node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
birA | exoA | BSU22440 | BSU40880 | Biotin acetyl-CoA-carboxylase ligase and biotin regulon repressor; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a repressor; Belongs to the biotin--protein ligase family. | Apurinic/apyrimidinic endonuclease; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. | 0.875 |
birA | mutY | BSU22440 | BSU08630 | Biotin acetyl-CoA-carboxylase ligase and biotin regulon repressor; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a repressor; Belongs to the biotin--protein ligase family. | A/G-specific adenine glycosylase or DNA-(apurinic or apyrimidinic site) lyase; Base excision repair (BER) glycosylase that initiates repair of A:oxoG to C:G by removing the inappropriately paired adenine base from the DNA backbone, generating an abasic site product. 8-oxoguanine (oxoG) is a genotoxic DNA lesion resulting from oxidation of guanine; this residue is misread by replicative DNA polymerases, that insert adenine instead of cytosine opposite the oxidized damaged base. Shows a powerful dicrimination of A versus C, since it does not cleave cytosine in oxoG:C pairs. May also be a [...] | 0.480 |
dnaN | exoA | BSU00020 | BSU40880 | 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 o [...] | Apurinic/apyrimidinic endonuclease; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. | 0.898 |
dnaN | mutY | BSU00020 | BSU08630 | 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 o [...] | A/G-specific adenine glycosylase or DNA-(apurinic or apyrimidinic site) lyase; Base excision repair (BER) glycosylase that initiates repair of A:oxoG to C:G by removing the inappropriately paired adenine base from the DNA backbone, generating an abasic site product. 8-oxoguanine (oxoG) is a genotoxic DNA lesion resulting from oxidation of guanine; this residue is misread by replicative DNA polymerases, that insert adenine instead of cytosine opposite the oxidized damaged base. Shows a powerful dicrimination of A versus C, since it does not cleave cytosine in oxoG:C pairs. May also be a [...] | 0.497 |
dnaN | polA | BSU00020 | BSU29090 | 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 o [...] | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity. | 0.998 |
dnaN | polX | BSU00020 | BSU28590 | 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 o [...] | 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 [...] | 0.624 |
dnaN | ung | BSU00020 | BSU37970 | 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 o [...] | 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; Belongs to the uracil-DNA glycosylase (UDG) superfamily. UNG family. | 0.742 |
dnaN | ykoU | BSU00020 | BSU13400 | 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 o [...] | 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. | 0.909 |
exoA | birA | BSU40880 | BSU22440 | Apurinic/apyrimidinic endonuclease; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. | Biotin acetyl-CoA-carboxylase ligase and biotin regulon repressor; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a repressor; Belongs to the biotin--protein ligase family. | 0.875 |
exoA | dnaN | BSU40880 | BSU00020 | Apurinic/apyrimidinic endonuclease; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. | 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 o [...] | 0.898 |
exoA | mutY | BSU40880 | BSU08630 | Apurinic/apyrimidinic endonuclease; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. | A/G-specific adenine glycosylase or DNA-(apurinic or apyrimidinic site) lyase; Base excision repair (BER) glycosylase that initiates repair of A:oxoG to C:G by removing the inappropriately paired adenine base from the DNA backbone, generating an abasic site product. 8-oxoguanine (oxoG) is a genotoxic DNA lesion resulting from oxidation of guanine; this residue is misread by replicative DNA polymerases, that insert adenine instead of cytosine opposite the oxidized damaged base. Shows a powerful dicrimination of A versus C, since it does not cleave cytosine in oxoG:C pairs. May also be a [...] | 0.835 |
exoA | nfo | BSU40880 | BSU25130 | Apurinic/apyrimidinic endonuclease; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. | 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. | 0.927 |
exoA | nth | BSU40880 | BSU22340 | Apurinic/apyrimidinic endonuclease; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. | 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. | 0.993 |
exoA | polA | BSU40880 | BSU29090 | Apurinic/apyrimidinic endonuclease; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity. | 0.844 |
exoA | polX | BSU40880 | BSU28590 | Apurinic/apyrimidinic endonuclease; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. | 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 [...] | 0.898 |
exoA | ung | BSU40880 | BSU37970 | Apurinic/apyrimidinic endonuclease; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. | 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; Belongs to the uracil-DNA glycosylase (UDG) superfamily. UNG family. | 0.910 |
exoA | ykoU | BSU40880 | BSU13400 | Apurinic/apyrimidinic endonuclease; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. | 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. | 0.848 |
exoA | ytzG | BSU40880 | BSU30035 | Apurinic/apyrimidinic endonuclease; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. | Putative 16S pseudouridylate synthase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.848 |
mutY | birA | BSU08630 | BSU22440 | A/G-specific adenine glycosylase or DNA-(apurinic or apyrimidinic site) lyase; Base excision repair (BER) glycosylase that initiates repair of A:oxoG to C:G by removing the inappropriately paired adenine base from the DNA backbone, generating an abasic site product. 8-oxoguanine (oxoG) is a genotoxic DNA lesion resulting from oxidation of guanine; this residue is misread by replicative DNA polymerases, that insert adenine instead of cytosine opposite the oxidized damaged base. Shows a powerful dicrimination of A versus C, since it does not cleave cytosine in oxoG:C pairs. May also be a [...] | Biotin acetyl-CoA-carboxylase ligase and biotin regulon repressor; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a repressor; Belongs to the biotin--protein ligase family. | 0.480 |
mutY | dnaN | BSU08630 | BSU00020 | A/G-specific adenine glycosylase or DNA-(apurinic or apyrimidinic site) lyase; Base excision repair (BER) glycosylase that initiates repair of A:oxoG to C:G by removing the inappropriately paired adenine base from the DNA backbone, generating an abasic site product. 8-oxoguanine (oxoG) is a genotoxic DNA lesion resulting from oxidation of guanine; this residue is misread by replicative DNA polymerases, that insert adenine instead of cytosine opposite the oxidized damaged base. Shows a powerful dicrimination of A versus C, since it does not cleave cytosine in oxoG:C pairs. May also be a [...] | 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 o [...] | 0.497 |