node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
MDS_0002 | MDS_2334 | MDS_0002 | MDS_2334 | 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 [...] | Exonuclease III. | 0.777 |
MDS_0002 | MDS_2413 | MDS_0002 | MDS_2413 | 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 [...] | ATP-dependent DNA ligase. | 0.911 |
MDS_0002 | MDS_4591 | MDS_0002 | MDS_4591 | 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 [...] | A/G-specific DNA-adenine glycosylase; Adenine glycosylase active on G-A mispairs. | 0.657 |
MDS_0002 | MDS_4714 | MDS_0002 | MDS_4714 | 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 Xth. | 0.777 |
MDS_0002 | polA | MDS_0002 | MDS_0170 | 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. | 0.995 |
MDS_0002 | ung | MDS_0002 | MDS_1436 | 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. | 0.739 |
MDS_1946 | MDS_2334 | MDS_1946 | MDS_2334 | Alcohol dehydrogenase. | Exonuclease III. | 0.779 |
MDS_1946 | MDS_2413 | MDS_1946 | MDS_2413 | Alcohol dehydrogenase. | ATP-dependent DNA ligase. | 0.512 |
MDS_1946 | MDS_4591 | MDS_1946 | MDS_4591 | Alcohol dehydrogenase. | A/G-specific DNA-adenine glycosylase; Adenine glycosylase active on G-A mispairs. | 0.459 |
MDS_1946 | MDS_4714 | MDS_1946 | MDS_4714 | Alcohol dehydrogenase. | Exodeoxyribonuclease III Xth. | 0.779 |
MDS_1946 | birA | MDS_1946 | MDS_4310 | Alcohol dehydrogenase. | Biotin--protein ligase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon. | 0.420 |
MDS_1946 | nth | MDS_1946 | MDS_1452 | Alcohol dehydrogenase. | DNA-(apurinic or apyrimidinic site) lyase / 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. | 0.533 |
MDS_1946 | polA | MDS_1946 | MDS_0170 | Alcohol dehydrogenase. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.682 |
MDS_2334 | MDS_0002 | MDS_2334 | MDS_0002 | Exonuclease 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 [...] | 0.777 |
MDS_2334 | MDS_1946 | MDS_2334 | MDS_1946 | Exonuclease III. | Alcohol dehydrogenase. | 0.779 |
MDS_2334 | MDS_2413 | MDS_2334 | MDS_2413 | Exonuclease III. | ATP-dependent DNA ligase. | 0.665 |
MDS_2334 | MDS_4591 | MDS_2334 | MDS_4591 | Exonuclease III. | A/G-specific DNA-adenine glycosylase; Adenine glycosylase active on G-A mispairs. | 0.760 |
MDS_2334 | MDS_4714 | MDS_2334 | MDS_4714 | Exonuclease III. | Exodeoxyribonuclease III Xth. | 0.918 |
MDS_2334 | birA | MDS_2334 | MDS_4310 | Exonuclease III. | Biotin--protein ligase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon. | 0.841 |
MDS_2334 | hfq | MDS_2334 | MDS_0709 | Exonuclease III. | RNA-binding protein Hfq; RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs. Belongs to the Hfq family. | 0.659 |