| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| PSHAa1159 | dinB | PSHAa1159 | PSHAa2389 | Putative orphan protein; Component of the SOS system and an inhibitor of cell division. Accumulation of SulA causes rapid cessation of cell division and the appearance of long, non-septate filaments. In the presence of GTP, binds a polymerization-competent form of FtsZ in a 1:1 ratio, thus inhibiting FtsZ polymerization and therefore preventing it from participating in the assembly of the Z ring. This mechanism prevents the premature segregation of damaged DNA to daughter cells during cell division. | DNA polymerase IV, devoid of proofreading, 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. | 0.851 |
| PSHAa1159 | dnaE | PSHAa1159 | PSHAa2015 | Putative orphan protein; Component of the SOS system and an inhibitor of cell division. Accumulation of SulA causes rapid cessation of cell division and the appearance of long, non-septate filaments. In the presence of GTP, binds a polymerization-competent form of FtsZ in a 1:1 ratio, thus inhibiting FtsZ polymerization and therefore preventing it from participating in the assembly of the Z ring. This mechanism prevents the premature segregation of damaged DNA to daughter cells during cell division. | DNA polymerase III, alpha subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.526 |
| PSHAa1990 | PSHAb0291 | PSHAa1990 | PSHAb0291 | DNA polymerase II; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Putative ADA regulatory protein (Regulatory protein of adaptative response); Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | 0.482 |
| PSHAa1990 | dinB | PSHAa1990 | PSHAa2389 | DNA polymerase II; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | DNA polymerase IV, devoid of proofreading, 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. | 0.852 |
| PSHAa1990 | dnaN | PSHAa1990 | PSHAa0002 | DNA polymerase II; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 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 [...] | 0.958 |
| PSHAa1990 | recA | PSHAa1990 | PSHAa0694 | DNA polymerase II; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | RecA protein (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. | 0.847 |
| PSHAb0291 | PSHAa1990 | PSHAb0291 | PSHAa1990 | Putative ADA regulatory protein (Regulatory protein of adaptative response); Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | DNA polymerase II; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.482 |
| PSHAb0291 | dinB | PSHAb0291 | PSHAa2389 | Putative ADA regulatory protein (Regulatory protein of adaptative response); Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | DNA polymerase IV, devoid of proofreading, 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. | 0.642 |
| PSHAb0291 | recA | PSHAb0291 | PSHAa0694 | Putative ADA regulatory protein (Regulatory protein of adaptative response); Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | RecA protein (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. | 0.765 |
| dinB | PSHAa1159 | PSHAa2389 | PSHAa1159 | DNA polymerase IV, devoid of proofreading, 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. | Putative orphan protein; Component of the SOS system and an inhibitor of cell division. Accumulation of SulA causes rapid cessation of cell division and the appearance of long, non-septate filaments. In the presence of GTP, binds a polymerization-competent form of FtsZ in a 1:1 ratio, thus inhibiting FtsZ polymerization and therefore preventing it from participating in the assembly of the Z ring. This mechanism prevents the premature segregation of damaged DNA to daughter cells during cell division. | 0.851 |
| dinB | PSHAa1990 | PSHAa2389 | PSHAa1990 | DNA polymerase IV, devoid of proofreading, 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 II; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.852 |
| dinB | PSHAb0291 | PSHAa2389 | PSHAb0291 | DNA polymerase IV, devoid of proofreading, 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. | Putative ADA regulatory protein (Regulatory protein of adaptative response); Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | 0.642 |
| dinB | dnaE | PSHAa2389 | PSHAa2015 | DNA polymerase IV, devoid of proofreading, 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; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.655 |
| dinB | dnaN | PSHAa2389 | PSHAa0002 | DNA polymerase IV, devoid of proofreading, 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 [...] | 0.851 |
| dinB | gcvP | PSHAa2389 | PSHAa2473 | DNA polymerase IV, devoid of proofreading, 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. | Glycine cleavage complex protein P, glycine decarboxylase, PLP-dependent; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family. | 0.609 |
| dinB | lexA | PSHAa2389 | PSHAa2873 | DNA polymerase IV, devoid of proofreading, 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. | Transcriptional repressor for SOS response; Represses a number of genes involved in the response to DNA damage (SOS response). | 0.781 |
| dinB | recA | PSHAa2389 | PSHAa0694 | DNA polymerase IV, devoid of proofreading, 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 (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. | 0.812 |
| dinB | tas | PSHAa2389 | PSHAa2392 | DNA polymerase IV, devoid of proofreading, 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. | Putative NADPH-dependent aldose reductase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.730 |
| dinB | umuD | PSHAa2389 | PSHAb0537 | DNA polymerase IV, devoid of proofreading, 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. | Component of DNA polymerase V; Function of strongly homologous gene; enzyme; Belongs to the peptidase S24 family. | 0.765 |
| dnaE | PSHAa1159 | PSHAa2015 | PSHAa1159 | DNA polymerase III, alpha subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Putative orphan protein; Component of the SOS system and an inhibitor of cell division. Accumulation of SulA causes rapid cessation of cell division and the appearance of long, non-septate filaments. In the presence of GTP, binds a polymerization-competent form of FtsZ in a 1:1 ratio, thus inhibiting FtsZ polymerization and therefore preventing it from participating in the assembly of the Z ring. This mechanism prevents the premature segregation of damaged DNA to daughter cells during cell division. | 0.526 |
