node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CC_3610 | dinB | CC_3610 | CC_2466 | DNA ligase, ATP-dependent, putative; Identified by match to protein family HMM. | DNA-damage-inducible protein P; 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. | 0.626 |
CC_3610 | dnaE1 | CC_3610 | CC_1926 | DNA ligase, ATP-dependent, putative; Identified by match to protein family HMM. | DNA polymerase III, alpha subunit; 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. The alpha chain is the DNA polymerase (By similarity); Belongs to the DNA polymerase type-C family. DnaE subfamily. | 0.537 |
CC_3610 | dnaE2 | CC_3610 | CC_3211 | DNA ligase, ATP-dependent, putative; Identified by match to protein family HMM. | DNA polymerase III, alpha subunit, putative; DNA polymerase involved in damage-induced mutagenesis and translesion synthesis (TLS). Along with ImuA and ImuB is required for the error-prone processing of DNA lesions (By similarity). | 0.528 |
CC_3610 | dnaN | CC_3610 | CC_0156 | DNA ligase, ATP-dependent, putative; Identified by match to protein family HMM. | DNA polymerase III, beta subunit; 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 [...] | 0.993 |
CC_3610 | imuA | CC_3610 | CC_3213 | DNA ligase, ATP-dependent, putative; Identified by match to protein family HMM. | Hypothetical protein; Along with DnaE2 and ImuB is required for the error-prone processing of DNA lesions. | 0.566 |
CC_3610 | imuB | CC_3610 | CC_3212 | DNA ligase, ATP-dependent, putative; Identified by match to protein family HMM. | Hypothetical protein; Along with DnaE2 and ImuA is required for the error-prone processing of DNA lesions. | 0.814 |
CC_3610 | polA | CC_3610 | CC_3464 | DNA ligase, ATP-dependent, putative; Identified by match to protein family HMM. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.934 |
CC_3610 | recA | CC_3610 | CC_1087 | DNA ligase, ATP-dependent, putative; Identified by match to protein family HMM. | recA protein; 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. | 0.427 |
dinB | CC_3610 | CC_2466 | CC_3610 | DNA-damage-inducible protein P; 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. | DNA ligase, ATP-dependent, putative; Identified by match to protein family HMM. | 0.626 |
dinB | dnaE1 | CC_2466 | CC_1926 | DNA-damage-inducible protein P; 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. | DNA polymerase III, alpha subunit; 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. The alpha chain is the DNA polymerase (By similarity); Belongs to the DNA polymerase type-C family. DnaE subfamily. | 0.876 |
dinB | dnaE2 | CC_2466 | CC_3211 | DNA-damage-inducible protein P; 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. | DNA polymerase III, alpha subunit, putative; DNA polymerase involved in damage-induced mutagenesis and translesion synthesis (TLS). Along with ImuA and ImuB is required for the error-prone processing of DNA lesions (By similarity). | 0.883 |
dinB | dnaN | CC_2466 | CC_0156 | DNA-damage-inducible protein P; 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. | DNA polymerase III, beta subunit; 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 [...] | 0.970 |
dinB | imuA | CC_2466 | CC_3213 | DNA-damage-inducible protein P; 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. | Hypothetical protein; Along with DnaE2 and ImuB is required for the error-prone processing of DNA lesions. | 0.955 |
dinB | imuB | CC_2466 | CC_3212 | DNA-damage-inducible protein P; 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. | Hypothetical protein; Along with DnaE2 and ImuA is required for the error-prone processing of DNA lesions. | 0.798 |
dinB | lexA | CC_2466 | CC_1902 | DNA-damage-inducible protein P; 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. | 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. | 0.953 |
dinB | polA | CC_2466 | CC_3464 | DNA-damage-inducible protein P; 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. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.744 |
dinB | recA | CC_2466 | CC_1087 | DNA-damage-inducible protein P; 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. | recA protein; 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. | 0.934 |
dinB | uvrA | CC_2466 | CC_2590 | DNA-damage-inducible protein P; 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. | Excinuclease ABC, subunit A; 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. | 0.865 |
dnaE1 | CC_3610 | CC_1926 | CC_3610 | DNA polymerase III, alpha subunit; 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. The alpha chain is the DNA polymerase (By similarity); Belongs to the DNA polymerase type-C family. DnaE subfamily. | DNA ligase, ATP-dependent, putative; Identified by match to protein family HMM. | 0.537 |
dnaE1 | dinB | CC_1926 | CC_2466 | DNA polymerase III, alpha subunit; 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. The alpha chain is the DNA polymerase (By similarity); Belongs to the DNA polymerase type-C family. DnaE subfamily. | DNA-damage-inducible protein P; 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. | 0.876 |