| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| VC_1212 | VC_1860 | VC_1212 | VC_1860 | DNA polymerase II; Similar to GB:D10483 SP:P21189 GB:M35371 GB:M62646 GB:X54847; identified by sequence similarity; putative. | Exodeoxyribonuclease III; Similar to PID:1388153; identified by sequence similarity; putative. | 0.762 |
| 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 | nfo | VC_1212 | VC_2360 | DNA polymerase II; Similar to GB:D10483 SP:P21189 GB:M35371 GB:M62646 GB:X54847; identified by sequence similarity; putative. | Endonuclease IV; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate. | 0.730 |
| VC_1212 | polA | VC_1212 | VC_0108 | DNA polymerase II; Similar to GB:D10483 SP:P21189 GB:M35371 GB:M62646 GB:X54847; identified by sequence similarity; putative. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.969 |
| VC_1860 | VC_1212 | VC_1860 | VC_1212 | Exodeoxyribonuclease III; Similar to PID:1388153; 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. | 0.762 |
| VC_1860 | VC_A1018 | VC_1860 | VC_A1018 | Exodeoxyribonuclease III; Similar to PID:1388153; identified by sequence similarity; putative. | Ada regulatory protein; Similar to SP:Q10630 PID:1340083 PID:1513196 GB:AL123456; identified by sequence similarity; putative. | 0.885 |
| VC_1860 | gmhB | VC_1860 | VC_0908 | Exodeoxyribonuclease III; Similar to PID:1388153; identified by sequence similarity; putative. | Histidinol phosphatase-related protein; Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position in vitro. Also catalyzes the dephosphorylation of D-glycero-alpha-D-manno-heptose-1,7- bisphosphate in vitro; Belongs to the GmhB family. | 0.696 |
| VC_1860 | hisB | VC_1860 | VC_1135 | Exodeoxyribonuclease III; Similar to PID:1388153; identified by sequence similarity; putative. | Imidazoleglycerol-phosphate dehydratase/histidinol-phosphatase; Similar to SP:P06987 GB:X03416 PID:41696 PID:41711 GB:U00096; identified by sequence similarity; putative; In the C-terminal section; belongs to the imidazoleglycerol-phosphate dehydratase family. | 0.796 |
| VC_1860 | nfo | VC_1860 | VC_2360 | Exodeoxyribonuclease III; Similar to PID:1388153; identified by sequence similarity; putative. | Endonuclease IV; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate. | 0.970 |
| VC_1860 | nth | VC_1860 | VC_1011 | Exodeoxyribonuclease III; Similar to PID:1388153; identified by sequence similarity; putative. | Endonuclease III; DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate. | 0.992 |
| VC_1860 | polA | VC_1860 | VC_0108 | Exodeoxyribonuclease III; Similar to PID:1388153; identified by sequence similarity; putative. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.840 |
| VC_1860 | ung | VC_1860 | VC_2359 | Exodeoxyribonuclease III; Similar to PID:1388153; identified by sequence similarity; putative. | uracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | 0.822 |
| 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 | VC_1860 | VC_A1018 | VC_1860 | Ada regulatory protein; Similar to SP:Q10630 PID:1340083 PID:1513196 GB:AL123456; identified by sequence similarity; putative. | Exodeoxyribonuclease III; Similar to PID:1388153; identified by sequence similarity; putative. | 0.885 |
| 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 | nfo | VC_A1018 | VC_2360 | Ada regulatory protein; Similar to SP:Q10630 PID:1340083 PID:1513196 GB:AL123456; identified by sequence similarity; putative. | Endonuclease IV; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate. | 0.760 |
| VC_A1018 | nth | VC_A1018 | VC_1011 | Ada regulatory protein; Similar to SP:Q10630 PID:1340083 PID:1513196 GB:AL123456; identified by sequence similarity; putative. | Endonuclease III; DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate. | 0.548 |
| VC_A1018 | polA | VC_A1018 | VC_0108 | Ada regulatory protein; Similar to SP:Q10630 PID:1340083 PID:1513196 GB:AL123456; identified by sequence similarity; putative. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.666 |
| 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 |