| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| F897_00580 | F897_02424 | F897_00580 | F897_02424 | Beta sliding clamp; 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 replication a [...] | Uncharacterized protein. | 0.997 |
| F897_00580 | F897_03249 | F897_00580 | F897_03249 | Beta sliding clamp; 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 replication a [...] | UmuC domain-containing protein. | 0.910 |
| F897_00580 | polA | F897_00580 | F897_01164 | Beta sliding clamp; 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 replication a [...] | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.999 |
| F897_00580 | recA | F897_00580 | F897_01883 | Beta sliding clamp; 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 replication a [...] | Protein 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. | 0.915 |
| F897_00580 | topA | F897_00580 | F897_00180 | Beta sliding clamp; 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 replication a [...] | DNA topoisomerase 1; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] | 0.845 |
| F897_00697 | F897_03249 | F897_00697 | F897_03249 | Peptidase_S24 domain-containing protein; Belongs to the peptidase S24 family. | UmuC domain-containing protein. | 0.907 |
| F897_00697 | recA | F897_00697 | F897_01883 | Peptidase_S24 domain-containing protein; Belongs to the peptidase S24 family. | Protein 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. | 0.858 |
| F897_01967 | F897_03249 | F897_01967 | F897_03249 | Peptidase_S24 domain-containing protein; Belongs to the peptidase S24 family. | UmuC domain-containing protein. | 0.921 |
| F897_01967 | recA | F897_01967 | F897_01883 | Peptidase_S24 domain-containing protein; Belongs to the peptidase S24 family. | Protein 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. | 0.897 |
| F897_02002 | F897_03249 | F897_02002 | F897_03249 | Peptidase_S24 domain-containing protein. | UmuC domain-containing protein. | 0.552 |
| F897_02002 | recA | F897_02002 | F897_01883 | Peptidase_S24 domain-containing protein. | Protein 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. | 0.832 |
| F897_02424 | F897_00580 | F897_02424 | F897_00580 | Uncharacterized protein. | Beta sliding clamp; 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 replication a [...] | 0.997 |
| F897_02424 | F897_03249 | F897_02424 | F897_03249 | Uncharacterized protein. | UmuC domain-containing protein. | 0.677 |
| F897_02424 | polA | F897_02424 | F897_01164 | Uncharacterized protein. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.972 |
| F897_02424 | recA | F897_02424 | F897_01883 | Uncharacterized protein. | Protein 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. | 0.855 |
| F897_02424 | topA | F897_02424 | F897_00180 | Uncharacterized protein. | DNA topoisomerase 1; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] | 0.790 |
| F897_03248 | F897_03249 | F897_03248 | F897_03249 | Uncharacterized protein. | UmuC domain-containing protein. | 0.780 |
| F897_03248 | F897_03250 | F897_03248 | F897_03250 | Uncharacterized protein. | Peptidase_S24 domain-containing protein. | 0.777 |
| F897_03249 | F897_00580 | F897_03249 | F897_00580 | UmuC domain-containing protein. | Beta sliding clamp; 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 replication a [...] | 0.910 |
| F897_03249 | F897_00697 | F897_03249 | F897_00697 | UmuC domain-containing protein. | Peptidase_S24 domain-containing protein; Belongs to the peptidase S24 family. | 0.907 |
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