| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CAP_0959 | ung | CAP_0959 | CAP_1240 | Hypothetical protein. | Uracil-DNA glycosylase, family 1; 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. | 0.435 |
| CAP_1239 | CAP_1242 | CAP_1239 | CAP_1242 | Hypothetical protein. | Penicillin-binding protein, transpeptidase. | 0.477 |
| CAP_1239 | nth | CAP_1239 | CAP_1241 | Hypothetical protein. | 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. | 0.757 |
| CAP_1239 | ung | CAP_1239 | CAP_1240 | Hypothetical protein. | Uracil-DNA glycosylase, family 1; 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. | 0.762 |
| CAP_1242 | CAP_1239 | CAP_1242 | CAP_1239 | Penicillin-binding protein, transpeptidase. | Hypothetical protein. | 0.477 |
| CAP_1242 | nth | CAP_1242 | CAP_1241 | Penicillin-binding protein, transpeptidase. | 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. | 0.504 |
| CAP_1242 | ung | CAP_1242 | CAP_1240 | Penicillin-binding protein, transpeptidase. | Uracil-DNA glycosylase, family 1; 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. | 0.504 |
| CAP_1727 | CAP_5377 | CAP_1727 | CAP_5377 | Exodeoxyribonuclease III. | 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 [...] | 0.867 |
| CAP_1727 | nth | CAP_1727 | CAP_1241 | Exodeoxyribonuclease III. | 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. | 0.807 |
| CAP_1727 | nth-2 | CAP_1727 | CAP_7013 | Exodeoxyribonuclease III. | 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. | 0.791 |
| CAP_1727 | ung | CAP_1727 | CAP_1240 | Exodeoxyribonuclease III. | Uracil-DNA glycosylase, family 1; 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. | 0.771 |
| CAP_4334 | CAP_5377 | CAP_4334 | CAP_5377 | Exodeoxyribonuclease III. | 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 [...] | 0.867 |
| CAP_4334 | CAP_6548 | CAP_4334 | CAP_6548 | Exodeoxyribonuclease III. | Exodeoxyribonuclease III. | 0.764 |
| CAP_4334 | nth | CAP_4334 | CAP_1241 | Exodeoxyribonuclease III. | 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. | 0.966 |
| CAP_4334 | nth-2 | CAP_4334 | CAP_7013 | Exodeoxyribonuclease III. | 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. | 0.819 |
| CAP_4334 | ung | CAP_4334 | CAP_1240 | Exodeoxyribonuclease III. | Uracil-DNA glycosylase, family 1; 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. | 0.771 |
| CAP_5377 | CAP_1727 | CAP_5377 | CAP_1727 | 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. | 0.867 |
| CAP_5377 | CAP_4334 | CAP_5377 | CAP_4334 | 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. | 0.867 |
| CAP_5377 | CAP_6548 | CAP_5377 | CAP_6548 | 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. | 0.867 |
| CAP_5377 | ung | CAP_5377 | CAP_1240 | 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 [...] | Uracil-DNA glycosylase, family 1; 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. | 0.871 |