| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| VC_0354 | dinB | VC_0354 | VC_2287 | Peptidyl-prolyl cis-trans isomerase, FKBP-type; Similar to SP:P45523 SP:P39175 PID:606281 PID:862300 GB:U00096; identified by sequence similarity; putative. | 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. | 0.836 |
| VC_0354 | ftsW | VC_0354 | VC_2402 | Peptidyl-prolyl cis-trans isomerase, FKBP-type; Similar to SP:P45523 SP:P39175 PID:606281 PID:862300 GB:U00096; identified by sequence similarity; putative. | Cell division protein FtsW; Peptidoglycan polymerase that is essential for cell division. Belongs to the SEDS family. FtsW subfamily. | 0.682 |
| VC_0354 | mrdB | VC_0354 | VC_0949 | Peptidyl-prolyl cis-trans isomerase, FKBP-type; Similar to SP:P45523 SP:P39175 PID:606281 PID:862300 GB:U00096; identified by sequence similarity; putative. | Rod shape-determining protein RodA; Peptidoglycan polymerase that is essential for cell wall elongation; Belongs to the SEDS family. MrdB/RodA subfamily. | 0.682 |
| VC_1212 | VC_A1018 | VC_1212 | VC_A1018 | DNA polymerase II; Similar to GB:D10483 SP:P21189 GB:M35371 GB:M62646 GB:X54847; identified by sequence similarity; putative. | Ada regulatory protein; Similar to SP:Q10630 PID:1340083 PID:1513196 GB:AL123456; identified by sequence similarity; putative. | 0.648 |
| VC_1212 | dinB | VC_1212 | VC_2287 | DNA polymerase II; Similar to GB:D10483 SP:P21189 GB:M35371 GB:M62646 GB:X54847; identified by sequence similarity; putative. | 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. | 0.971 |
| VC_1212 | dnaN | VC_1212 | VC_0013 | DNA polymerase II; Similar to GB:D10483 SP:P21189 GB:M35371 GB:M62646 GB:X54847; identified by sequence similarity; putative. | DNA polymerase III, beta chain; 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 r [...] | 0.987 |
| VC_1212 | lexA | VC_1212 | VC_0092 | DNA polymerase II; Similar to GB:D10483 SP:P21189 GB:M35371 GB:M62646 GB:X54847; identified by sequence similarity; putative. | LexA repressor; 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. | 0.536 |
| VC_1212 | recA | VC_1212 | VC_0543 | DNA polymerase II; Similar to GB:D10483 SP:P21189 GB:M35371 GB:M62646 GB:X54847; identified by sequence similarity; putative. | 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. | 0.921 |
| VC_2568 | dinB | VC_2568 | VC_2287 | Peptidyl-prolyl cis-trans isomerase, FKBP-type; Similar to GB:U14003 SP:P39311 PID:537048 GB:U00096 PID:1790652; identified by sequence similarity; putative. | 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. | 0.836 |
| VC_2568 | ftsW | VC_2568 | VC_2402 | Peptidyl-prolyl cis-trans isomerase, FKBP-type; Similar to GB:U14003 SP:P39311 PID:537048 GB:U00096 PID:1790652; identified by sequence similarity; putative. | Cell division protein FtsW; Peptidoglycan polymerase that is essential for cell division. Belongs to the SEDS family. FtsW subfamily. | 0.682 |
| VC_2568 | mrdB | VC_2568 | VC_0949 | Peptidyl-prolyl cis-trans isomerase, FKBP-type; Similar to GB:U14003 SP:P39311 PID:537048 GB:U00096 PID:1790652; identified by sequence similarity; putative. | Rod shape-determining protein RodA; Peptidoglycan polymerase that is essential for cell wall elongation; Belongs to the SEDS family. MrdB/RodA subfamily. | 0.682 |
| VC_A0530 | dinB | VC_A0530 | VC_2287 | Pyruvate-flavoredoxin oxidoreductase; Similar to GB:U00096 PID:1742250 PID:1742256 PID:1787642; identified by sequence similarity; putative. | 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. | 0.871 |
| VC_A0530 | recA | VC_A0530 | VC_0543 | Pyruvate-flavoredoxin oxidoreductase; Similar to GB:U00096 PID:1742250 PID:1742256 PID:1787642; identified by sequence similarity; putative. | 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. | 0.515 |
| VC_A1018 | VC_1212 | VC_A1018 | VC_1212 | Ada regulatory protein; Similar to SP:Q10630 PID:1340083 PID:1513196 GB:AL123456; identified by sequence similarity; putative. | DNA polymerase II; Similar to GB:D10483 SP:P21189 GB:M35371 GB:M62646 GB:X54847; identified by sequence similarity; putative. | 0.648 |
| VC_A1018 | dinB | VC_A1018 | VC_2287 | Ada regulatory protein; Similar to SP:Q10630 PID:1340083 PID:1513196 GB:AL123456; identified by sequence similarity; putative. | 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. | 0.842 |
| VC_A1018 | recA | VC_A1018 | VC_0543 | Ada regulatory protein; Similar to SP:Q10630 PID:1340083 PID:1513196 GB:AL123456; identified by sequence similarity; putative. | 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. | 0.734 |
| dinB | VC_0354 | VC_2287 | VC_0354 | 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. | Peptidyl-prolyl cis-trans isomerase, FKBP-type; Similar to SP:P45523 SP:P39175 PID:606281 PID:862300 GB:U00096; identified by sequence similarity; putative. | 0.836 |
| dinB | VC_1212 | VC_2287 | VC_1212 | 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 II; Similar to GB:D10483 SP:P21189 GB:M35371 GB:M62646 GB:X54847; identified by sequence similarity; putative. | 0.971 |
| dinB | VC_2568 | VC_2287 | VC_2568 | 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. | Peptidyl-prolyl cis-trans isomerase, FKBP-type; Similar to GB:U14003 SP:P39311 PID:537048 GB:U00096 PID:1790652; identified by sequence similarity; putative. | 0.836 |
| dinB | VC_A0530 | VC_2287 | VC_A0530 | 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. | Pyruvate-flavoredoxin oxidoreductase; Similar to GB:U00096 PID:1742250 PID:1742256 PID:1787642; identified by sequence similarity; putative. | 0.871 |