| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| FtsW | dinP | azo0883 | azo2786 | Cell division protein FtsW; Peptidoglycan polymerase that is essential for cell division. Belongs to the SEDS family. FtsW subfamily. | 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. | 0.775 |
| FtsW | dnaN | azo0883 | azo0002 | Cell division protein FtsW; Peptidoglycan polymerase that is essential for cell division. Belongs to the SEDS family. FtsW subfamily. | DNA-directed DNA polymerase; 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 repl [...] | 0.667 |
| FtsW | fkbP | azo0883 | azo3319 | Cell division protein FtsW; Peptidoglycan polymerase that is essential for cell division. Belongs to the SEDS family. FtsW subfamily. | Peptidyl-prolyl cis-trans isomerase. Homology to fkbP of N. meningitidis of 69% (sprot|FKBP_NEIMB) PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. InterPro: FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase)(IPR001179) Pfam: FKBP-type peptidyl-prolyl cis-trans isomerase no signal peptide no TMHs; High confidence in function and specificity. | 0.678 |
| FtsW | polA | azo0883 | azo3600 | Cell division protein FtsW; Peptidoglycan polymerase that is essential for cell division. Belongs to the SEDS family. FtsW subfamily. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.504 |
| azo0839 | dinP | azo0839 | azo2786 | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | 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. | 0.729 |
| azo0839 | dnaN | azo0839 | azo0002 | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | DNA-directed DNA polymerase; 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 repl [...] | 0.967 |
| azo0839 | holB | azo0839 | azo1596 | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | DNA polymerase III delta 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 (By similarity). TIGRFAM: holB: DNA polymerase III delta prime; High confidence in function and specificity. | 0.431 |
| azo0839 | polA | azo0839 | azo3600 | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.986 |
| azo0839 | recA | azo0839 | azo0507 | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | Recombinase A; 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. | 0.931 |
| azo3955 | dinP | azo3955 | azo2786 | Conserved hypothetical protein. Homology to Daro03000439 of Dechloromonas aromatica of 48% (gi|41725494|ref|ZP_00152252.1|(NBCI ENTREZ)). No domains predicted. No signal peptide. No TMHs. | 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. | 0.864 |
| azo3955 | lexA | azo3955 | azo2064 | Conserved hypothetical protein. Homology to Daro03000439 of Dechloromonas aromatica of 48% (gi|41725494|ref|ZP_00152252.1|(NBCI ENTREZ)). No domains predicted. No signal peptide. No TMHs. | 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. | 0.600 |
| azo3955 | recA | azo3955 | azo0507 | Conserved hypothetical protein. Homology to Daro03000439 of Dechloromonas aromatica of 48% (gi|41725494|ref|ZP_00152252.1|(NBCI ENTREZ)). No domains predicted. No signal peptide. No TMHs. | Recombinase A; 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. | 0.555 |
| dinP | FtsW | azo2786 | azo0883 | 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. | Cell division protein FtsW; Peptidoglycan polymerase that is essential for cell division. Belongs to the SEDS family. FtsW subfamily. | 0.775 |
| dinP | azo0839 | azo2786 | azo0839 | 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. | SWI/SNF family helicase Pfam: Helicase conserved C-terminal domain; Specificity unclear. | 0.729 |
| dinP | azo3955 | azo2786 | azo3955 | 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. | Conserved hypothetical protein. Homology to Daro03000439 of Dechloromonas aromatica of 48% (gi|41725494|ref|ZP_00152252.1|(NBCI ENTREZ)). No domains predicted. No signal peptide. No TMHs. | 0.864 |
| dinP | dnaN | azo2786 | azo0002 | 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-directed DNA polymerase; 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 repl [...] | 0.974 |
| dinP | fkbP | azo2786 | azo3319 | 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. | Peptidyl-prolyl cis-trans isomerase. Homology to fkbP of N. meningitidis of 69% (sprot|FKBP_NEIMB) PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. InterPro: FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase)(IPR001179) Pfam: FKBP-type peptidyl-prolyl cis-trans isomerase no signal peptide no TMHs; High confidence in function and specificity. | 0.827 |
| dinP | holB | azo2786 | azo1596 | 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 delta 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 (By similarity). TIGRFAM: holB: DNA polymerase III delta prime; High confidence in function and specificity. | 0.765 |
| dinP | lexA | azo2786 | azo2064 | 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. | 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. | 0.931 |
| dinP | polA | azo2786 | azo3600 | 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 I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.831 |