| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ABF39007.1 | ABF39809.1 | Acid345_0002 | Acid345_0804 | 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 [...] | A/G-specific DNA glycosylase. | 0.591 |
| ABF39007.1 | ABF40994.1 | Acid345_0002 | Acid345_1993 | 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 [...] | Exodeoxyribonuclease III (xth). | 0.901 |
| ABF39007.1 | ABF41390.1 | Acid345_0002 | Acid345_2389 | 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 [...] | DNA polymerase X family protein. | 0.786 |
| ABF39007.1 | dinB | Acid345_0002 | Acid345_1547 | 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 [...] | 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. | 0.973 |
| ABF39278.1 | ABF39809.1 | Acid345_0273 | Acid345_0804 | methylated-DNA--protein-cysteine 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. | A/G-specific DNA glycosylase. | 0.418 |
| ABF39278.1 | dinB | Acid345_0273 | Acid345_1547 | methylated-DNA--protein-cysteine 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-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. | 0.415 |
| ABF39809.1 | ABF39007.1 | Acid345_0804 | Acid345_0002 | A/G-specific DNA glycosylase. | 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 [...] | 0.591 |
| ABF39809.1 | ABF39278.1 | Acid345_0804 | Acid345_0273 | A/G-specific DNA glycosylase. | methylated-DNA--protein-cysteine 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. | 0.418 |
| ABF39809.1 | ABF39810.1 | Acid345_0804 | Acid345_0805 | A/G-specific DNA glycosylase. | Peroxiredoxin-like protein. | 0.773 |
| ABF39809.1 | ABF39811.1 | Acid345_0804 | Acid345_0806 | A/G-specific DNA glycosylase. | Peptidase M28. | 0.510 |
| ABF39809.1 | ABF40994.1 | Acid345_0804 | Acid345_1993 | A/G-specific DNA glycosylase. | Exodeoxyribonuclease III (xth). | 0.860 |
| ABF39809.1 | ABF41367.1 | Acid345_0804 | Acid345_2366 | A/G-specific DNA glycosylase. | Putative oxygen-independent coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.491 |
| ABF39809.1 | ABF41390.1 | Acid345_0804 | Acid345_2389 | A/G-specific DNA glycosylase. | DNA polymerase X family protein. | 0.410 |
| ABF39809.1 | birA | Acid345_0804 | Acid345_0135 | A/G-specific DNA glycosylase. | Biotin--acetyl-CoA-carboxylase ligase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a repressor; Belongs to the biotin--protein ligase family. | 0.466 |
| ABF39809.1 | dinB | Acid345_0804 | Acid345_1547 | A/G-specific DNA glycosylase. | 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. | 0.453 |
| ABF39810.1 | ABF39809.1 | Acid345_0805 | Acid345_0804 | Peroxiredoxin-like protein. | A/G-specific DNA glycosylase. | 0.773 |
| ABF39810.1 | ABF39811.1 | Acid345_0805 | Acid345_0806 | Peroxiredoxin-like protein. | Peptidase M28. | 0.450 |
| ABF39811.1 | ABF39809.1 | Acid345_0806 | Acid345_0804 | Peptidase M28. | A/G-specific DNA glycosylase. | 0.510 |
| ABF39811.1 | ABF39810.1 | Acid345_0806 | Acid345_0805 | Peptidase M28. | Peroxiredoxin-like protein. | 0.450 |
| ABF40994.1 | ABF39007.1 | Acid345_1993 | Acid345_0002 | Exodeoxyribonuclease III (xth). | 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 [...] | 0.901 |