| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ligB | polA | BSU20500 | BSU29090 | Bacteriophage SPbeta DNA ligase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type h: extrachromosomal origin; Belongs to the ATP-dependent DNA ligase family. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity. | 0.882 |
| ligB | polC | BSU20500 | BSU16580 | Bacteriophage SPbeta DNA ligase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type h: extrachromosomal origin; Belongs to the ATP-dependent DNA ligase family. | DNA polymerase III (alpha subunit); Required for replicative DNA synthesis. This DNA polymerase also exhibits 3' to 5' exonuclease activity; Belongs to the DNA polymerase type-C family. PolC subfamily. | 0.484 |
| ligB | polX | BSU20500 | BSU28590 | Bacteriophage SPbeta DNA ligase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type h: extrachromosomal origin; Belongs to the ATP-dependent DNA ligase family. | DNA polymerase/3'-5' exonuclease X; Strictly DNA-template-directed DNA polymerase, preferentially acting on DNA structures containing gaps from one to a few nucleotides and bearing a phosphate group at the 5' end of the downstream DNA. The fact that PolX is able to conduct filling of a single-nucleotide gap, allowing further sealing of the resulting nick by a DNA ligase, points to a putative role in base excision repair (BER) during the B.subtilis life cycle. Moreover, also possesses a 3'-5' exonuclease activity able to edit unpaired 3'-termini in a gapped DNA substrate and likely invo [...] | 0.813 |
| ligB | ykoU | BSU20500 | BSU13400 | Bacteriophage SPbeta DNA ligase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type h: extrachromosomal origin; Belongs to the ATP-dependent DNA ligase family. | ATP-dependent DNA ligase subunit; With Ku forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity (Probable). Probably involved in DNA repair during spore germination. In the N-terminal section; belongs to the LigD polymerase family. | 0.938 |
| mutSB | polA | BSU28580 | BSU29090 | Putative DNA mismatch repair enzyme; Endonuclease that is involved in the suppression of homologous recombination and may therefore have a key role in the control of bacterial genetic diversity; Belongs to the DNA mismatch repair MutS family. MutS2 subfamily. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity. | 0.633 |
| mutSB | polX | BSU28580 | BSU28590 | Putative DNA mismatch repair enzyme; Endonuclease that is involved in the suppression of homologous recombination and may therefore have a key role in the control of bacterial genetic diversity; Belongs to the DNA mismatch repair MutS family. MutS2 subfamily. | DNA polymerase/3'-5' exonuclease X; Strictly DNA-template-directed DNA polymerase, preferentially acting on DNA structures containing gaps from one to a few nucleotides and bearing a phosphate group at the 5' end of the downstream DNA. The fact that PolX is able to conduct filling of a single-nucleotide gap, allowing further sealing of the resulting nick by a DNA ligase, points to a putative role in base excision repair (BER) during the B.subtilis life cycle. Moreover, also possesses a 3'-5' exonuclease activity able to edit unpaired 3'-termini in a gapped DNA substrate and likely invo [...] | 0.979 |
| mutSB | yshA | BSU28580 | BSU28610 | Putative DNA mismatch repair enzyme; Endonuclease that is involved in the suppression of homologous recombination and may therefore have a key role in the control of bacterial genetic diversity; Belongs to the DNA mismatch repair MutS family. MutS2 subfamily. | Conserved hypothetical protein; Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division (By similarity); Belongs to the ZapA family. Type 2 subfamily. | 0.735 |
| mutSB | yshB | BSU28580 | BSU28600 | Putative DNA mismatch repair enzyme; Endonuclease that is involved in the suppression of homologous recombination and may therefore have a key role in the control of bacterial genetic diversity; Belongs to the DNA mismatch repair MutS family. MutS2 subfamily. | Putative integral membrane protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component. | 0.826 |
| mutSB | yshE | BSU28580 | BSU28570 | Putative DNA mismatch repair enzyme; Endonuclease that is involved in the suppression of homologous recombination and may therefore have a key role in the control of bacterial genetic diversity; Belongs to the DNA mismatch repair MutS family. MutS2 subfamily. | Putative integral inner membrane protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component. | 0.931 |
| nfo | nth | BSU25130 | BSU22340 | Type IV apurinic/apyrimidinic endonuclease; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate. | 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; Belongs to the Nth/MutY family. | 0.983 |
| nfo | polA | BSU25130 | BSU29090 | Type IV apurinic/apyrimidinic endonuclease; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity. | 0.862 |
| nfo | polX | BSU25130 | BSU28590 | Type IV apurinic/apyrimidinic endonuclease; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate. | DNA polymerase/3'-5' exonuclease X; Strictly DNA-template-directed DNA polymerase, preferentially acting on DNA structures containing gaps from one to a few nucleotides and bearing a phosphate group at the 5' end of the downstream DNA. The fact that PolX is able to conduct filling of a single-nucleotide gap, allowing further sealing of the resulting nick by a DNA ligase, points to a putative role in base excision repair (BER) during the B.subtilis life cycle. Moreover, also possesses a 3'-5' exonuclease activity able to edit unpaired 3'-termini in a gapped DNA substrate and likely invo [...] | 0.812 |
| nfo | ykoU | BSU25130 | BSU13400 | Type IV apurinic/apyrimidinic endonuclease; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate. | ATP-dependent DNA ligase subunit; With Ku forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity (Probable). Probably involved in DNA repair during spore germination. In the N-terminal section; belongs to the LigD polymerase family. | 0.781 |
| nth | nfo | BSU22340 | BSU25130 | 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; Belongs to the Nth/MutY family. | Type IV apurinic/apyrimidinic endonuclease; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate. | 0.983 |
| nth | polA | BSU22340 | BSU29090 | 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; Belongs to the Nth/MutY family. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity. | 0.848 |
| nth | polX | BSU22340 | BSU28590 | 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; Belongs to the Nth/MutY family. | DNA polymerase/3'-5' exonuclease X; Strictly DNA-template-directed DNA polymerase, preferentially acting on DNA structures containing gaps from one to a few nucleotides and bearing a phosphate group at the 5' end of the downstream DNA. The fact that PolX is able to conduct filling of a single-nucleotide gap, allowing further sealing of the resulting nick by a DNA ligase, points to a putative role in base excision repair (BER) during the B.subtilis life cycle. Moreover, also possesses a 3'-5' exonuclease activity able to edit unpaired 3'-termini in a gapped DNA substrate and likely invo [...] | 0.792 |
| nth | ykoU | BSU22340 | BSU13400 | 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; Belongs to the Nth/MutY family. | ATP-dependent DNA ligase subunit; With Ku forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity (Probable). Probably involved in DNA repair during spore germination. In the N-terminal section; belongs to the LigD polymerase family. | 0.541 |
| polA | ligB | BSU29090 | BSU20500 | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity. | Bacteriophage SPbeta DNA ligase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type h: extrachromosomal origin; Belongs to the ATP-dependent DNA ligase family. | 0.882 |
| polA | mutSB | BSU29090 | BSU28580 | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity. | Putative DNA mismatch repair enzyme; Endonuclease that is involved in the suppression of homologous recombination and may therefore have a key role in the control of bacterial genetic diversity; Belongs to the DNA mismatch repair MutS family. MutS2 subfamily. | 0.633 |
| polA | nfo | BSU29090 | BSU25130 | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity. | Type IV apurinic/apyrimidinic endonuclease; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate. | 0.862 |