| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| FMG_0374 | FMG_0376 | FMG_0374 | FMG_0376 | Putative X-prolyl aminopeptidase. | Conserved hypothetical protein. | 0.651 |
| FMG_0374 | thiE-2 | FMG_0374 | FMG_0378 | Putative X-prolyl aminopeptidase. | Thiamine-phosphate pyrophosphorylase; Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). Belongs to the thiamine-phosphate synthase family. | 0.652 |
| FMG_0374 | thiM | FMG_0374 | FMG_0377 | Putative X-prolyl aminopeptidase. | Hydroxyethylthiazole kinase; Catalyzes the phosphorylation of the hydroxyl group of 4- methyl-5-beta-hydroxyethylthiazole (THZ); Belongs to the Thz kinase family. | 0.651 |
| FMG_0374 | uvrC | FMG_0374 | FMG_0375 | Putative X-prolyl aminopeptidase. | Excinuclease ABC subunit C; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. | 0.814 |
| FMG_0376 | FMG_0374 | FMG_0376 | FMG_0374 | Conserved hypothetical protein. | Putative X-prolyl aminopeptidase. | 0.651 |
| FMG_0376 | thiE-2 | FMG_0376 | FMG_0378 | Conserved hypothetical protein. | Thiamine-phosphate pyrophosphorylase; Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). Belongs to the thiamine-phosphate synthase family. | 0.876 |
| FMG_0376 | thiM | FMG_0376 | FMG_0377 | Conserved hypothetical protein. | Hydroxyethylthiazole kinase; Catalyzes the phosphorylation of the hydroxyl group of 4- methyl-5-beta-hydroxyethylthiazole (THZ); Belongs to the Thz kinase family. | 0.914 |
| FMG_0376 | uvrC | FMG_0376 | FMG_0375 | Conserved hypothetical protein. | Excinuclease ABC subunit C; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. | 0.651 |
| FMG_0568 | FMG_0647 | FMG_0568 | FMG_0647 | ATP-dependent DNA helicase. | DNA helicase II. | 0.927 |
| FMG_0568 | radA | FMG_0568 | FMG_0336 | ATP-dependent DNA helicase. | DNA repair protein; DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function. | 0.621 |
| FMG_0568 | uvrA | FMG_0568 | FMG_0900 | ATP-dependent DNA helicase. | Excinuclease ABC subunit A; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate. | 0.500 |
| FMG_0568 | uvrB | FMG_0568 | FMG_0901 | ATP-dependent DNA helicase. | UvrABC system protein 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 dissociate and [...] | 0.603 |
| FMG_0568 | uvrC | FMG_0568 | FMG_0375 | ATP-dependent DNA helicase. | Excinuclease ABC subunit C; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. | 0.790 |
| FMG_0647 | FMG_0568 | FMG_0647 | FMG_0568 | DNA helicase II. | ATP-dependent DNA helicase. | 0.927 |
| FMG_0647 | radA | FMG_0647 | FMG_0336 | DNA helicase II. | DNA repair protein; DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function. | 0.617 |
| FMG_0647 | uvrC | FMG_0647 | FMG_0375 | DNA helicase II. | Excinuclease ABC subunit C; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. | 0.668 |
| radA | FMG_0568 | FMG_0336 | FMG_0568 | DNA repair protein; DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function. | ATP-dependent DNA helicase. | 0.621 |
| radA | FMG_0647 | FMG_0336 | FMG_0647 | DNA repair protein; DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function. | DNA helicase II. | 0.617 |
| radA | ruvA | FMG_0336 | FMG_0816 | DNA repair protein; DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function. | Holliday junction DNA helicase; 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. | 0.421 |
| radA | uvrB | FMG_0336 | FMG_0901 | DNA repair protein; DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function. | UvrABC system protein 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 dissociate and [...] | 0.455 |