node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
fliG | fliG_1 | CH64_240 | CH64_1985 | Flagellar motor switch protein FliG; FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. | fliG middle domain protein. | 0.924 |
fliG | xseA | CH64_240 | CH64_1455 | Flagellar motor switch protein FliG; FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. | Exodeoxyribonuclease VII, large subunit; Bidirectionally degrades single-stranded DNA into large acid- insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides; Belongs to the XseA family. | 0.592 |
fliG_1 | fliG | CH64_1985 | CH64_240 | fliG middle domain protein. | Flagellar motor switch protein FliG; FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. | 0.924 |
fliG_1 | xseA | CH64_1985 | CH64_1455 | fliG middle domain protein. | Exodeoxyribonuclease VII, large subunit; Bidirectionally degrades single-stranded DNA into large acid- insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides; Belongs to the XseA family. | 0.592 |
folD | guaB | CH64_3649 | CH64_1454 | Bifunctional protein FolD protein; Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate. | Inosine-5'-monophosphate dehydrogenase; Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Belongs to the IMPDH/GMPR family. | 0.412 |
folD | ispA | CH64_3649 | CH64_3560 | Bifunctional protein FolD protein; Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate. | Polyprenyl synthetase family protein; Belongs to the FPP/GGPP synthase family. | 0.441 |
folD | xseA | CH64_3649 | CH64_1455 | Bifunctional protein FolD protein; Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate. | Exodeoxyribonuclease VII, large subunit; Bidirectionally degrades single-stranded DNA into large acid- insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides; Belongs to the XseA family. | 0.662 |
guaB | folD | CH64_1454 | CH64_3649 | Inosine-5'-monophosphate dehydrogenase; Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Belongs to the IMPDH/GMPR family. | Bifunctional protein FolD protein; Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate. | 0.412 |
guaB | xseA | CH64_1454 | CH64_1455 | Inosine-5'-monophosphate dehydrogenase; Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Belongs to the IMPDH/GMPR family. | Exodeoxyribonuclease VII, large subunit; Bidirectionally degrades single-stranded DNA into large acid- insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides; Belongs to the XseA family. | 0.565 |
ispA | folD | CH64_3560 | CH64_3649 | Polyprenyl synthetase family protein; Belongs to the FPP/GGPP synthase family. | Bifunctional protein FolD protein; Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate. | 0.441 |
ispA | xseA | CH64_3560 | CH64_1455 | Polyprenyl synthetase family protein; Belongs to the FPP/GGPP synthase family. | Exodeoxyribonuclease VII, large subunit; Bidirectionally degrades single-stranded DNA into large acid- insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides; Belongs to the XseA family. | 0.585 |
ispA | xseB | CH64_3560 | CH64_3561 | Polyprenyl synthetase family protein; Belongs to the FPP/GGPP synthase family. | Exodeoxyribonuclease VII, small subunit; Bidirectionally degrades single-stranded DNA into large acid- insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides; Belongs to the XseB family. | 0.927 |
recN | ruvA | CH64_1527 | CH64_404 | DNA repair protein RecN; May be involved in recombinational repair of damaged DNA. | 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. | 0.613 |
recN | uvrB | CH64_1527 | CH64_3831 | DNA repair protein RecN; May be involved in recombinational repair of damaged DNA. | Excinuclease ABC 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 dissociate [...] | 0.536 |
recN | uvrC | CH64_1527 | CH64_281 | DNA repair protein RecN; May be involved in recombinational repair of damaged DNA. | 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. | 0.667 |
recN | xseA | CH64_1527 | CH64_1455 | DNA repair protein RecN; May be involved in recombinational repair of damaged DNA. | Exodeoxyribonuclease VII, large subunit; Bidirectionally degrades single-stranded DNA into large acid- insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides; Belongs to the XseA family. | 0.670 |
recN | xseB | CH64_1527 | CH64_3561 | DNA repair protein RecN; May be involved in recombinational repair of damaged DNA. | Exodeoxyribonuclease VII, small subunit; Bidirectionally degrades single-stranded DNA into large acid- insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides; Belongs to the XseB family. | 0.407 |
ruvA | recN | CH64_404 | CH64_1527 | 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. | DNA repair protein RecN; May be involved in recombinational repair of damaged DNA. | 0.613 |
ruvA | uvrB | CH64_404 | CH64_3831 | 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. | Excinuclease ABC 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 dissociate [...] | 0.542 |
ruvA | uvrC | CH64_404 | CH64_281 | 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. | 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. | 0.560 |