’ to 5’ exonuclease activity. The beta chain is required for initiation of replication once it is clamped onto DNA, it slides freely (bidirectional and ATP- independent) along duplex DNA | Nuclease SbcCD subunit C ; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3’->5’ double strand exonuclease that can open hairpins. It also has a 5’ single-strand endonuclease activity | 0.710 |
| Mettu_1953 | Mettu_2674 | Mettu_1953 | Mettu_2674 | DNA polymerase III subunit beta ; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3’ to 5’ exonuclease activity. The beta chain is required for initiation of replication once it is clamped onto DNA, it slides freely (bidirectional and ATP- independent) along duplex DNA | ATP-dependent DNA helicase RecQ | 0.639 |
| Mettu_1953 | recA | Mettu_1953 | Mettu_4087 | DNA polymerase III subunit beta ; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3’ to 5’ exonuclease activity. The beta chain is required for initiation of replication once it is clamped onto DNA, it slides freely (bidirectional and ATP- independent) along duplex DNA | Recombinase A ; Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage | 0.956 |
| Mettu_1953 | sbcD | Mettu_1953 | Mettu_2608 | DNA polymerase III subunit beta ; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3’ to 5’ exonuclease activity. The beta chain is required for initiation of replication once it is clamped onto DNA, it slides freely (bidirectional and ATP- independent) along duplex DNA | Nuclease SbcCD subunit D ; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3’->5’ double strand exonuclease that can open hairpins. It also has a 5’ single-strand endonuclease activity | 0.705 |
| Mettu_1953 | smc | Mettu_1953 | Mettu_0837 | DNA polymerase III subunit beta ; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3’ to 5’ exonuclease activity. The beta chain is required for initiation of replication once it is clamped onto DNA, it slides freely (bidirectional and ATP- independent) along duplex DNA | Chromosome partition protein Smc ; Required for chromosome condensation and partitioning | 0.618 |
