| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| MMAR_1976 | miaB2 | MMAR_1976 | MMAR_1979 | Conserved hypothetical protein. | Conserved hypothetical protein; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | 0.500 |
| MMAR_1976 | recA | MMAR_1976 | MMAR_1977 | Conserved hypothetical protein. | Recombinase A RecA; 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; Belongs to the RecA family. | 0.749 |
| MMAR_1976 | recX | MMAR_1976 | MMAR_1978 | Conserved hypothetical protein. | Regulatory protein RecX; Modulates RecA activity; Belongs to the RecX family. | 0.749 |
| MMAR_4573 | ku | MMAR_4573 | MMAR_4575 | ATP dependent DNA ligase; This protein is thought to seal nicks in double- stranded DNA during DNA replication, DNA recombination and DNA repair [catalytic activity:ATP + {deoxyribonucleotide}(N) + {deoxyribonucleotide}(M) = AMP + diphosphate + {deoxyribonucleotide}(N+M)]. | Conserved hypothetical protein; With LigD forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity. Binds linear dsDNA with 5'- and 3'- overhangs but not closed circular dsDNA nor ssDNA. Recruits and stimulates the ligase activity of LigD. Belongs to the prokaryotic Ku family. | 0.993 |
| MMAR_4573 | recA | MMAR_4573 | MMAR_1977 | ATP dependent DNA ligase; This protein is thought to seal nicks in double- stranded DNA during DNA replication, DNA recombination and DNA repair [catalytic activity:ATP + {deoxyribonucleotide}(N) + {deoxyribonucleotide}(M) = AMP + diphosphate + {deoxyribonucleotide}(N+M)]. | Recombinase A RecA; 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; Belongs to the RecA family. | 0.812 |
| MMAR_4573 | recX | MMAR_4573 | MMAR_1978 | ATP dependent DNA ligase; This protein is thought to seal nicks in double- stranded DNA during DNA replication, DNA recombination and DNA repair [catalytic activity:ATP + {deoxyribonucleotide}(N) + {deoxyribonucleotide}(M) = AMP + diphosphate + {deoxyribonucleotide}(N+M)]. | Regulatory protein RecX; Modulates RecA activity; Belongs to the RecX family. | 0.784 |
| cinA | lexA | MMAR_2796 | MMAR_1992 | Competence/damage-inducible protein CinA; CinA is the first gene in the competence-inducible (cin) operon, and is thought to be specifically required at some stage in the process of transformation. | Repressor LexA; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair. | 0.586 |
| cinA | recA | MMAR_2796 | MMAR_1977 | Competence/damage-inducible protein CinA; CinA is the first gene in the competence-inducible (cin) operon, and is thought to be specifically required at some stage in the process of transformation. | Recombinase A RecA; 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; Belongs to the RecA family. | 0.827 |
| cinA | recX | MMAR_2796 | MMAR_1978 | Competence/damage-inducible protein CinA; CinA is the first gene in the competence-inducible (cin) operon, and is thought to be specifically required at some stage in the process of transformation. | Regulatory protein RecX; Modulates RecA activity; Belongs to the RecX family. | 0.763 |
| cinA | ruvA | MMAR_2796 | MMAR_2110 | Competence/damage-inducible protein CinA; CinA is the first gene in the competence-inducible (cin) operon, and is thought to be specifically required at some stage in the process of transformation. | 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. | 0.687 |
| ku | MMAR_4573 | MMAR_4575 | MMAR_4573 | Conserved hypothetical protein; With LigD forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity. Binds linear dsDNA with 5'- and 3'- overhangs but not closed circular dsDNA nor ssDNA. Recruits and stimulates the ligase activity of LigD. Belongs to the prokaryotic Ku family. | ATP dependent DNA ligase; This protein is thought to seal nicks in double- stranded DNA during DNA replication, DNA recombination and DNA repair [catalytic activity:ATP + {deoxyribonucleotide}(N) + {deoxyribonucleotide}(M) = AMP + diphosphate + {deoxyribonucleotide}(N+M)]. | 0.993 |
| ku | recX | MMAR_4575 | MMAR_1978 | Conserved hypothetical protein; With LigD forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity. Binds linear dsDNA with 5'- and 3'- overhangs but not closed circular dsDNA nor ssDNA. Recruits and stimulates the ligase activity of LigD. Belongs to the prokaryotic Ku family. | Regulatory protein RecX; Modulates RecA activity; Belongs to the RecX family. | 0.685 |
| lexA | cinA | MMAR_1992 | MMAR_2796 | Repressor LexA; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair. | Competence/damage-inducible protein CinA; CinA is the first gene in the competence-inducible (cin) operon, and is thought to be specifically required at some stage in the process of transformation. | 0.586 |
| lexA | radA | MMAR_1992 | MMAR_5085 | Repressor LexA; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair. | DNA repair protein RadA; 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. | 0.563 |
| lexA | recA | MMAR_1992 | MMAR_1977 | Repressor LexA; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair. | Recombinase A RecA; 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; Belongs to the RecA family. | 0.995 |
| lexA | recX | MMAR_1992 | MMAR_1978 | Repressor LexA; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair. | Regulatory protein RecX; Modulates RecA activity; Belongs to the RecX family. | 0.706 |
| lexA | ruvA | MMAR_1992 | MMAR_2110 | Repressor LexA; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair. | 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. | 0.787 |
| lexA | ruvC | MMAR_1992 | MMAR_2109 | Repressor LexA; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair. | Crossover junction endodeoxyribonuclease RuvC; 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. | 0.516 |
| miaB2 | MMAR_1976 | MMAR_1979 | MMAR_1976 | Conserved hypothetical protein; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | Conserved hypothetical protein. | 0.500 |
| miaB2 | recA | MMAR_1979 | MMAR_1977 | Conserved hypothetical protein; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | Recombinase A RecA; 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; Belongs to the RecA family. | 0.672 |