| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Swit_0585 | ung | Swit_0585 | Swit_3206 | TIGRFAM: alkylphosphonate utilization operon protein PhnA; PFAM: PhnA protein-like. | 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. | 0.529 |
| Swit_2795 | Swit_3788 | Swit_2795 | Swit_3788 | 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 [...] | TIGRFAM: exodeoxyribonuclease III Xth; PFAM: Endonuclease/exonuclease/phosphatase. | 0.791 |
| Swit_2795 | Swit_3911 | Swit_2795 | Swit_3911 | 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 [...] | TIGRFAM: exodeoxyribonuclease III; exodeoxyribonuclease III Xth; PFAM: Endonuclease/exonuclease/phosphatase. | 0.791 |
| Swit_2795 | dut | Swit_2795 | Swit_4879 | 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; 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. | 0.873 |
| Swit_2795 | recA | Swit_2795 | Swit_0512 | 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 [...] | recA protein; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family. | 0.890 |
| Swit_2795 | ung | Swit_2795 | Swit_3206 | 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. | 0.775 |
| Swit_3205 | Swit_3207 | Swit_3205 | Swit_3207 | PFAM: GCN5-related N-acetyltransferase. | Hypothetical protein. | 0.567 |
| Swit_3205 | ung | Swit_3205 | Swit_3206 | PFAM: GCN5-related N-acetyltransferase. | 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. | 0.777 |
| Swit_3207 | Swit_3205 | Swit_3207 | Swit_3205 | Hypothetical protein. | PFAM: GCN5-related N-acetyltransferase. | 0.567 |
| Swit_3207 | recA | Swit_3207 | Swit_0512 | Hypothetical protein. | recA protein; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family. | 0.414 |
| Swit_3207 | ung | Swit_3207 | Swit_3206 | 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. | 0.590 |
| Swit_3788 | Swit_2795 | Swit_3788 | Swit_2795 | TIGRFAM: exodeoxyribonuclease III Xth; 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 [...] | 0.791 |
| Swit_3788 | Swit_3911 | Swit_3788 | Swit_3911 | TIGRFAM: exodeoxyribonuclease III Xth; PFAM: Endonuclease/exonuclease/phosphatase. | TIGRFAM: exodeoxyribonuclease III; exodeoxyribonuclease III Xth; PFAM: Endonuclease/exonuclease/phosphatase. | 0.923 |
| Swit_3788 | dut | Swit_3788 | Swit_4879 | TIGRFAM: exodeoxyribonuclease III Xth; PFAM: Endonuclease/exonuclease/phosphatase. | Deoxyuridine 5'-triphosphate nucleotidohydrolase; 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. | 0.416 |
| Swit_3788 | nth | Swit_3788 | Swit_0203 | TIGRFAM: exodeoxyribonuclease III Xth; PFAM: Endonuclease/exonuclease/phosphatase. | Endonuclease 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. | 0.827 |
| Swit_3788 | recA | Swit_3788 | Swit_0512 | TIGRFAM: exodeoxyribonuclease III Xth; PFAM: Endonuclease/exonuclease/phosphatase. | recA protein; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family. | 0.483 |
| Swit_3788 | ung | Swit_3788 | Swit_3206 | TIGRFAM: exodeoxyribonuclease III Xth; 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. | 0.585 |
| Swit_3911 | Swit_2795 | Swit_3911 | Swit_2795 | TIGRFAM: exodeoxyribonuclease III; exodeoxyribonuclease III Xth; 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 [...] | 0.791 |
| Swit_3911 | Swit_3788 | Swit_3911 | Swit_3788 | TIGRFAM: exodeoxyribonuclease III; exodeoxyribonuclease III Xth; PFAM: Endonuclease/exonuclease/phosphatase. | TIGRFAM: exodeoxyribonuclease III Xth; PFAM: Endonuclease/exonuclease/phosphatase. | 0.923 |
| Swit_3911 | dut | Swit_3911 | Swit_4879 | TIGRFAM: exodeoxyribonuclease III; exodeoxyribonuclease III Xth; PFAM: Endonuclease/exonuclease/phosphatase. | Deoxyuridine 5'-triphosphate nucleotidohydrolase; 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. | 0.416 |