| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Coch_0371 | Coch_1451 | Coch_0371 | Coch_1451 | KEGG: fjo:Fjoh_1310 DNA polymerase III, alpha subunit; TIGRFAM: DNA polymerase III, alpha subunit; PFAM: DNA polymerase III alpha subunit; Exonuclease RNase T and DNA polymerase III; PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; SMART: phosphoesterase PHP domain protein; Exonuclease. | KEGG: fjo:Fjoh_0832 exodeoxyribonuclease III Xth; TIGRFAM: exodeoxyribonuclease III Xth; exodeoxyribonuclease III; PFAM: Endonuclease/exonuclease/phosphatase. | 0.421 |
| Coch_0371 | Coch_1752 | Coch_0371 | Coch_1752 | KEGG: fjo:Fjoh_1310 DNA polymerase III, alpha subunit; TIGRFAM: DNA polymerase III, alpha subunit; PFAM: DNA polymerase III alpha subunit; Exonuclease RNase T and DNA polymerase III; PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; SMART: phosphoesterase PHP domain protein; Exonuclease. | 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 [...] | 0.997 |
| Coch_0371 | nth | Coch_0371 | Coch_2158 | KEGG: fjo:Fjoh_1310 DNA polymerase III, alpha subunit; TIGRFAM: DNA polymerase III, alpha subunit; PFAM: DNA polymerase III alpha subunit; Exonuclease RNase T and DNA polymerase III; PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; SMART: phosphoesterase PHP domain protein; Exonuclease. | 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. | 0.457 |
| Coch_0371 | polA | Coch_0371 | Coch_1092 | KEGG: fjo:Fjoh_1310 DNA polymerase III, alpha subunit; TIGRFAM: DNA polymerase III, alpha subunit; PFAM: DNA polymerase III alpha subunit; Exonuclease RNase T and DNA polymerase III; PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; SMART: phosphoesterase PHP domain protein; Exonuclease. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.796 |
| Coch_0371 | ung | Coch_0371 | Coch_2033 | KEGG: fjo:Fjoh_1310 DNA polymerase III, alpha subunit; TIGRFAM: DNA polymerase III, alpha subunit; PFAM: DNA polymerase III alpha subunit; Exonuclease RNase T and DNA polymerase III; PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; SMART: phosphoesterase PHP domain protein; Exonuclease. | 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. | 0.413 |
| Coch_1451 | Coch_0371 | Coch_1451 | Coch_0371 | KEGG: fjo:Fjoh_0832 exodeoxyribonuclease III Xth; TIGRFAM: exodeoxyribonuclease III Xth; exodeoxyribonuclease III; PFAM: Endonuclease/exonuclease/phosphatase. | KEGG: fjo:Fjoh_1310 DNA polymerase III, alpha subunit; TIGRFAM: DNA polymerase III, alpha subunit; PFAM: DNA polymerase III alpha subunit; Exonuclease RNase T and DNA polymerase III; PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; SMART: phosphoesterase PHP domain protein; Exonuclease. | 0.421 |
| Coch_1451 | Coch_1752 | Coch_1451 | Coch_1752 | KEGG: fjo:Fjoh_0832 exodeoxyribonuclease III Xth; TIGRFAM: exodeoxyribonuclease III Xth; exodeoxyribonuclease III; PFAM: Endonuclease/exonuclease/phosphatase. | 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 [...] | 0.831 |
| Coch_1451 | dut | Coch_1451 | Coch_0751 | KEGG: fjo:Fjoh_0832 exodeoxyribonuclease III Xth; TIGRFAM: exodeoxyribonuclease III Xth; exodeoxyribonuclease III; PFAM: Endonuclease/exonuclease/phosphatase. | Deoxyuridine 5'-triphosphate nucleotidohydrolase Dut; This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA; Belongs to the dUTPase family. | 0.447 |
| Coch_1451 | nth | Coch_1451 | Coch_2158 | KEGG: fjo:Fjoh_0832 exodeoxyribonuclease III Xth; TIGRFAM: exodeoxyribonuclease III Xth; exodeoxyribonuclease III; PFAM: Endonuclease/exonuclease/phosphatase. | 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. | 0.987 |
| Coch_1451 | polA | Coch_1451 | Coch_1092 | KEGG: fjo:Fjoh_0832 exodeoxyribonuclease III Xth; TIGRFAM: exodeoxyribonuclease III Xth; exodeoxyribonuclease III; PFAM: Endonuclease/exonuclease/phosphatase. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.848 |
| Coch_1451 | ung | Coch_1451 | Coch_2033 | KEGG: fjo:Fjoh_0832 exodeoxyribonuclease III Xth; TIGRFAM: exodeoxyribonuclease III Xth; exodeoxyribonuclease III; PFAM: Endonuclease/exonuclease/phosphatase. | 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. | 0.680 |
| Coch_1752 | Coch_0371 | Coch_1752 | Coch_0371 | 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 [...] | KEGG: fjo:Fjoh_1310 DNA polymerase III, alpha subunit; TIGRFAM: DNA polymerase III, alpha subunit; PFAM: DNA polymerase III alpha subunit; Exonuclease RNase T and DNA polymerase III; PHP domain protein; nucleic acid binding OB-fold tRNA/helicase-type; SMART: phosphoesterase PHP domain protein; Exonuclease. | 0.997 |
| Coch_1752 | Coch_1451 | Coch_1752 | Coch_1451 | 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 [...] | KEGG: fjo:Fjoh_0832 exodeoxyribonuclease III Xth; TIGRFAM: exodeoxyribonuclease III Xth; exodeoxyribonuclease III; PFAM: Endonuclease/exonuclease/phosphatase. | 0.831 |
| Coch_1752 | dut | Coch_1752 | Coch_0751 | 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 [...] | Deoxyuridine 5'-triphosphate nucleotidohydrolase Dut; This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA; Belongs to the dUTPase family. | 0.684 |
| Coch_1752 | polA | Coch_1752 | Coch_1092 | 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. | 0.994 |
| Coch_1752 | ung | Coch_1752 | Coch_2033 | 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. | 0.713 |
| Coch_2032 | Coch_2034 | Coch_2032 | Coch_2034 | KEGG: smu:SMU.1208c hypothetical protein. | PFAM: ribonuclease BN; KEGG: gfo:GFO_1103 ribonuclease BN. | 0.439 |
| Coch_2032 | polA | Coch_2032 | Coch_1092 | KEGG: smu:SMU.1208c 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. | 0.404 |
| Coch_2032 | priA | Coch_2032 | Coch_2035 | KEGG: smu:SMU.1208c hypothetical protein. | Transcriptional regulator, TrmB; Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA; Belongs to the helicase family. PriA subfamily. | 0.455 |
| Coch_2032 | ung | Coch_2032 | Coch_2033 | KEGG: smu:SMU.1208c hypothetical 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. | 0.773 |