node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
asnS | dnaD | BSU22360 | BSU22350 | asparaginyl-tRNA synthetase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | DNA-remodelling primosomal protein; Probable component of primosome involved in the initiation of DNA replication. | 0.657 |
asnS | nth | BSU22360 | BSU22340 | asparaginyl-tRNA synthetase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; 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. | 0.645 |
asnS | polA | BSU22360 | BSU29090 | asparaginyl-tRNA synthetase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity. | 0.917 |
asnS | ypoC | BSU22360 | BSU22330 | asparaginyl-tRNA synthetase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. | 0.596 |
dnaD | asnS | BSU22350 | BSU22360 | DNA-remodelling primosomal protein; Probable component of primosome involved in the initiation of DNA replication. | asparaginyl-tRNA synthetase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | 0.657 |
dnaD | nth | BSU22350 | BSU22340 | DNA-remodelling primosomal protein; Probable component of primosome involved in the initiation of DNA replication. | 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. | 0.967 |
dnaD | yonN | BSU22350 | BSU21050 | DNA-remodelling primosomal protein; Probable component of primosome involved in the initiation of DNA replication. | Putative HU-related DNA-binding protein; Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions; Belongs to the bacterial histone-like protein family. | 0.500 |
dnaD | ypoC | BSU22350 | BSU22330 | DNA-remodelling primosomal protein; Probable component of primosome involved in the initiation of DNA replication. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. | 0.813 |
exoA | mutM | BSU40880 | BSU29080 | Apurinic/apyrimidinic endonuclease; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. | formamidopyrimidine-DNA glycosidase; Involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine, 8-oxo- dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions (By similarity). Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 8-oxo-dGTP. Has AP (apurinic/apyrimidi [...] | 0.407 |
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 |
mutM | exoA | BSU29080 | BSU40880 | formamidopyrimidine-DNA glycosidase; Involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine, 8-oxo- dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions (By similarity). Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 8-oxo-dGTP. Has AP (apurinic/apyrimidi [...] | Apurinic/apyrimidinic endonuclease; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. | 0.407 |
mutM | nfo | BSU29080 | BSU25130 | formamidopyrimidine-DNA glycosidase; Involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine, 8-oxo- dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions (By similarity). Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 8-oxo-dGTP. Has AP (apurinic/apyrimidi [...] | 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. | 0.893 |
mutM | nth | BSU29080 | BSU22340 | formamidopyrimidine-DNA glycosidase; Involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine, 8-oxo- dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions (By similarity). Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 8-oxo-dGTP. Has AP (apurinic/apyrimidi [...] | 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. | 0.973 |
mutM | polA | BSU29080 | BSU29090 | formamidopyrimidine-DNA glycosidase; Involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine, 8-oxo- dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions (By similarity). Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 8-oxo-dGTP. Has AP (apurinic/apyrimidi [...] | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity. | 0.996 |
mutM | polX | BSU29080 | BSU28590 | formamidopyrimidine-DNA glycosidase; Involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine, 8-oxo- dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions (By similarity). Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 8-oxo-dGTP. Has AP (apurinic/apyrimidi [...] | 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 [...] | 0.587 |
mutM | ung | BSU29080 | BSU37970 | formamidopyrimidine-DNA glycosidase; Involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine, 8-oxo- dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions (By similarity). Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 8-oxo-dGTP. Has AP (apurinic/apyrimidi [...] | 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. | 0.603 |