node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
KDR94545.1 | ogt | CLIT_14c00060 | CLIT_8c00190 | 51.5 kDa protein. | methylated-DNA--protein-cysteine methyltransferase Ogt; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | 0.434 |
KDR95110.1 | ogt | CLIT_11c01390 | CLIT_8c00190 | uracil-DNA glycosylase-like protein. | methylated-DNA--protein-cysteine methyltransferase Ogt; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | 0.403 |
KDR95816.1 | ogt | CLIT_10c05440 | CLIT_8c00190 | GntR family transcriptional regulator. | methylated-DNA--protein-cysteine methyltransferase Ogt; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | 0.402 |
KDR95849.1 | ogt | CLIT_8c00180 | CLIT_8c00190 | Hypothetical protein. | methylated-DNA--protein-cysteine methyltransferase Ogt; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | 0.570 |
dinB | ogt | CLIT_2c03030 | CLIT_8c00190 | DNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. | methylated-DNA--protein-cysteine methyltransferase Ogt; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | 0.527 |
htrA | nnr | CLIT_4c01760 | CLIT_5c00490 | Putative serine protease HtrA. | Bifunctional NAD(P)H-hydrate repair enzyme Nnr; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to al [...] | 0.428 |
htrA | ogt | CLIT_4c01760 | CLIT_8c00190 | Putative serine protease HtrA. | methylated-DNA--protein-cysteine methyltransferase Ogt; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | 0.400 |
mucD | nnr | CLIT_10c01350 | CLIT_5c00490 | Putative periplasmic serine endoprotease DegP. | Bifunctional NAD(P)H-hydrate repair enzyme Nnr; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to al [...] | 0.428 |
mucD | ogt | CLIT_10c01350 | CLIT_8c00190 | Putative periplasmic serine endoprotease DegP. | methylated-DNA--protein-cysteine methyltransferase Ogt; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | 0.400 |
nnr | htrA | CLIT_5c00490 | CLIT_4c01760 | Bifunctional NAD(P)H-hydrate repair enzyme Nnr; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to al [...] | Putative serine protease HtrA. | 0.428 |
nnr | mucD | CLIT_5c00490 | CLIT_10c01350 | Bifunctional NAD(P)H-hydrate repair enzyme Nnr; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to al [...] | Putative periplasmic serine endoprotease DegP. | 0.428 |
nnr | ogt | CLIT_5c00490 | CLIT_8c00190 | Bifunctional NAD(P)H-hydrate repair enzyme Nnr; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to al [...] | methylated-DNA--protein-cysteine methyltransferase Ogt; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | 0.416 |
ogt | KDR94545.1 | CLIT_8c00190 | CLIT_14c00060 | methylated-DNA--protein-cysteine methyltransferase Ogt; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | 51.5 kDa protein. | 0.434 |
ogt | KDR95110.1 | CLIT_8c00190 | CLIT_11c01390 | methylated-DNA--protein-cysteine methyltransferase Ogt; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | uracil-DNA glycosylase-like protein. | 0.403 |
ogt | KDR95816.1 | CLIT_8c00190 | CLIT_10c05440 | methylated-DNA--protein-cysteine methyltransferase Ogt; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | GntR family transcriptional regulator. | 0.402 |
ogt | KDR95849.1 | CLIT_8c00190 | CLIT_8c00180 | methylated-DNA--protein-cysteine methyltransferase Ogt; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | Hypothetical protein. | 0.570 |
ogt | dinB | CLIT_8c00190 | CLIT_2c03030 | methylated-DNA--protein-cysteine methyltransferase Ogt; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | DNA polymerase IV; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. | 0.527 |
ogt | htrA | CLIT_8c00190 | CLIT_4c01760 | methylated-DNA--protein-cysteine methyltransferase Ogt; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | Putative serine protease HtrA. | 0.400 |
ogt | mucD | CLIT_8c00190 | CLIT_10c01350 | methylated-DNA--protein-cysteine methyltransferase Ogt; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | Putative periplasmic serine endoprotease DegP. | 0.400 |
ogt | nnr | CLIT_8c00190 | CLIT_5c00490 | methylated-DNA--protein-cysteine methyltransferase Ogt; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. | Bifunctional NAD(P)H-hydrate repair enzyme Nnr; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to al [...] | 0.416 |