| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EKY27305.1 | EKY27398.1 | HMPREF0216_01469 | HMPREF0216_01431 | 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 of [...] | 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. | 0.410 |
| EKY27305.1 | dinB | HMPREF0216_01469 | HMPREF0216_03140 | 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 of [...] | ImpB/MucB/SamB family protein; 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. | 0.998 |
| EKY27305.1 | polA | HMPREF0216_01469 | HMPREF0216_02185 | 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 of [...] | DNA-directed DNA polymerase; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.999 |
| EKY27305.1 | sigA | HMPREF0216_01469 | HMPREF0216_02095 | 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 of [...] | 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. | 0.643 |
| EKY27396.1 | EKY27397.1 | HMPREF0216_01429 | HMPREF0216_01430 | Hypothetical protein. | Hypothetical protein. | 0.966 |
| EKY27396.1 | EKY27398.1 | HMPREF0216_01429 | HMPREF0216_01431 | Hypothetical protein. | 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. | 0.437 |
| EKY27397.1 | EKY27396.1 | HMPREF0216_01430 | HMPREF0216_01429 | Hypothetical protein. | Hypothetical protein. | 0.966 |
| EKY27397.1 | EKY27398.1 | HMPREF0216_01430 | HMPREF0216_01431 | Hypothetical protein. | 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. | 0.437 |
| EKY27398.1 | EKY27305.1 | HMPREF0216_01431 | HMPREF0216_01469 | 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. | 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 of [...] | 0.410 |
| EKY27398.1 | EKY27396.1 | HMPREF0216_01431 | HMPREF0216_01429 | 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. | Hypothetical protein. | 0.437 |
| EKY27398.1 | EKY27397.1 | HMPREF0216_01431 | HMPREF0216_01430 | 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. | Hypothetical protein. | 0.437 |
| EKY27398.1 | EKY28087.1 | HMPREF0216_01431 | HMPREF0216_00929 | 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. | AIG2-like family protein. | 0.745 |
| EKY27398.1 | EKY28170.1 | HMPREF0216_01431 | HMPREF0216_01013 | 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. | Putative iron-sulfur cluster-binding protein. | 0.794 |
| EKY27398.1 | EKY28580.1 | HMPREF0216_01431 | HMPREF0216_00633 | 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. | KEGG: cbt:CLH_0367 2.4e-111 8-oxoguanine DNA glycosylase; K03660 N-glycosylase/DNA lyase; Psort location: Cytoplasmic, score: 7.50. | 0.574 |
| EKY27398.1 | EKY29669.1 | HMPREF0216_01431 | HMPREF0216_00077 | 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. | Hypothetical protein; KEGG: lpl:lp_2906 2.5e-22 endA; DNA-entry nuclease K01173; Psort location: CytoplasmicMembrane, score: 10.00. | 0.472 |
| EKY27398.1 | dinB | HMPREF0216_01431 | HMPREF0216_03140 | 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. | ImpB/MucB/SamB family protein; 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. | 0.482 |
| EKY27398.1 | polA | HMPREF0216_01431 | HMPREF0216_02185 | 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. | DNA-directed DNA polymerase; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.541 |
| EKY27398.1 | sigA | HMPREF0216_01431 | HMPREF0216_02095 | 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. | 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. | 0.595 |
| EKY28087.1 | EKY27398.1 | HMPREF0216_00929 | HMPREF0216_01431 | AIG2-like family protein. | 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. | 0.745 |
| EKY28170.1 | EKY27398.1 | HMPREF0216_01013 | HMPREF0216_01431 | Putative iron-sulfur cluster-binding protein. | 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. | 0.794 |