node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SHE50042.1 | SHF77191.1 | SAMN04488522_101383 | SAMN04488522_103604 | Exodeoxyribonuclease-3. | DNA-3-methyladenine glycosylase II. | 0.804 |
SHE50042.1 | SHG75714.1 | SAMN04488522_101383 | SAMN04488522_107164 | Exodeoxyribonuclease-3. | Exodeoxyribonuclease-3. | 0.807 |
SHE50042.1 | polA | SAMN04488522_101383 | SAMN04488522_10792 | Exodeoxyribonuclease-3. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.854 |
SHE60973.1 | SHE74417.1 | SAMN04488522_101700 | SAMN04488522_1011077 | 5'-nucleotidase, C-terminal domain. | Methylated-DNA--protein-cysteine methyltransferase; 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. Belongs to the MGMT family. | 0.479 |
SHE60973.1 | SHF74982.1 | SAMN04488522_101700 | SAMN04488522_103533 | 5'-nucleotidase, C-terminal domain. | Purine-nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. | 0.785 |
SHE60973.1 | SHF77191.1 | SAMN04488522_101700 | SAMN04488522_103604 | 5'-nucleotidase, C-terminal domain. | DNA-3-methyladenine glycosylase II. | 0.500 |
SHE60973.1 | surE | SAMN04488522_101700 | SAMN04488522_10260 | 5'-nucleotidase, C-terminal domain. | 5'-nucleotidase /3'-nucleotidase; Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates; Belongs to the SurE nucleotidase family. | 0.450 |
SHE74417.1 | SHE60973.1 | SAMN04488522_1011077 | SAMN04488522_101700 | Methylated-DNA--protein-cysteine methyltransferase; 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. Belongs to the MGMT family. | 5'-nucleotidase, C-terminal domain. | 0.479 |
SHE74417.1 | SHF74982.1 | SAMN04488522_1011077 | SAMN04488522_103533 | Methylated-DNA--protein-cysteine methyltransferase; 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. Belongs to the MGMT family. | Purine-nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. | 0.557 |
SHE74417.1 | SHF77191.1 | SAMN04488522_1011077 | SAMN04488522_103604 | Methylated-DNA--protein-cysteine methyltransferase; 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. Belongs to the MGMT family. | DNA-3-methyladenine glycosylase II. | 0.798 |
SHE74417.1 | polA | SAMN04488522_1011077 | SAMN04488522_10792 | Methylated-DNA--protein-cysteine methyltransferase; 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. Belongs to the MGMT family. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.623 |
SHE74417.1 | surE | SAMN04488522_1011077 | SAMN04488522_10260 | Methylated-DNA--protein-cysteine methyltransferase; 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. Belongs to the MGMT family. | 5'-nucleotidase /3'-nucleotidase; Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates; Belongs to the SurE nucleotidase family. | 0.608 |
SHF29500.1 | SHF77191.1 | SAMN04488522_102740 | SAMN04488522_103604 | Metal binding domain of Ada. | DNA-3-methyladenine glycosylase II. | 0.576 |
SHF29500.1 | surE | SAMN04488522_102740 | SAMN04488522_10260 | Metal binding domain of Ada. | 5'-nucleotidase /3'-nucleotidase; Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates; Belongs to the SurE nucleotidase family. | 0.524 |
SHF69715.1 | SHF77191.1 | SAMN04488522_103360 | SAMN04488522_103604 | Exonuclease III. | DNA-3-methyladenine glycosylase II. | 0.804 |
SHF69715.1 | polA | SAMN04488522_103360 | SAMN04488522_10792 | Exonuclease III. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. | 0.854 |
SHF74982.1 | SHE60973.1 | SAMN04488522_103533 | SAMN04488522_101700 | Purine-nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. | 5'-nucleotidase, C-terminal domain. | 0.785 |
SHF74982.1 | SHE74417.1 | SAMN04488522_103533 | SAMN04488522_1011077 | Purine-nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. | Methylated-DNA--protein-cysteine methyltransferase; 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. Belongs to the MGMT family. | 0.557 |
SHF74982.1 | SHF77191.1 | SAMN04488522_103533 | SAMN04488522_103604 | Purine-nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. | DNA-3-methyladenine glycosylase II. | 0.609 |
SHF74982.1 | surE | SAMN04488522_103533 | SAMN04488522_10260 | Purine-nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. | 5'-nucleotidase /3'-nucleotidase; Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates; Belongs to the SurE nucleotidase family. | 0.887 |