node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AKT39640.1 | xth-2 | CMC5_037890 | CMC5_037880 | Uncharacterized protein. | Exodeoxyribonuclease III. | 0.773 |
AKT39943.1 | xth | CMC5_040960 | CMC5_006560 | Pseudouridine synthase; Belongs to the pseudouridine synthase RsuA family. | Exodeoxyribonuclease III. | 0.771 |
AKT39943.1 | xth-2 | CMC5_040960 | CMC5_037880 | Pseudouridine synthase; Belongs to the pseudouridine synthase RsuA family. | Exodeoxyribonuclease III. | 0.771 |
AKT40959.1 | AKT41086.1 | CMC5_051160 | CMC5_052450 | Adenine glycosylase; Adenine glycosylase active on G-A mispairs. | DNA-3-methyladenine glycosylase. | 0.402 |
AKT40959.1 | dnaN | CMC5_051160 | CMC5_005410 | Adenine glycosylase; Adenine glycosylase active on G-A mispairs. | DNA polymerase III subunit beta; 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 [...] | 0.525 |
AKT40959.1 | xth | CMC5_051160 | CMC5_006560 | Adenine glycosylase; Adenine glycosylase active on G-A mispairs. | Exodeoxyribonuclease III. | 0.743 |
AKT40959.1 | xth-2 | CMC5_051160 | CMC5_037880 | Adenine glycosylase; Adenine glycosylase active on G-A mispairs. | Exodeoxyribonuclease III. | 0.743 |
AKT41086.1 | AKT40959.1 | CMC5_052450 | CMC5_051160 | DNA-3-methyladenine glycosylase. | Adenine glycosylase; Adenine glycosylase active on G-A mispairs. | 0.402 |
AKT41086.1 | nth | CMC5_052450 | CMC5_032300 | DNA-3-methyladenine glycosylase. | 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. | 0.425 |
AKT41086.1 | nth-2 | CMC5_052450 | CMC5_050980 | DNA-3-methyladenine glycosylase. | Uncharacterized protein; 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. | 0.425 |
AKT41086.1 | polA | CMC5_052450 | CMC5_003550 | DNA-3-methyladenine glycosylase. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.608 |
AKT41086.1 | xth | CMC5_052450 | CMC5_006560 | DNA-3-methyladenine glycosylase. | Exodeoxyribonuclease III. | 0.816 |
AKT41086.1 | xth-2 | CMC5_052450 | CMC5_037880 | DNA-3-methyladenine glycosylase. | Exodeoxyribonuclease III. | 0.816 |
dnaN | AKT40959.1 | CMC5_005410 | CMC5_051160 | DNA polymerase III subunit beta; 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 [...] | Adenine glycosylase; Adenine glycosylase active on G-A mispairs. | 0.525 |
dnaN | polA | CMC5_005410 | CMC5_003550 | DNA polymerase III subunit beta; 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 I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.997 |
dnaN | ung-2 | CMC5_005410 | CMC5_032310 | DNA polymerase III subunit beta; 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; 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. | 0.778 |
dnaN | xth | CMC5_005410 | CMC5_006560 | DNA polymerase III subunit beta; 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. | 0.800 |
dnaN | xth-2 | CMC5_005410 | CMC5_037880 | DNA polymerase III subunit beta; 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. | 0.800 |
nth | AKT41086.1 | CMC5_032300 | CMC5_052450 | 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. | DNA-3-methyladenine glycosylase. | 0.425 |
nth | nth-2 | CMC5_032300 | CMC5_050980 | 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. | Uncharacterized protein; 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. | 0.905 |