| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| dnaN | hepA | PFREUD_00080 | PFREUD_00710 | DNA polymerase III, beta chain; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of r [...] | Helicase (SNF2-related protein). | 0.890 |
| dnaN | polA | PFREUD_00080 | PFREUD_15360 | DNA polymerase III, beta chain; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of r [...] | Putative DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.998 |
| dnaN | recA | PFREUD_00080 | PFREUD_13130 | DNA polymerase III, beta chain; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of r [...] | RecA (Recombinase A); 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. | 0.868 |
| dnaN | sbcC | PFREUD_00080 | PFREUD_04360 | DNA polymerase III, beta chain; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of r [...] | ATP-dependent dsDNA exonuclease SbcC; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3prime->5prime double strand exonuclease that can open hairpins. It also has a 5prim single-strand endonuclease activity. | 0.496 |
| dnaN | sbcD | PFREUD_00080 | PFREUD_04370 | DNA polymerase III, beta chain; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of r [...] | SbcD, DNA repair exonuclease; 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. | 0.498 |
| dnaN | uvrD | PFREUD_00080 | PFREUD_09880 | DNA polymerase III, beta chain; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of r [...] | DNA helicase. | 0.991 |
| dnaN | xthA | PFREUD_00080 | PFREUD_05380 | DNA polymerase III, beta chain; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of r [...] | Exodeoxyribonuclease III/exonuclease III; Exonucleolytic cleavage in the 3 prime- to 5 prime -direction to yield nucleoside 5 prime-phosphates. | 0.897 |
| hepA | dnaN | PFREUD_00710 | PFREUD_00080 | Helicase (SNF2-related protein). | DNA polymerase III, beta chain; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of r [...] | 0.890 |
| hepA | polA | PFREUD_00710 | PFREUD_15360 | Helicase (SNF2-related protein). | Putative DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.958 |
| hepA | recA | PFREUD_00710 | PFREUD_13130 | Helicase (SNF2-related protein). | RecA (Recombinase A); 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. | 0.853 |
| hepA | sbcC | PFREUD_00710 | PFREUD_04360 | Helicase (SNF2-related protein). | ATP-dependent dsDNA exonuclease SbcC; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3prime->5prime double strand exonuclease that can open hairpins. It also has a 5prim single-strand endonuclease activity. | 0.451 |
| hepA | sbcD | PFREUD_00710 | PFREUD_04370 | Helicase (SNF2-related protein). | SbcD, DNA repair exonuclease; 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. | 0.575 |
| hepA | uvrD | PFREUD_00710 | PFREUD_09880 | Helicase (SNF2-related protein). | DNA helicase. | 0.982 |
| mutM1 | mutM2 | PFREUD_01050 | PFREUD_07110 | Formamidopyrimidine-DNA glycosylase (Fapy-DNA glycosylase) (DNA-(apurinic or apyrimidinic site) lyase mutM) (AP lyase mutM); Belongs to the FPG family. | Formamidopyrimidine-DNA glycosylase (DNA-formamidopyrimidine glycosylase); Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3- and 5-phosphates; Belongs to the FPG family. | 0.928 |
| mutM1 | mutM3 | PFREUD_01050 | PFREUD_14440 | Formamidopyrimidine-DNA glycosylase (Fapy-DNA glycosylase) (DNA-(apurinic or apyrimidinic site) lyase mutM) (AP lyase mutM); Belongs to the FPG family. | Formamidopyrimidine-DNA glycosylase; Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. | 0.929 |
| mutM1 | polA | PFREUD_01050 | PFREUD_15360 | Formamidopyrimidine-DNA glycosylase (Fapy-DNA glycosylase) (DNA-(apurinic or apyrimidinic site) lyase mutM) (AP lyase mutM); Belongs to the FPG family. | Putative DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.936 |
| mutM2 | mutM1 | PFREUD_07110 | PFREUD_01050 | Formamidopyrimidine-DNA glycosylase (DNA-formamidopyrimidine glycosylase); Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3- and 5-phosphates; Belongs to the FPG family. | Formamidopyrimidine-DNA glycosylase (Fapy-DNA glycosylase) (DNA-(apurinic or apyrimidinic site) lyase mutM) (AP lyase mutM); Belongs to the FPG family. | 0.928 |
| mutM2 | mutM3 | PFREUD_07110 | PFREUD_14440 | Formamidopyrimidine-DNA glycosylase (DNA-formamidopyrimidine glycosylase); Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3- and 5-phosphates; Belongs to the FPG family. | Formamidopyrimidine-DNA glycosylase; Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. | 0.978 |
| mutM2 | polA | PFREUD_07110 | PFREUD_15360 | Formamidopyrimidine-DNA glycosylase (DNA-formamidopyrimidine glycosylase); Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3- and 5-phosphates; Belongs to the FPG family. | Putative DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.936 |
| mutM3 | mutM1 | PFREUD_14440 | PFREUD_01050 | Formamidopyrimidine-DNA glycosylase; Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. | Formamidopyrimidine-DNA glycosylase (Fapy-DNA glycosylase) (DNA-(apurinic or apyrimidinic site) lyase mutM) (AP lyase mutM); Belongs to the FPG family. | 0.929 |
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