node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AEA67512.1 | ung | PSEBR_a1325 | PSEBR_a1326 | Putative hydratase/isomerase protein. | 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. | 0.660 |
AEA68012.1 | AEA70080.1 | PSEBR_a1798 | PSEBR_a3728 | Putative exodeoxyribonuclease III. | Exodeoxyribonuclease III. | 0.916 |
AEA68012.1 | AEA72053.1 | PSEBR_a1798 | PSEBR_a5526 | Putative exodeoxyribonuclease III. | Catabolite repression control protein. | 0.927 |
AEA68012.1 | PSEBR_a2 | PSEBR_a1798 | PSEBR_a2 | Putative exodeoxyribonuclease III. | 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 [...] | 0.705 |
AEA68012.1 | nth | PSEBR_a1798 | PSEBR_a4386 | Putative exodeoxyribonuclease III. | DNA-(apurinic or apyrimidinic site) lyase; 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. | 0.769 |
AEA68012.1 | polA | PSEBR_a1798 | PSEBR_a40 | Putative exodeoxyribonuclease III. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.781 |
AEA68012.1 | ung | PSEBR_a1798 | PSEBR_a1326 | Putative exodeoxyribonuclease III. | 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. | 0.586 |
AEA70080.1 | AEA68012.1 | PSEBR_a3728 | PSEBR_a1798 | Exodeoxyribonuclease III. | Putative exodeoxyribonuclease III. | 0.916 |
AEA70080.1 | AEA72053.1 | PSEBR_a3728 | PSEBR_a5526 | Exodeoxyribonuclease III. | Catabolite repression control protein. | 0.922 |
AEA70080.1 | PSEBR_a2 | PSEBR_a3728 | PSEBR_a2 | Exodeoxyribonuclease III. | 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 [...] | 0.705 |
AEA70080.1 | nth | PSEBR_a3728 | PSEBR_a4386 | Exodeoxyribonuclease III. | DNA-(apurinic or apyrimidinic site) lyase; 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. | 0.777 |
AEA70080.1 | polA | PSEBR_a3728 | PSEBR_a40 | Exodeoxyribonuclease III. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.781 |
AEA70080.1 | ung | PSEBR_a3728 | PSEBR_a1326 | Exodeoxyribonuclease III. | 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. | 0.586 |
AEA72053.1 | AEA68012.1 | PSEBR_a5526 | PSEBR_a1798 | Catabolite repression control protein. | Putative exodeoxyribonuclease III. | 0.927 |
AEA72053.1 | AEA70080.1 | PSEBR_a5526 | PSEBR_a3728 | Catabolite repression control protein. | Exodeoxyribonuclease III. | 0.922 |
AEA72053.1 | PSEBR_a2 | PSEBR_a5526 | PSEBR_a2 | Catabolite repression control protein. | 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 [...] | 0.705 |
AEA72053.1 | nth | PSEBR_a5526 | PSEBR_a4386 | Catabolite repression control protein. | DNA-(apurinic or apyrimidinic site) lyase; 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. | 0.893 |
AEA72053.1 | polA | PSEBR_a5526 | PSEBR_a40 | Catabolite repression control protein. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.781 |
AEA72053.1 | ung | PSEBR_a5526 | PSEBR_a1326 | Catabolite repression control protein. | 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. | 0.586 |
PSEBR_a2 | AEA68012.1 | PSEBR_a2 | PSEBR_a1798 | 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 [...] | Putative exodeoxyribonuclease III. | 0.705 |