node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
EEG76427.1 | EEG76442.1 | DealDRAFT_2664 | DealDRAFT_2679 | TIGRFAM: DNA ligase D, 3'-phosphoesterase domain protein; KEGG: fjo:Fjoh_3303 ATP dependent DNA ligase. | PFAM: PHP domain protein; SMART: phosphoesterase PHP domain protein; KEGG: drm:Dred_1634 PHP C-terminal domain protein. | 0.982 |
EEG76427.1 | EEG76920.1 | DealDRAFT_2664 | DealDRAFT_2181 | TIGRFAM: DNA ligase D, 3'-phosphoesterase domain protein; KEGG: fjo:Fjoh_3303 ATP dependent DNA ligase. | 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 [...] | 0.978 |
EEG76427.1 | EEG77988.1 | DealDRAFT_2664 | DealDRAFT_1287 | TIGRFAM: DNA ligase D, 3'-phosphoesterase domain protein; KEGG: fjo:Fjoh_3303 ATP dependent DNA ligase. | TIGRFAM: exodeoxyribonuclease III; exodeoxyribonuclease III Xth; PFAM: Endonuclease/exonuclease/phosphatase; KEGG: sul:SYO3AOP1_1609 exodeoxyribonuclease III Xth. | 0.978 |
EEG76427.1 | EEG78240.1 | DealDRAFT_2664 | DealDRAFT_1117 | TIGRFAM: DNA ligase D, 3'-phosphoesterase domain protein; KEGG: fjo:Fjoh_3303 ATP dependent DNA ligase. | TIGRFAM: DNA polymerase LigD, ligase domain protein; PFAM: ATP dependent DNA ligase domain protein; ATP dependent DNA ligase; KEGG: sth:STH1797 ATP-dependent DNA ligase. | 0.986 |
EEG76427.1 | nfo | DealDRAFT_2664 | DealDRAFT_3029 | TIGRFAM: DNA ligase D, 3'-phosphoesterase domain protein; KEGG: fjo:Fjoh_3303 ATP dependent DNA ligase. | Apurinic endonuclease Apn1; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to produce new 5'-ends that are base-free deoxyribose 5-phosphate residues. It preferentially attacks modified AP sites created by bleomycin and neocarzinostatin. | 0.483 |
EEG76427.1 | nth | DealDRAFT_2664 | DealDRAFT_0481 | TIGRFAM: DNA ligase D, 3'-phosphoesterase domain protein; KEGG: fjo:Fjoh_3303 ATP dependent DNA ligase. | 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. | 0.436 |
EEG76427.1 | polA | DealDRAFT_2664 | DealDRAFT_2375 | TIGRFAM: DNA ligase D, 3'-phosphoesterase domain protein; KEGG: fjo:Fjoh_3303 ATP dependent DNA ligase. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.983 |
EEG76440.1 | EEG76442.1 | DealDRAFT_2677 | DealDRAFT_2679 | KEGG: pth:PTH_1946 3-methyladenine DNA glycosylase; TIGRFAM: DNA-3-methyladenine glycosylase; PFAM: methylpurine-DNA glycosylase (MPG); Belongs to the DNA glycosylase MPG family. | PFAM: PHP domain protein; SMART: phosphoesterase PHP domain protein; KEGG: drm:Dred_1634 PHP C-terminal domain protein. | 0.501 |
EEG76440.1 | EEG77988.1 | DealDRAFT_2677 | DealDRAFT_1287 | KEGG: pth:PTH_1946 3-methyladenine DNA glycosylase; TIGRFAM: DNA-3-methyladenine glycosylase; PFAM: methylpurine-DNA glycosylase (MPG); Belongs to the DNA glycosylase MPG family. | TIGRFAM: exodeoxyribonuclease III; exodeoxyribonuclease III Xth; PFAM: Endonuclease/exonuclease/phosphatase; KEGG: sul:SYO3AOP1_1609 exodeoxyribonuclease III Xth. | 0.877 |
EEG76440.1 | tadA | DealDRAFT_2677 | DealDRAFT_2912 | KEGG: pth:PTH_1946 3-methyladenine DNA glycosylase; TIGRFAM: DNA-3-methyladenine glycosylase; PFAM: methylpurine-DNA glycosylase (MPG); Belongs to the DNA glycosylase MPG family. | CMP/dCMP deaminase zinc-binding; Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2); Belongs to the cytidine and deoxycytidylate deaminase family. | 0.724 |
EEG76442.1 | EEG76427.1 | DealDRAFT_2679 | DealDRAFT_2664 | PFAM: PHP domain protein; SMART: phosphoesterase PHP domain protein; KEGG: drm:Dred_1634 PHP C-terminal domain protein. | TIGRFAM: DNA ligase D, 3'-phosphoesterase domain protein; KEGG: fjo:Fjoh_3303 ATP dependent DNA ligase. | 0.982 |
EEG76442.1 | EEG76440.1 | DealDRAFT_2679 | DealDRAFT_2677 | PFAM: PHP domain protein; SMART: phosphoesterase PHP domain protein; KEGG: drm:Dred_1634 PHP C-terminal domain protein. | KEGG: pth:PTH_1946 3-methyladenine DNA glycosylase; TIGRFAM: DNA-3-methyladenine glycosylase; PFAM: methylpurine-DNA glycosylase (MPG); Belongs to the DNA glycosylase MPG family. | 0.501 |
EEG76442.1 | EEG76920.1 | DealDRAFT_2679 | DealDRAFT_2181 | PFAM: PHP domain protein; SMART: phosphoesterase PHP domain protein; KEGG: drm:Dred_1634 PHP C-terminal domain protein. | 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 [...] | 0.834 |
EEG76442.1 | EEG77988.1 | DealDRAFT_2679 | DealDRAFT_1287 | PFAM: PHP domain protein; SMART: phosphoesterase PHP domain protein; KEGG: drm:Dred_1634 PHP C-terminal domain protein. | TIGRFAM: exodeoxyribonuclease III; exodeoxyribonuclease III Xth; PFAM: Endonuclease/exonuclease/phosphatase; KEGG: sul:SYO3AOP1_1609 exodeoxyribonuclease III Xth. | 0.999 |
EEG76442.1 | EEG78240.1 | DealDRAFT_2679 | DealDRAFT_1117 | PFAM: PHP domain protein; SMART: phosphoesterase PHP domain protein; KEGG: drm:Dred_1634 PHP C-terminal domain protein. | TIGRFAM: DNA polymerase LigD, ligase domain protein; PFAM: ATP dependent DNA ligase domain protein; ATP dependent DNA ligase; KEGG: sth:STH1797 ATP-dependent DNA ligase. | 0.953 |
EEG76442.1 | nfo | DealDRAFT_2679 | DealDRAFT_3029 | PFAM: PHP domain protein; SMART: phosphoesterase PHP domain protein; KEGG: drm:Dred_1634 PHP C-terminal domain protein. | Apurinic endonuclease Apn1; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to produce new 5'-ends that are base-free deoxyribose 5-phosphate residues. It preferentially attacks modified AP sites created by bleomycin and neocarzinostatin. | 0.459 |
EEG76442.1 | nth | DealDRAFT_2679 | DealDRAFT_0481 | PFAM: PHP domain protein; SMART: phosphoesterase PHP domain protein; KEGG: drm:Dred_1634 PHP C-terminal domain protein. | 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. | 0.649 |
EEG76442.1 | polA | DealDRAFT_2679 | DealDRAFT_2375 | PFAM: PHP domain protein; SMART: phosphoesterase PHP domain protein; KEGG: drm:Dred_1634 PHP C-terminal domain protein. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.981 |
EEG76920.1 | EEG76427.1 | DealDRAFT_2181 | DealDRAFT_2664 | 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 [...] | TIGRFAM: DNA ligase D, 3'-phosphoesterase domain protein; KEGG: fjo:Fjoh_3303 ATP dependent DNA ligase. | 0.978 |
EEG76920.1 | EEG76442.1 | DealDRAFT_2181 | DealDRAFT_2679 | 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 [...] | PFAM: PHP domain protein; SMART: phosphoesterase PHP domain protein; KEGG: drm:Dred_1634 PHP C-terminal domain protein. | 0.834 |