node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
cho | mutS | b1741 | b2733 | Endonuclease of nucleotide excision repair; Incises the DNA at the 3' side of a lesion during nucleotide excision repair. Incises the DNA farther away from the lesion than UvrC. Not able to incise the 5' site of a lesion. In vitro, the incision activity of Cho is UvrA and UvrB dependent. When a lesion remains because UvrC is not able to induce the 3' incision, Cho incises the DNA. Then UvrC makes the 5' incision. The combined action of Cho and UvrC broadens the substrate range of nucleotide excision repair. | Methyl-directed mismatch repair protein; This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity. | 0.755 |
cho | nadE | b1741 | b1740 | Endonuclease of nucleotide excision repair; Incises the DNA at the 3' side of a lesion during nucleotide excision repair. Incises the DNA farther away from the lesion than UvrC. Not able to incise the 5' site of a lesion. In vitro, the incision activity of Cho is UvrA and UvrB dependent. When a lesion remains because UvrC is not able to induce the 3' incision, Cho incises the DNA. Then UvrC makes the 5' incision. The combined action of Cho and UvrC broadens the substrate range of nucleotide excision repair. | NAD synthetase, NH3/glutamine-dependent; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. | 0.802 |
cho | ruvA | b1741 | b1861 | Endonuclease of nucleotide excision repair; Incises the DNA at the 3' side of a lesion during nucleotide excision repair. Incises the DNA farther away from the lesion than UvrC. Not able to incise the 5' site of a lesion. In vitro, the incision activity of Cho is UvrA and UvrB dependent. When a lesion remains because UvrC is not able to induce the 3' incision, Cho incises the DNA. Then UvrC makes the 5' incision. The combined action of Cho and UvrC broadens the substrate range of nucleotide excision repair. | Component of RuvABC resolvasome, regulatory subunit; 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. Binds both single- and double-stranded DNA (dsDNA). Binds preferentially to supercoiled rather than to relaxed dsDNA. | 0.664 |
cho | ruvB | b1741 | b1860 | Endonuclease of nucleotide excision repair; Incises the DNA at the 3' side of a lesion during nucleotide excision repair. Incises the DNA farther away from the lesion than UvrC. Not able to incise the 5' site of a lesion. In vitro, the incision activity of Cho is UvrA and UvrB dependent. When a lesion remains because UvrC is not able to induce the 3' incision, Cho incises the DNA. Then UvrC makes the 5' incision. The combined action of Cho and UvrC broadens the substrate range of nucleotide excision repair. | ATP-dependent DNA helicase, component of RuvABC resolvasome; 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. Belongs to the RuvB family. | 0.693 |
cho | sbcD | b1741 | b0398 | Endonuclease of nucleotide excision repair; Incises the DNA at the 3' side of a lesion during nucleotide excision repair. Incises the DNA farther away from the lesion than UvrC. Not able to incise the 5' site of a lesion. In vitro, the incision activity of Cho is UvrA and UvrB dependent. When a lesion remains because UvrC is not able to induce the 3' incision, Cho incises the DNA. Then UvrC makes the 5' incision. The combined action of Cho and UvrC broadens the substrate range of nucleotide excision repair. | Exonuclease, dsDNA, ATP-dependent; 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; Belongs to the SbcD family. | 0.675 |
cho | uvrA | b1741 | b4058 | Endonuclease of nucleotide excision repair; Incises the DNA at the 3' side of a lesion during nucleotide excision repair. Incises the DNA farther away from the lesion than UvrC. Not able to incise the 5' site of a lesion. In vitro, the incision activity of Cho is UvrA and UvrB dependent. When a lesion remains because UvrC is not able to induce the 3' incision, Cho incises the DNA. Then UvrC makes the 5' incision. The combined action of Cho and UvrC broadens the substrate range of nucleotide excision repair. | ATPase and DNA damage recognition protein of nucleotide excision repair excinuclease UvrABC; 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. | 0.939 |
cho | uvrB | b1741 | b0779 | Endonuclease of nucleotide excision repair; Incises the DNA at the 3' side of a lesion during nucleotide excision repair. Incises the DNA farther away from the lesion than UvrC. Not able to incise the 5' site of a lesion. In vitro, the incision activity of Cho is UvrA and UvrB dependent. When a lesion remains because UvrC is not able to induce the 3' incision, Cho incises the DNA. Then UvrC makes the 5' incision. The combined action of Cho and UvrC broadens the substrate range of nucleotide excision repair. | Exision nuclease of nucleotide excision repair, DNA damage recognition component; 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 lesi [...] | 0.977 |
cho | uvrC | b1741 | b1913 | Endonuclease of nucleotide excision repair; Incises the DNA at the 3' side of a lesion during nucleotide excision repair. Incises the DNA farther away from the lesion than UvrC. Not able to incise the 5' site of a lesion. In vitro, the incision activity of Cho is UvrA and UvrB dependent. When a lesion remains because UvrC is not able to induce the 3' incision, Cho incises the DNA. Then UvrC makes the 5' incision. The combined action of Cho and UvrC broadens the substrate range of nucleotide excision repair. | Excinuclease UvrABC, endonuclease subunit; 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. | 0.736 |
cho | uvrD | b1741 | b3813 | Endonuclease of nucleotide excision repair; Incises the DNA at the 3' side of a lesion during nucleotide excision repair. Incises the DNA farther away from the lesion than UvrC. Not able to incise the 5' site of a lesion. In vitro, the incision activity of Cho is UvrA and UvrB dependent. When a lesion remains because UvrC is not able to induce the 3' incision, Cho incises the DNA. Then UvrC makes the 5' incision. The combined action of Cho and UvrC broadens the substrate range of nucleotide excision repair. | DNA-dependent ATPase I and helicase II; A helicase with DNA-dependent ATPase activity. Unwinds DNA duplexes with 3' to 5' polarity with respect to the bound strand. Initiates unwinding more efficiently from a nicked substrate than ds duplex DNA. Involved in the post-incision events of nucleotide excision repair and methyl-directed mismatch repair, and probably also in repair of alkylated DNA (Probable). | 0.671 |
cho | ydjM | b1741 | b1728 | Endonuclease of nucleotide excision repair; Incises the DNA at the 3' side of a lesion during nucleotide excision repair. Incises the DNA farther away from the lesion than UvrC. Not able to incise the 5' site of a lesion. In vitro, the incision activity of Cho is UvrA and UvrB dependent. When a lesion remains because UvrC is not able to induce the 3' incision, Cho incises the DNA. Then UvrC makes the 5' incision. The combined action of Cho and UvrC broadens the substrate range of nucleotide excision repair. | Inner membrane protein regulated by LexA; Protein involved in SOS response; To B.subtilis YvsG. | 0.800 |
mutS | cho | b2733 | b1741 | Methyl-directed mismatch repair protein; This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity. | Endonuclease of nucleotide excision repair; Incises the DNA at the 3' side of a lesion during nucleotide excision repair. Incises the DNA farther away from the lesion than UvrC. Not able to incise the 5' site of a lesion. In vitro, the incision activity of Cho is UvrA and UvrB dependent. When a lesion remains because UvrC is not able to induce the 3' incision, Cho incises the DNA. Then UvrC makes the 5' incision. The combined action of Cho and UvrC broadens the substrate range of nucleotide excision repair. | 0.755 |
mutS | sbcD | b2733 | b0398 | Methyl-directed mismatch repair protein; This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity. | Exonuclease, dsDNA, ATP-dependent; 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; Belongs to the SbcD family. | 0.719 |
mutS | uvrA | b2733 | b4058 | Methyl-directed mismatch repair protein; This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity. | ATPase and DNA damage recognition protein of nucleotide excision repair excinuclease UvrABC; 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. | 0.703 |
mutS | uvrB | b2733 | b0779 | Methyl-directed mismatch repair protein; This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity. | Exision nuclease of nucleotide excision repair, DNA damage recognition component; 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 lesi [...] | 0.682 |
mutS | uvrC | b2733 | b1913 | Methyl-directed mismatch repair protein; This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity. | Excinuclease UvrABC, endonuclease subunit; 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. | 0.796 |
mutS | uvrD | b2733 | b3813 | Methyl-directed mismatch repair protein; This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity. | DNA-dependent ATPase I and helicase II; A helicase with DNA-dependent ATPase activity. Unwinds DNA duplexes with 3' to 5' polarity with respect to the bound strand. Initiates unwinding more efficiently from a nicked substrate than ds duplex DNA. Involved in the post-incision events of nucleotide excision repair and methyl-directed mismatch repair, and probably also in repair of alkylated DNA (Probable). | 0.718 |
nadE | cho | b1740 | b1741 | NAD synthetase, NH3/glutamine-dependent; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. | Endonuclease of nucleotide excision repair; Incises the DNA at the 3' side of a lesion during nucleotide excision repair. Incises the DNA farther away from the lesion than UvrC. Not able to incise the 5' site of a lesion. In vitro, the incision activity of Cho is UvrA and UvrB dependent. When a lesion remains because UvrC is not able to induce the 3' incision, Cho incises the DNA. Then UvrC makes the 5' incision. The combined action of Cho and UvrC broadens the substrate range of nucleotide excision repair. | 0.802 |
ruvA | cho | b1861 | b1741 | Component of RuvABC resolvasome, regulatory subunit; 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. Binds both single- and double-stranded DNA (dsDNA). Binds preferentially to supercoiled rather than to relaxed dsDNA. | Endonuclease of nucleotide excision repair; Incises the DNA at the 3' side of a lesion during nucleotide excision repair. Incises the DNA farther away from the lesion than UvrC. Not able to incise the 5' site of a lesion. In vitro, the incision activity of Cho is UvrA and UvrB dependent. When a lesion remains because UvrC is not able to induce the 3' incision, Cho incises the DNA. Then UvrC makes the 5' incision. The combined action of Cho and UvrC broadens the substrate range of nucleotide excision repair. | 0.664 |
ruvA | ruvB | b1861 | b1860 | Component of RuvABC resolvasome, regulatory subunit; 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. Binds both single- and double-stranded DNA (dsDNA). Binds preferentially to supercoiled rather than to relaxed dsDNA. | ATP-dependent DNA helicase, component of RuvABC resolvasome; 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. Belongs to the RuvB family. | 0.999 |
ruvA | sbcD | b1861 | b0398 | Component of RuvABC resolvasome, regulatory subunit; 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. Binds both single- and double-stranded DNA (dsDNA). Binds preferentially to supercoiled rather than to relaxed dsDNA. | Exonuclease, dsDNA, ATP-dependent; 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; Belongs to the SbcD family. | 0.608 |