node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
EFS24594.2 | EFS27189.2 | FUAG_00109 | FUAG_02704 | DNA-3-methyladenine glycosylase; Belongs to the DNA glycosylase MPG family. | Hypothetical protein. | 0.497 |
EFS24594.2 | xth | FUAG_00109 | FUAG_02812 | DNA-3-methyladenine glycosylase; Belongs to the DNA glycosylase MPG family. | Exodeoxyribonuclease III (xth). | 0.762 |
EFS26022.1 | xth | FUAG_01537 | FUAG_02812 | Pseudouridine synthase; Belongs to the pseudouridine synthase RsuA family. | Exodeoxyribonuclease III (xth). | 0.679 |
EFS27189.2 | EFS24594.2 | FUAG_02704 | FUAG_00109 | Hypothetical protein. | DNA-3-methyladenine glycosylase; Belongs to the DNA glycosylase MPG family. | 0.497 |
EFS27189.2 | nfo | FUAG_02704 | FUAG_02110 | Hypothetical protein. | Apurinic endonuclease (APN1); 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. | 0.456 |
EFS27189.2 | nth | FUAG_02704 | FUAG_03015 | Hypothetical protein. | 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. | 0.474 |
EFS27189.2 | polA | FUAG_02704 | FUAG_01977 | Hypothetical 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. | 0.713 |
EFS27189.2 | xth | FUAG_02704 | FUAG_02812 | Hypothetical protein. | Exodeoxyribonuclease III (xth). | 0.898 |
EFS27298.1 | xth | FUAG_02813 | FUAG_02812 | Hypothetical protein. | Exodeoxyribonuclease III (xth). | 0.768 |
dnaN | dnaN-2 | FUAG_01401 | FUAG_01901 | 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 [...] | DNA polymerase III, beta subunit. | 0.916 |
dnaN | polA | FUAG_01401 | FUAG_01977 | 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 [...] | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.999 |
dnaN | ung | FUAG_01401 | FUAG_00934 | 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; 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. | 0.609 |
dnaN | xth | FUAG_01401 | FUAG_02812 | 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 (xth). | 0.824 |
dnaN-2 | dnaN | FUAG_01901 | FUAG_01401 | DNA polymerase III, beta subunit. | 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 [...] | 0.916 |
dnaN-2 | polA | FUAG_01901 | FUAG_01977 | DNA polymerase III, beta subunit. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.999 |
dnaN-2 | ung | FUAG_01901 | FUAG_00934 | DNA polymerase III, beta subunit. | 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. | 0.609 |
dnaN-2 | xth | FUAG_01901 | FUAG_02812 | DNA polymerase III, beta subunit. | Exodeoxyribonuclease III (xth). | 0.824 |
nfo | EFS27189.2 | FUAG_02110 | FUAG_02704 | Apurinic endonuclease (APN1); 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. | Hypothetical protein. | 0.456 |
nfo | nth | FUAG_02110 | FUAG_03015 | Apurinic endonuclease (APN1); 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. | 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. | 0.747 |
nfo | polA | FUAG_02110 | FUAG_01977 | Apurinic endonuclease (APN1); 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. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.488 |