| 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. | 0.566 |
| 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. | 0.687 |
| 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. | 0.944 |
| 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. | 0.717 |
| VC_1212 | nth | VC_1212 | VC_1011 | DNA polymerase II; Similar to GB:D10483 SP:P21189 GB:M35371 GB:M62646 GB:X54847; 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. | 0.573 |
| 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. | 0.951 |
| 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. | 0.881 |
| 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. | 0.566 |
| 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. | 0.906 |
| 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. | 0.915 |
| 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. | 0.973 |
| 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. | 0.819 |
| VC_A0961 | VC_A1017 | VC_A0961 | VC_A1017 | Hypothetical protein; Identified by Glimmer2; putative. | methylated-DNA--protein-cysteine S-methyltransferase; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | 0.419 |
| VC_A0961 | VC_A1018 | VC_A0961 | VC_A1018 | Hypothetical protein; Identified by Glimmer2; putative. | Ada regulatory protein; Similar to SP:Q10630 PID:1340083 PID:1513196 GB:AL123456; identified by sequence similarity; putative. | 0.697 |
| VC_A1016 | VC_A1017 | VC_A1016 | VC_A1017 | Hypothetical protein; Identified by Glimmer2; putative. | methylated-DNA--protein-cysteine S-methyltransferase; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | 0.847 |
| VC_A1016 | VC_A1018 | VC_A1016 | VC_A1018 | Hypothetical protein; Identified by Glimmer2; putative. | Ada regulatory protein; Similar to SP:Q10630 PID:1340083 PID:1513196 GB:AL123456; identified by sequence similarity; putative. | 0.847 |
| VC_A1017 | VC_A0961 | VC_A1017 | VC_A0961 | methylated-DNA--protein-cysteine S-methyltransferase; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | Hypothetical protein; Identified by Glimmer2; putative. | 0.419 |
| VC_A1017 | VC_A1016 | VC_A1017 | VC_A1016 | methylated-DNA--protein-cysteine S-methyltransferase; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | Hypothetical protein; Identified by Glimmer2; putative. | 0.847 |
| VC_A1017 | VC_A1018 | VC_A1017 | VC_A1018 | methylated-DNA--protein-cysteine S-methyltransferase; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | Ada regulatory protein; Similar to SP:Q10630 PID:1340083 PID:1513196 GB:AL123456; identified by sequence similarity; putative. | 0.997 |
| VC_A1017 | polA | VC_A1017 | VC_0108 | methylated-DNA--protein-cysteine S-methyltransferase; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.427 |