node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CPQ89_01705 | xth | GCA_001953785_01444 | GCA_001953785_00081 | Unannotated protein. | Unannotated protein. | 0.745 |
CPQ89_02480 | CPQ89_05180 | GCA_001953785_01726 | GCA_001953785_00082 | Unannotated protein; 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 replication [...] | Unannotated protein. | 0.986 |
CPQ89_02480 | polA | GCA_001953785_01726 | GCA_001953785_00559 | Unannotated protein; 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 replication [...] | Unannotated protein; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.999 |
CPQ89_02480 | ung | GCA_001953785_01726 | GCA_001953785_00085 | Unannotated protein; 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 replication [...] | Unannotated protein; 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. | 0.841 |
CPQ89_02480 | xth | GCA_001953785_01726 | GCA_001953785_00081 | Unannotated protein; 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 replication [...] | Unannotated protein. | 0.950 |
CPQ89_05180 | CPQ89_02480 | GCA_001953785_00082 | GCA_001953785_01726 | Unannotated protein. | Unannotated protein; 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 replication [...] | 0.986 |
CPQ89_05180 | polA | GCA_001953785_00082 | GCA_001953785_00559 | Unannotated protein. | Unannotated protein; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.728 |
CPQ89_05180 | xth | GCA_001953785_00082 | GCA_001953785_00081 | Unannotated protein. | Unannotated protein. | 0.793 |
CPQ89_06325 | rpoZ | GCA_001953785_01131 | GCA_001953785_01376 | Unannotated protein; Belongs to the ArsC family. | Unannotated protein; Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits. | 0.752 |
CPQ89_06325 | xth | GCA_001953785_01131 | GCA_001953785_00081 | Unannotated protein; Belongs to the ArsC family. | Unannotated protein. | 0.767 |
birA | nth | GCA_001953785_00518 | GCA_001953785_01851 | Unannotated protein; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a repressor; Belongs to the biotin--protein ligase family. | Unannotated 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. | 0.502 |
birA | xth | GCA_001953785_00518 | GCA_001953785_00081 | Unannotated protein; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a repressor; Belongs to the biotin--protein ligase family. | Unannotated protein. | 0.821 |
nfo | nth | GCA_001953785_01952 | GCA_001953785_01851 | Unannotated protein; 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. | Unannotated 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. | 0.858 |
nfo | polA | GCA_001953785_01952 | GCA_001953785_00559 | Unannotated protein; 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. | Unannotated protein; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.664 |
nfo | ung | GCA_001953785_01952 | GCA_001953785_00085 | Unannotated protein; 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. | Unannotated protein; 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. | 0.724 |
nfo | xth | GCA_001953785_01952 | GCA_001953785_00081 | Unannotated protein; 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. | Unannotated protein. | 0.965 |
nth | birA | GCA_001953785_01851 | GCA_001953785_00518 | Unannotated 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. | Unannotated protein; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a repressor; Belongs to the biotin--protein ligase family. | 0.502 |
nth | nfo | GCA_001953785_01851 | GCA_001953785_01952 | Unannotated 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. | Unannotated protein; 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. | 0.858 |
nth | polA | GCA_001953785_01851 | GCA_001953785_00559 | Unannotated 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. | Unannotated protein; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.851 |
nth | ung | GCA_001953785_01851 | GCA_001953785_00085 | Unannotated 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. | Unannotated protein; 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. | 0.909 |