| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AEB82442.1 | AEB82551.1 | Alide2_0002 | Alide2_0113 | 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 [...] | TIGRFAM: DNA helicase, ATP-dependent, RecQ type, bacterial; DNA helicase, ATP-dependent, RecQ type; PFAM: RQC domain; Helicase, C-terminal; DNA/RNA helicase, DEAD/DEAH box type, N-terminal; Helicase/RNase D C-terminal, HRDC domain; KEGG: dia:Dtpsy_0103 ATP-dependent DNA helicase RecQ; SMART: RQC domain; Helicase, C-terminal; DEAD-like helicase, N-terminal; Helicase/RNase D C-terminal, HRDC domain. | 0.796 |
| AEB82442.1 | dinB | Alide2_0002 | Alide2_1246 | 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 [...] | DNA-directed 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. | 0.922 |
| AEB82442.1 | lexA | Alide2_0002 | Alide2_2949 | 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 [...] | SOS-response transcriptional 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. | 0.405 |
| AEB82442.1 | polA | Alide2_0002 | Alide2_3637 | 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 [...] | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.987 |
| AEB82442.1 | recA | Alide2_0002 | Alide2_4568 | 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 [...] | 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. | 0.888 |
| AEB82442.1 | rpoB | Alide2_0002 | Alide2_0409 | 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 [...] | DNA-directed RNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.677 |
| AEB82551.1 | AEB82442.1 | Alide2_0113 | Alide2_0002 | TIGRFAM: DNA helicase, ATP-dependent, RecQ type, bacterial; DNA helicase, ATP-dependent, RecQ type; PFAM: RQC domain; Helicase, C-terminal; DNA/RNA helicase, DEAD/DEAH box type, N-terminal; Helicase/RNase D C-terminal, HRDC domain; KEGG: dia:Dtpsy_0103 ATP-dependent DNA helicase RecQ; SMART: RQC domain; Helicase, C-terminal; DEAD-like helicase, N-terminal; Helicase/RNase D C-terminal, HRDC domain. | 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 [...] | 0.796 |
| AEB82551.1 | dinB | Alide2_0113 | Alide2_1246 | TIGRFAM: DNA helicase, ATP-dependent, RecQ type, bacterial; DNA helicase, ATP-dependent, RecQ type; PFAM: RQC domain; Helicase, C-terminal; DNA/RNA helicase, DEAD/DEAH box type, N-terminal; Helicase/RNase D C-terminal, HRDC domain; KEGG: dia:Dtpsy_0103 ATP-dependent DNA helicase RecQ; SMART: RQC domain; Helicase, C-terminal; DEAD-like helicase, N-terminal; Helicase/RNase D C-terminal, HRDC domain. | DNA-directed 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. | 0.516 |
| AEB82551.1 | polA | Alide2_0113 | Alide2_3637 | TIGRFAM: DNA helicase, ATP-dependent, RecQ type, bacterial; DNA helicase, ATP-dependent, RecQ type; PFAM: RQC domain; Helicase, C-terminal; DNA/RNA helicase, DEAD/DEAH box type, N-terminal; Helicase/RNase D C-terminal, HRDC domain; KEGG: dia:Dtpsy_0103 ATP-dependent DNA helicase RecQ; SMART: RQC domain; Helicase, C-terminal; DEAD-like helicase, N-terminal; Helicase/RNase D C-terminal, HRDC domain. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.970 |
| AEB82551.1 | recA | Alide2_0113 | Alide2_4568 | TIGRFAM: DNA helicase, ATP-dependent, RecQ type, bacterial; DNA helicase, ATP-dependent, RecQ type; PFAM: RQC domain; Helicase, C-terminal; DNA/RNA helicase, DEAD/DEAH box type, N-terminal; Helicase/RNase D C-terminal, HRDC domain; KEGG: dia:Dtpsy_0103 ATP-dependent DNA helicase RecQ; SMART: RQC domain; Helicase, C-terminal; DEAD-like helicase, N-terminal; Helicase/RNase D C-terminal, HRDC domain. | 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. | 0.916 |
| AEB82872.1 | dinB | Alide2_0453 | Alide2_1246 | Hypothetical protein; Manually curated; KEGG: aav:Aave_0642 hypothetical protein. | DNA-directed 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. | 0.605 |
| AEB82872.1 | polA | Alide2_0453 | Alide2_3637 | Hypothetical protein; Manually curated; KEGG: aav:Aave_0642 hypothetical 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. | 0.432 |
| AEB82872.1 | recA | Alide2_0453 | Alide2_4568 | Hypothetical protein; Manually curated; KEGG: aav:Aave_0642 hypothetical protein. | 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. | 0.928 |
| AEB84440.1 | dinB | Alide2_2066 | Alide2_1246 | PFAM: Peptidase S24/S26A/S26B, conserved region; KEGG: tin:Tint_2913 peptidase S24/S26A/S26B, conserved region; Belongs to the peptidase S24 family. | DNA-directed 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. | 0.772 |
| AEB84440.1 | polA | Alide2_2066 | Alide2_3637 | PFAM: Peptidase S24/S26A/S26B, conserved region; KEGG: tin:Tint_2913 peptidase S24/S26A/S26B, conserved region; Belongs to the peptidase S24 family. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.432 |
| AEB84440.1 | recA | Alide2_2066 | Alide2_4568 | PFAM: Peptidase S24/S26A/S26B, conserved region; KEGG: tin:Tint_2913 peptidase S24/S26A/S26B, conserved region; Belongs to the peptidase S24 family. | 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. | 0.955 |
| dinB | AEB82442.1 | Alide2_1246 | Alide2_0002 | DNA-directed 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. | 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 [...] | 0.922 |
| dinB | AEB82551.1 | Alide2_1246 | Alide2_0113 | DNA-directed 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. | TIGRFAM: DNA helicase, ATP-dependent, RecQ type, bacterial; DNA helicase, ATP-dependent, RecQ type; PFAM: RQC domain; Helicase, C-terminal; DNA/RNA helicase, DEAD/DEAH box type, N-terminal; Helicase/RNase D C-terminal, HRDC domain; KEGG: dia:Dtpsy_0103 ATP-dependent DNA helicase RecQ; SMART: RQC domain; Helicase, C-terminal; DEAD-like helicase, N-terminal; Helicase/RNase D C-terminal, HRDC domain. | 0.516 |
| dinB | AEB82872.1 | Alide2_1246 | Alide2_0453 | DNA-directed 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. | Hypothetical protein; Manually curated; KEGG: aav:Aave_0642 hypothetical protein. | 0.605 |
| dinB | AEB84440.1 | Alide2_1246 | Alide2_2066 | DNA-directed 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. | PFAM: Peptidase S24/S26A/S26B, conserved region; KEGG: tin:Tint_2913 peptidase S24/S26A/S26B, conserved region; Belongs to the peptidase S24 family. | 0.772 |