| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| lexA | polYA | BSU17850 | BSU23870 | Transcriptional repressor of the SOS regulon; Represses dinA, dinB, dinC, recA genes and itself by binding to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'; some genes have a tandem consensus sequence and their binding is cooperative. 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; autocleavage is maximal at pH 11 in the absence of RecA and ssDNA. | DNA-damage lesion bypass DNA polymerase; 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 (By similarity). | 0.888 |
| lexA | polYB | BSU17850 | BSU23710 | Transcriptional repressor of the SOS regulon; Represses dinA, dinB, dinC, recA genes and itself by binding to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'; some genes have a tandem consensus sequence and their binding is cooperative. 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; autocleavage is maximal at pH 11 in the absence of RecA and ssDNA. | Y family DNA polymerase V bypassing lesions during replication; 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 (By similarity). | 0.887 |
| lexA | uvrX | BSU17850 | BSU21500 | Transcriptional repressor of the SOS regulon; Represses dinA, dinB, dinC, recA genes and itself by binding to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'; some genes have a tandem consensus sequence and their binding is cooperative. 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; autocleavage is maximal at pH 11 in the absence of RecA and ssDNA. | Lesion bypass phage DNA polymerase; Evidence 2b: Function of strongly homologous gene; enzyme. | 0.732 |
| lexA | yozK | BSU17850 | BSU18940 | Transcriptional repressor of the SOS regulon; Represses dinA, dinB, dinC, recA genes and itself by binding to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'; some genes have a tandem consensus sequence and their binding is cooperative. 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; autocleavage is maximal at pH 11 in the absence of RecA and ssDNA. | Putative DNA repair protein fragment; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; extrachromosomal origin. | 0.674 |
| lexA | yozL | BSU17850 | BSU18950 | Transcriptional repressor of the SOS regulon; Represses dinA, dinB, dinC, recA genes and itself by binding to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'; some genes have a tandem consensus sequence and their binding is cooperative. 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; autocleavage is maximal at pH 11 in the absence of RecA and ssDNA. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 12137951. | 0.487 |
| lexA | yqjX | BSU17850 | BSU23700 | Transcriptional repressor of the SOS regulon; Represses dinA, dinB, dinC, recA genes and itself by binding to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'; some genes have a tandem consensus sequence and their binding is cooperative. 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; autocleavage is maximal at pH 11 in the absence of RecA and ssDNA. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 12137951, 16267290. | 0.490 |
| polYA | lexA | BSU23870 | BSU17850 | DNA-damage lesion bypass DNA polymerase; 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 (By similarity). | Transcriptional repressor of the SOS regulon; Represses dinA, dinB, dinC, recA genes and itself by binding to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'; some genes have a tandem consensus sequence and their binding is cooperative. 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; autocleavage is maximal at pH 11 in the absence of RecA and ssDNA. | 0.888 |
| polYA | uvrX | BSU23870 | BSU21500 | DNA-damage lesion bypass DNA polymerase; 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 (By similarity). | Lesion bypass phage DNA polymerase; Evidence 2b: Function of strongly homologous gene; enzyme. | 0.481 |
| polYA | yozK | BSU23870 | BSU18940 | DNA-damage lesion bypass DNA polymerase; 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 (By similarity). | Putative DNA repair protein fragment; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; extrachromosomal origin. | 0.759 |
| polYA | yozL | BSU23870 | BSU18950 | DNA-damage lesion bypass DNA polymerase; 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 (By similarity). | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 12137951. | 0.689 |
| polYA | yqjX | BSU23870 | BSU23700 | DNA-damage lesion bypass DNA polymerase; 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 (By similarity). | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 12137951, 16267290. | 0.693 |
| polYB | lexA | BSU23710 | BSU17850 | Y family DNA polymerase V bypassing lesions during replication; 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 (By similarity). | Transcriptional repressor of the SOS regulon; Represses dinA, dinB, dinC, recA genes and itself by binding to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'; some genes have a tandem consensus sequence and their binding is cooperative. 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; autocleavage is maximal at pH 11 in the absence of RecA and ssDNA. | 0.887 |
| polYB | yozL | BSU23710 | BSU18950 | Y family DNA polymerase V bypassing lesions during replication; 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 (By similarity). | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 12137951. | 0.689 |
| polYB | yqjX | BSU23710 | BSU23700 | Y family DNA polymerase V bypassing lesions during replication; 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 (By similarity). | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 12137951, 16267290. | 0.935 |
| polYB | yqjZ | BSU23710 | BSU23680 | Y family DNA polymerase V bypassing lesions during replication; 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 (By similarity). | Putative degradation enzyme (oxygenase); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.453 |
| polYB | yqkA | BSU23710 | BSU23670 | Y family DNA polymerase V bypassing lesions during replication; 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 (By similarity). | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; In the C-terminal section; belongs to the UPF0157 (GrpB) family. | 0.474 |
| polYB | yqkB | BSU23710 | BSU23660 | Y family DNA polymerase V bypassing lesions during replication; 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 (By similarity). | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. | 0.470 |
| polYB | yqzH | BSU23710 | BSU23720 | Y family DNA polymerase V bypassing lesions during replication; 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 (By similarity). | Hypothetical protein; Evidence 5: No homology to any previously reported sequences. | 0.690 |
| uvrX | lexA | BSU21500 | BSU17850 | Lesion bypass phage DNA polymerase; Evidence 2b: Function of strongly homologous gene; enzyme. | Transcriptional repressor of the SOS regulon; Represses dinA, dinB, dinC, recA genes and itself by binding to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'; some genes have a tandem consensus sequence and their binding is cooperative. 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; autocleavage is maximal at pH 11 in the absence of RecA and ssDNA. | 0.732 |
| uvrX | polYA | BSU21500 | BSU23870 | Lesion bypass phage DNA polymerase; Evidence 2b: Function of strongly homologous gene; enzyme. | DNA-damage lesion bypass DNA polymerase; 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 (By similarity). | 0.481 |
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