node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AKI99283.1 | AKJ01985.1 | AA314_00910 | AA314_03611 | 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. | 0.703 |
AKI99283.1 | AKJ04171.1 | AA314_00910 | AA314_05797 | 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. | 0.690 |
AKI99283.1 | AKJ05421.1 | AA314_00910 | AA314_07047 | 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. | 0.703 |
AKI99283.1 | AKJ07373.1 | AA314_00910 | AA314_08999 | 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 [...] | Hypothetical protein. | 0.690 |
AKI99283.1 | ung | AA314_00910 | AA314_01696 | 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. | 0.725 |
AKJ00069.1 | ung | AA314_01695 | AA314_01696 | 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. | 0.525 |
AKJ01985.1 | AKI99283.1 | AA314_03611 | AA314_00910 | 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 [...] | 0.703 |
AKJ01985.1 | AKJ04171.1 | AA314_03611 | AA314_05797 | Exodeoxyribonuclease III. | Exodeoxyribonuclease III. | 0.925 |
AKJ01985.1 | AKJ05421.1 | AA314_03611 | AA314_07047 | Exodeoxyribonuclease III. | Exodeoxyribonuclease III. | 0.909 |
AKJ01985.1 | AKJ07373.1 | AA314_03611 | AA314_08999 | Exodeoxyribonuclease III. | Hypothetical protein. | 0.900 |
AKJ01985.1 | nfo | AA314_03611 | AA314_06682 | Exodeoxyribonuclease III. | Endonuclease IV; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to produce new 5'-ends that are base-free deoxyribose 5-phosphate residues. It preferentially attacks modified AP sites created by bleomycin and neocarzinostatin. | 0.592 |
AKJ01985.1 | nth-2 | AA314_03611 | AA314_05582 | 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. | 0.515 |
AKJ01985.1 | tadA | AA314_03611 | AA314_03218 | Exodeoxyribonuclease III. | tRNA-specific adenosine-34 deaminase; Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2); Belongs to the cytidine and deoxycytidylate deaminase family. | 0.440 |
AKJ01985.1 | ung | AA314_03611 | AA314_01696 | 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. | 0.543 |
AKJ04171.1 | AKI99283.1 | AA314_05797 | AA314_00910 | 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 [...] | 0.690 |
AKJ04171.1 | AKJ01985.1 | AA314_05797 | AA314_03611 | Exodeoxyribonuclease III. | Exodeoxyribonuclease III. | 0.925 |
AKJ04171.1 | AKJ05421.1 | AA314_05797 | AA314_07047 | Exodeoxyribonuclease III. | Exodeoxyribonuclease III. | 0.924 |
AKJ04171.1 | AKJ07373.1 | AA314_05797 | AA314_08999 | Exodeoxyribonuclease III. | Hypothetical protein. | 0.900 |
AKJ04171.1 | nfo | AA314_05797 | AA314_06682 | Exodeoxyribonuclease III. | Endonuclease IV; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to produce new 5'-ends that are base-free deoxyribose 5-phosphate residues. It preferentially attacks modified AP sites created by bleomycin and neocarzinostatin. | 0.592 |
AKJ04171.1 | nth-2 | AA314_05797 | AA314_05582 | 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. | 0.827 |