node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SFN76281.1 | SFO12629.1 | SAMN04489757_101116 | SAMN04489757_11018 | Helicase conserved C-terminal domain-containing protein. | Bifunctional non-homologous end joining protein LigD. | 0.740 |
SFN76281.1 | SFO51528.1 | SAMN04489757_101116 | SAMN04489757_13432 | Helicase conserved C-terminal domain-containing protein. | DNA polymerase-3 subunit beta; 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 re [...] | 0.996 |
SFN76281.1 | SFO63201.1 | SAMN04489757_101116 | SAMN04489757_1513 | Helicase conserved C-terminal domain-containing protein. | ATP-dependent DNA ligase LigD phosphoesterase module /ATP-dependent DNA ligase LigD polymerase module. | 0.755 |
SFN76281.1 | dinB | SAMN04489757_101116 | SAMN04489757_11064 | Helicase conserved C-terminal domain-containing protein. | DNA polymerase-4; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. | 0.528 |
SFN76281.1 | polA | SAMN04489757_101116 | SAMN04489757_1259 | Helicase conserved C-terminal domain-containing protein. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.997 |
SFN87205.1 | SFO51528.1 | SAMN04489757_103106 | SAMN04489757_13432 | MutS domain V. | DNA polymerase-3 subunit beta; 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 re [...] | 0.996 |
SFN87205.1 | polA | SAMN04489757_103106 | SAMN04489757_1259 | MutS domain V. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.996 |
SFN91342.1 | SFO51528.1 | SAMN04489757_10471 | SAMN04489757_13432 | DNA polymerase III, delta subunit. | DNA polymerase-3 subunit beta; 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 re [...] | 0.995 |
SFN91342.1 | dnaX | SAMN04489757_10471 | SAMN04489757_10860 | DNA polymerase III, delta subunit. | DNA polymerase-3 subunit gamma/tau; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. | 0.993 |
SFN91342.1 | polA | SAMN04489757_10471 | SAMN04489757_1259 | DNA polymerase III, delta subunit. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.746 |
SFO12629.1 | SFN76281.1 | SAMN04489757_11018 | SAMN04489757_101116 | Bifunctional non-homologous end joining protein LigD. | Helicase conserved C-terminal domain-containing protein. | 0.740 |
SFO12629.1 | SFO51528.1 | SAMN04489757_11018 | SAMN04489757_13432 | Bifunctional non-homologous end joining protein LigD. | DNA polymerase-3 subunit beta; 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 re [...] | 0.997 |
SFO12629.1 | SFO63201.1 | SAMN04489757_11018 | SAMN04489757_1513 | Bifunctional non-homologous end joining protein LigD. | ATP-dependent DNA ligase LigD phosphoesterase module /ATP-dependent DNA ligase LigD polymerase module. | 0.630 |
SFO12629.1 | polA | SAMN04489757_11018 | SAMN04489757_1259 | Bifunctional non-homologous end joining protein LigD. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.969 |
SFO51528.1 | SFN76281.1 | SAMN04489757_13432 | SAMN04489757_101116 | DNA polymerase-3 subunit beta; 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 re [...] | Helicase conserved C-terminal domain-containing protein. | 0.996 |
SFO51528.1 | SFN87205.1 | SAMN04489757_13432 | SAMN04489757_103106 | DNA polymerase-3 subunit beta; 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 re [...] | MutS domain V. | 0.996 |
SFO51528.1 | SFN91342.1 | SAMN04489757_13432 | SAMN04489757_10471 | DNA polymerase-3 subunit beta; 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 re [...] | DNA polymerase III, delta subunit. | 0.995 |
SFO51528.1 | SFO12629.1 | SAMN04489757_13432 | SAMN04489757_11018 | DNA polymerase-3 subunit beta; 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 re [...] | Bifunctional non-homologous end joining protein LigD. | 0.997 |
SFO51528.1 | SFO63201.1 | SAMN04489757_13432 | SAMN04489757_1513 | DNA polymerase-3 subunit beta; 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 re [...] | ATP-dependent DNA ligase LigD phosphoesterase module /ATP-dependent DNA ligase LigD polymerase module. | 0.997 |
SFO51528.1 | dinB | SAMN04489757_13432 | SAMN04489757_11064 | DNA polymerase-3 subunit beta; 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 re [...] | DNA polymerase-4; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. | 0.995 |