| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| RMCC_2110 | RMCC_2111 | RMCC_2110 | RMCC_2111 | Uncharacterized protein. | AsnC family transcriptional regulator. | 0.843 |
| RMCC_2110 | thiL | RMCC_2110 | RMCC_2112 | Uncharacterized protein. | Thiamine monophosphate kinase; Catalyzes the ATP-dependent phosphorylation of thiamine- monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1; Belongs to the thiamine-monophosphate kinase family. | 0.667 |
| RMCC_2110 | ung | RMCC_2110 | RMCC_2113 | Uncharacterized protein. | 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. | 0.642 |
| RMCC_2111 | RMCC_2110 | RMCC_2111 | RMCC_2110 | AsnC family transcriptional regulator. | Uncharacterized protein. | 0.843 |
| RMCC_2111 | thiL | RMCC_2111 | RMCC_2112 | AsnC family transcriptional regulator. | Thiamine monophosphate kinase; Catalyzes the ATP-dependent phosphorylation of thiamine- monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1; Belongs to the thiamine-monophosphate kinase family. | 0.632 |
| RMCC_2111 | ung | RMCC_2111 | RMCC_2113 | AsnC family transcriptional regulator. | 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. | 0.560 |
| RMCC_3547 | RMCC_4727 | RMCC_3547 | RMCC_4727 | 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 protein XthA. | 0.952 |
| RMCC_3547 | RMCC_6092 | RMCC_3547 | RMCC_6092 | 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. | 0.952 |
| RMCC_3547 | ung | RMCC_3547 | RMCC_2113 | 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. | 0.855 |
| RMCC_3945 | ung | RMCC_3945 | RMCC_2113 | Aminopeptidase N pepN. | 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. | 0.563 |
| RMCC_4148 | RMCC_4727 | RMCC_4148 | RMCC_4727 | Endonuclease IV. | Exodeoxyribonuclease III protein XthA. | 0.936 |
| RMCC_4148 | RMCC_6092 | RMCC_4148 | RMCC_6092 | Endonuclease IV. | Exodeoxyribonuclease III. | 0.928 |
| RMCC_4148 | nth | RMCC_4148 | RMCC_3851 | Endonuclease IV. | Ultraviolet N-glycosylase/AP 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. | 0.821 |
| RMCC_4148 | ung | RMCC_4148 | RMCC_2113 | Endonuclease IV. | 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. | 0.677 |
| RMCC_4727 | RMCC_3547 | RMCC_4727 | RMCC_3547 | Exodeoxyribonuclease III protein XthA. | 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 [...] | 0.952 |
| RMCC_4727 | RMCC_4148 | RMCC_4727 | RMCC_4148 | Exodeoxyribonuclease III protein XthA. | Endonuclease IV. | 0.936 |
| RMCC_4727 | RMCC_6092 | RMCC_4727 | RMCC_6092 | Exodeoxyribonuclease III protein XthA. | Exodeoxyribonuclease III. | 0.916 |
| RMCC_4727 | nth | RMCC_4727 | RMCC_3851 | Exodeoxyribonuclease III protein XthA. | Ultraviolet N-glycosylase/AP 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. | 0.866 |
| RMCC_4727 | ung | RMCC_4727 | RMCC_2113 | Exodeoxyribonuclease III protein XthA. | 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. | 0.883 |
| RMCC_6092 | RMCC_3547 | RMCC_6092 | RMCC_3547 | Exodeoxyribonuclease 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 [...] | 0.952 |