| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AGB15795.1 | AGB17633.1 | Halru_1178 | Halru_3067 | DNA polymerase elongation subunit (family B); PFAM: DNA polymerase family B; DNA polymerase family B, exonuclease domain. | Secreted protein with C-terminal beta-propeller domain; PFAM: Beta propeller domain. | 0.503 |
| AGB15795.1 | dbh | Halru_1178 | Halru_1420 | DNA polymerase elongation subunit (family B); PFAM: DNA polymerase family B; DNA polymerase family B, exonuclease domain. | nucleotidyltransferase/DNA polymerase involved in DNA repair; 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. | 0.891 |
| AGB15795.1 | fen | Halru_1178 | Halru_0771 | DNA polymerase elongation subunit (family B); PFAM: DNA polymerase family B; DNA polymerase family B, exonuclease domain. | Flap structure-specific endonuclease; Structure-specific nuclease with 5'-flap endonuclease and 5'- 3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair [...] | 0.909 |
| AGB15795.1 | nfo | Halru_1178 | Halru_2377 | DNA polymerase elongation subunit (family B); PFAM: DNA polymerase family B; DNA polymerase family B, exonuclease domain. | 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. | 0.485 |
| AGB16328.1 | AGB16733.1 | Halru_1727 | Halru_2144 | Superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. | Thioredoxin reductase; PFAM: Pyridine nucleotide-disulphide oxidoreductase; Glutaredoxin; TIGRFAM: thioredoxin-disulfide reductase; Glutaredoxin, GrxC family. | 0.630 |
| AGB16328.1 | nfo | Halru_1727 | Halru_2377 | Superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. | 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. | 0.582 |
| AGB16503.1 | fen | Halru_1905 | Halru_0771 | Putative endoIII-related endonuclease; PFAM: HhH-GPD superfamily base excision DNA repair protein; Iron-sulfur binding domain of endonuclease III; Helix-hairpin-helix motif. | Flap structure-specific endonuclease; Structure-specific nuclease with 5'-flap endonuclease and 5'- 3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair [...] | 0.481 |
| AGB16503.1 | nfo | Halru_1905 | Halru_2377 | Putative endoIII-related endonuclease; PFAM: HhH-GPD superfamily base excision DNA repair protein; Iron-sulfur binding domain of endonuclease III; Helix-hairpin-helix motif. | 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. | 0.661 |
| AGB16503.1 | nth | Halru_1905 | Halru_0777 | Putative endoIII-related endonuclease; PFAM: HhH-GPD superfamily base excision DNA repair protein; Iron-sulfur binding domain of endonuclease III; Helix-hairpin-helix motif. | 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. | 0.919 |
| AGB16733.1 | AGB16328.1 | Halru_2144 | Halru_1727 | Thioredoxin reductase; PFAM: Pyridine nucleotide-disulphide oxidoreductase; Glutaredoxin; TIGRFAM: thioredoxin-disulfide reductase; Glutaredoxin, GrxC family. | Superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. | 0.630 |
| AGB16733.1 | fen | Halru_2144 | Halru_0771 | Thioredoxin reductase; PFAM: Pyridine nucleotide-disulphide oxidoreductase; Glutaredoxin; TIGRFAM: thioredoxin-disulfide reductase; Glutaredoxin, GrxC family. | Flap structure-specific endonuclease; Structure-specific nuclease with 5'-flap endonuclease and 5'- 3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair [...] | 0.482 |
| AGB16733.1 | nfo | Halru_2144 | Halru_2377 | Thioredoxin reductase; PFAM: Pyridine nucleotide-disulphide oxidoreductase; Glutaredoxin; TIGRFAM: thioredoxin-disulfide reductase; Glutaredoxin, GrxC family. | 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. | 0.488 |
| AGB16961.1 | AGB16963.1 | Halru_2376 | Halru_2378 | PFAM: Biotin/lipoate A/B protein ligase family. | Methylase involved in ubiquinone/menaquinone biosynthesis; PFAM: Methyltransferase domain. | 0.503 |
| AGB16961.1 | nfo | Halru_2376 | Halru_2377 | PFAM: Biotin/lipoate A/B protein ligase family. | 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. | 0.581 |
| AGB16963.1 | AGB16961.1 | Halru_2378 | Halru_2376 | Methylase involved in ubiquinone/menaquinone biosynthesis; PFAM: Methyltransferase domain. | PFAM: Biotin/lipoate A/B protein ligase family. | 0.503 |
| AGB16963.1 | nfo | Halru_2378 | Halru_2377 | Methylase involved in ubiquinone/menaquinone biosynthesis; PFAM: Methyltransferase domain. | 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. | 0.672 |
| AGB17633.1 | AGB15795.1 | Halru_3067 | Halru_1178 | Secreted protein with C-terminal beta-propeller domain; PFAM: Beta propeller domain. | DNA polymerase elongation subunit (family B); PFAM: DNA polymerase family B; DNA polymerase family B, exonuclease domain. | 0.503 |
| AGB17633.1 | dbh | Halru_3067 | Halru_1420 | Secreted protein with C-terminal beta-propeller domain; PFAM: Beta propeller domain. | nucleotidyltransferase/DNA polymerase involved in DNA repair; 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. | 0.441 |
| AGB17633.1 | fen | Halru_3067 | Halru_0771 | Secreted protein with C-terminal beta-propeller domain; PFAM: Beta propeller domain. | Flap structure-specific endonuclease; Structure-specific nuclease with 5'-flap endonuclease and 5'- 3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair [...] | 0.942 |
| AGB17633.1 | nfo | Halru_3067 | Halru_2377 | Secreted protein with C-terminal beta-propeller domain; PFAM: Beta propeller domain. | 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. | 0.633 |
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