| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| BF49_0231 | BF49_3732 | BF49_0231 | BF49_3732 | Cell division protein FtsK. | Mobile element protein. | 0.453 |
| BF49_0231 | priA | BF49_0231 | BF49_0414 | Cell division protein FtsK. | Helicase PriA essential for oriCDnaAindependent DNA replication; Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA; Belongs to the helicase family. PriA subfamily. | 0.424 |
| BF49_0231 | ruvA | BF49_0231 | BF49_4317 | Cell division protein FtsK. | Holliday junction 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. | 0.645 |
| BF49_0231 | ruvB | BF49_0231 | BF49_4319 | Cell division protein FtsK. | Holliday junction DNA helicase RuvB; 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. | 0.580 |
| BF49_0231 | ruvC | BF49_0231 | BF49_4316 | Cell division protein FtsK. | Crossover junction endodeoxyribonuclease RuvC EC 31224; Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group. | 0.443 |
| BF49_0231 | xerC | BF49_0231 | BF49_0413 | Cell division protein FtsK. | Tyrosine recombinase XerC; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | 0.635 |
| BF49_0231 | xerD | BF49_0231 | BF49_0590 | Cell division protein FtsK. | Tyrosine recombinase XerD; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | 0.635 |
| BF49_0412 | priA | BF49_0412 | BF49_0414 | FIG00441012 hypothetical protein. | Helicase PriA essential for oriCDnaAindependent DNA replication; Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA; Belongs to the helicase family. PriA subfamily. | 0.460 |
| BF49_0412 | xerC | BF49_0412 | BF49_0413 | FIG00441012 hypothetical protein. | Tyrosine recombinase XerC; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | 0.696 |
| BF49_0571 | BF49_3732 | BF49_0571 | BF49_3732 | Competence protein F homolog phosphoribosyltransferase domain protein YhgH required for utilization of DNA as sole source of carbon and energy. | Mobile element protein. | 0.568 |
| BF49_0571 | BF49_4716 | BF49_0571 | BF49_4716 | Competence protein F homolog phosphoribosyltransferase domain protein YhgH required for utilization of DNA as sole source of carbon and energy. | Integraserecombinase; Belongs to the 'phage' integrase family. | 0.568 |
| BF49_0571 | priA | BF49_0571 | BF49_0414 | Competence protein F homolog phosphoribosyltransferase domain protein YhgH required for utilization of DNA as sole source of carbon and energy. | Helicase PriA essential for oriCDnaAindependent DNA replication; Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA; Belongs to the helicase family. PriA subfamily. | 0.604 |
| BF49_0571 | ruvA | BF49_0571 | BF49_4317 | Competence protein F homolog phosphoribosyltransferase domain protein YhgH required for utilization of DNA as sole source of carbon and energy. | Holliday junction 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. | 0.460 |
| BF49_0571 | xerC | BF49_0571 | BF49_0413 | Competence protein F homolog phosphoribosyltransferase domain protein YhgH required for utilization of DNA as sole source of carbon and energy. | Tyrosine recombinase XerC; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | 0.617 |
| BF49_0571 | xerD | BF49_0571 | BF49_0590 | Competence protein F homolog phosphoribosyltransferase domain protein YhgH required for utilization of DNA as sole source of carbon and energy. | Tyrosine recombinase XerD; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | 0.627 |
| BF49_3732 | BF49_0231 | BF49_3732 | BF49_0231 | Mobile element protein. | Cell division protein FtsK. | 0.453 |
| BF49_3732 | BF49_0571 | BF49_3732 | BF49_0571 | Mobile element protein. | Competence protein F homolog phosphoribosyltransferase domain protein YhgH required for utilization of DNA as sole source of carbon and energy. | 0.568 |
| BF49_3732 | BF49_4716 | BF49_3732 | BF49_4716 | Mobile element protein. | Integraserecombinase; Belongs to the 'phage' integrase family. | 0.677 |
| BF49_3732 | ruvA | BF49_3732 | BF49_4317 | Mobile element protein. | Holliday junction 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. | 0.688 |
| BF49_3732 | ruvB | BF49_3732 | BF49_4319 | Mobile element protein. | Holliday junction DNA helicase RuvB; 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. | 0.697 |