| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| VC_1672 | VC_A1017 | VC_1672 | VC_A1017 | DNA-3-methyladenine glycosidase I; Similar to SP:P05100 GB:J02606 GB:X03845 PID:147920 PID:43030; identified by sequence similarity; putative. | methylated-DNA--protein-cysteine S-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. | 0.786 |
| VC_1672 | VC_A1018 | VC_1672 | VC_A1018 | DNA-3-methyladenine glycosidase I; Similar to SP:P05100 GB:J02606 GB:X03845 PID:147920 PID:43030; identified by sequence similarity; putative. | Ada regulatory protein; Similar to SP:Q10630 PID:1340083 PID:1513196 GB:AL123456; identified by sequence similarity; putative. | 0.564 |
| VC_A1016 | VC_A1017 | VC_A1016 | VC_A1017 | Hypothetical protein; Identified by Glimmer2; putative. | methylated-DNA--protein-cysteine S-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. | 0.847 |
| VC_A1016 | VC_A1018 | VC_A1016 | VC_A1018 | Hypothetical protein; Identified by Glimmer2; putative. | Ada regulatory protein; Similar to SP:Q10630 PID:1340083 PID:1513196 GB:AL123456; identified by sequence similarity; putative. | 0.847 |
| VC_A1017 | VC_1672 | VC_A1017 | VC_1672 | methylated-DNA--protein-cysteine S-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. | DNA-3-methyladenine glycosidase I; Similar to SP:P05100 GB:J02606 GB:X03845 PID:147920 PID:43030; identified by sequence similarity; putative. | 0.786 |
| VC_A1017 | VC_A1016 | VC_A1017 | VC_A1016 | methylated-DNA--protein-cysteine S-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. | Hypothetical protein; Identified by Glimmer2; putative. | 0.847 |
| VC_A1017 | VC_A1018 | VC_A1017 | VC_A1018 | methylated-DNA--protein-cysteine S-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. | Ada regulatory protein; Similar to SP:Q10630 PID:1340083 PID:1513196 GB:AL123456; identified by sequence similarity; putative. | 0.997 |
| VC_A1017 | dnaN | VC_A1017 | VC_0013 | methylated-DNA--protein-cysteine S-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. | DNA polymerase III, beta chain; 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 of r [...] | 0.662 |
| VC_A1017 | lpxB | VC_A1017 | VC_2247 | methylated-DNA--protein-cysteine S-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. | lipid-A-disaccharide synthase; Condensation of UDP-2,3-diacylglucosamine and 2,3- diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. | 0.648 |
| VC_A1017 | mdh | VC_A1017 | VC_0432 | methylated-DNA--protein-cysteine S-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. | Malate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate. | 0.508 |
| VC_A1017 | queG | VC_A1017 | VC_0342 | methylated-DNA--protein-cysteine S-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. | Iron-sulfur cluster-binding protein; Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr); Belongs to the QueG family. | 0.514 |
| VC_A1017 | rpoD | VC_A1017 | VC_0517 | methylated-DNA--protein-cysteine S-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. | RNA polymerase sigma factor RpoD; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth. | 0.540 |
| VC_A1017 | rpoH | VC_A1017 | VC_0150 | methylated-DNA--protein-cysteine S-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. | RNA polymerase sigma-32 factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of expression of heat shock genes. | 0.540 |
| VC_A1017 | rpoS | VC_A1017 | VC_0534 | methylated-DNA--protein-cysteine S-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. | RNA polymerase sigma-38 factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the master transcriptional regulator of the stationary phase and the general stress response (By similarity). May be required for the persistence of V.cholerae in aquatic habitats. | 0.544 |
| VC_A1018 | VC_1672 | VC_A1018 | VC_1672 | Ada regulatory protein; Similar to SP:Q10630 PID:1340083 PID:1513196 GB:AL123456; identified by sequence similarity; putative. | DNA-3-methyladenine glycosidase I; Similar to SP:P05100 GB:J02606 GB:X03845 PID:147920 PID:43030; identified by sequence similarity; putative. | 0.564 |
| VC_A1018 | VC_A1016 | VC_A1018 | VC_A1016 | Ada regulatory protein; Similar to SP:Q10630 PID:1340083 PID:1513196 GB:AL123456; identified by sequence similarity; putative. | Hypothetical protein; Identified by Glimmer2; putative. | 0.847 |
| VC_A1018 | VC_A1017 | VC_A1018 | VC_A1017 | Ada regulatory protein; Similar to SP:Q10630 PID:1340083 PID:1513196 GB:AL123456; identified by sequence similarity; putative. | methylated-DNA--protein-cysteine S-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. | 0.997 |
| VC_A1018 | rpoD | VC_A1018 | VC_0517 | Ada regulatory protein; Similar to SP:Q10630 PID:1340083 PID:1513196 GB:AL123456; identified by sequence similarity; putative. | RNA polymerase sigma factor RpoD; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth. | 0.521 |
| VC_A1018 | rpoH | VC_A1018 | VC_0150 | Ada regulatory protein; Similar to SP:Q10630 PID:1340083 PID:1513196 GB:AL123456; identified by sequence similarity; putative. | RNA polymerase sigma-32 factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of expression of heat shock genes. | 0.521 |
| VC_A1018 | rpoS | VC_A1018 | VC_0534 | Ada regulatory protein; Similar to SP:Q10630 PID:1340083 PID:1513196 GB:AL123456; identified by sequence similarity; putative. | RNA polymerase sigma-38 factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the master transcriptional regulator of the stationary phase and the general stress response (By similarity). May be required for the persistence of V.cholerae in aquatic habitats. | 0.521 |