| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| SCL46070.1 | SCL48288.1 | GA0070617_0136 | GA0070617_0831 | DNA polymerase-3 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 re [...] | Exonuclease III. | 0.893 |
| SCL46070.1 | SCL53291.1 | GA0070617_0136 | GA0070617_2326 | DNA polymerase-3 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 re [...] | Exodeoxyribonuclease-3. | 0.893 |
| SCL46070.1 | SCL60513.1 | GA0070617_0136 | GA0070617_4402 | DNA polymerase-3 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 re [...] | DNA polymerase III beta subunit, C-terminal domain. | 0.927 |
| SCL46070.1 | ung | GA0070617_0136 | GA0070617_5117 | DNA polymerase-3 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 re [...] | 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. | 0.826 |
| SCL48288.1 | SCL46070.1 | GA0070617_0831 | GA0070617_0136 | Exonuclease III. | DNA polymerase-3 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 re [...] | 0.893 |
| SCL48288.1 | SCL53291.1 | GA0070617_0831 | GA0070617_2326 | Exonuclease III. | Exodeoxyribonuclease-3. | 0.732 |
| SCL48288.1 | SCL60513.1 | GA0070617_0831 | GA0070617_4402 | Exonuclease III. | DNA polymerase III beta subunit, C-terminal domain. | 0.900 |
| SCL48288.1 | nth | GA0070617_0831 | GA0070617_5631 | Exonuclease 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. | 0.863 |
| SCL48288.1 | ung | GA0070617_0831 | GA0070617_5117 | Exonuclease 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. | 0.892 |
| SCL53291.1 | SCL46070.1 | GA0070617_2326 | GA0070617_0136 | Exodeoxyribonuclease-3. | DNA polymerase-3 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 re [...] | 0.893 |
| SCL53291.1 | SCL48288.1 | GA0070617_2326 | GA0070617_0831 | Exodeoxyribonuclease-3. | Exonuclease III. | 0.732 |
| SCL53291.1 | SCL60513.1 | GA0070617_2326 | GA0070617_4402 | Exodeoxyribonuclease-3. | DNA polymerase III beta subunit, C-terminal domain. | 0.900 |
| SCL53291.1 | nth | GA0070617_2326 | GA0070617_5631 | Exodeoxyribonuclease-3. | 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. | 0.863 |
| SCL53291.1 | ung | GA0070617_2326 | GA0070617_5117 | Exodeoxyribonuclease-3. | 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. | 0.892 |
| SCL58628.1 | SCL65783.1 | GA0070617_3871 | GA0070617_5865 | Phenazine biosynthesis protein phzE. | Phenazine biosynthesis protein phzE. | 0.999 |
| SCL58628.1 | ung | GA0070617_3871 | GA0070617_5117 | Phenazine biosynthesis protein phzE. | 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. | 0.640 |
| SCL60513.1 | SCL46070.1 | GA0070617_4402 | GA0070617_0136 | DNA polymerase III beta subunit, C-terminal domain. | DNA polymerase-3 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 re [...] | 0.927 |
| SCL60513.1 | SCL48288.1 | GA0070617_4402 | GA0070617_0831 | DNA polymerase III beta subunit, C-terminal domain. | Exonuclease III. | 0.900 |
| SCL60513.1 | SCL53291.1 | GA0070617_4402 | GA0070617_2326 | DNA polymerase III beta subunit, C-terminal domain. | Exodeoxyribonuclease-3. | 0.900 |
| SCL60513.1 | ung | GA0070617_4402 | GA0070617_5117 | DNA polymerase III beta subunit, C-terminal domain. | 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. | 0.830 |