| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ACF07400.1 | dnaN | MARTH_orf613 | MARTH_orf003 | 5'-3' exonuclease, exo domain of DNA polymerase I. | DNA polymerase III, beta subunit. | 0.999 |
| ACF07400.1 | fpg | MARTH_orf613 | MARTH_orf656 | 5'-3' exonuclease, exo domain of DNA polymerase I. | formamidopyrimidine-DNA glycosylase, MutM; Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. | 0.982 |
| ACF07400.1 | nfo | MARTH_orf613 | MARTH_orf342 | 5'-3' exonuclease, exo domain of DNA polymerase I. | Endonuclease IV; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate. | 0.821 |
| ACF07400.1 | ung | MARTH_orf613 | MARTH_orf815 | 5'-3' exonuclease, exo domain of DNA polymerase I. | uracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | 0.806 |
| dnaN | ACF07400.1 | MARTH_orf003 | MARTH_orf613 | DNA polymerase III, beta subunit. | 5'-3' exonuclease, exo domain of DNA polymerase I. | 0.999 |
| dnaN | ung | MARTH_orf003 | MARTH_orf815 | DNA polymerase III, beta subunit. | uracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | 0.900 |
| fmt | pepA1 | MARTH_orf816 | MARTH_orf812 | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | Leucyl aminopeptidase; Belongs to the peptidase M17 family. | 0.400 |
| fmt | pepA2 | MARTH_orf816 | MARTH_orf813 | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | Leucyl aminopeptidase; Belongs to the peptidase M17 family. | 0.400 |
| fmt | ung | MARTH_orf816 | MARTH_orf815 | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | uracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | 0.690 |
| fpg | ACF07400.1 | MARTH_orf656 | MARTH_orf613 | formamidopyrimidine-DNA glycosylase, MutM; Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. | 5'-3' exonuclease, exo domain of DNA polymerase I. | 0.982 |
| fpg | nfo | MARTH_orf656 | MARTH_orf342 | formamidopyrimidine-DNA glycosylase, MutM; Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. | Endonuclease IV; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate. | 0.498 |
| fpg | ung | MARTH_orf656 | MARTH_orf815 | formamidopyrimidine-DNA glycosylase, MutM; Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. | uracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | 0.604 |
| ldh | ung | MARTH_orf109 | MARTH_orf815 | L-lactate dehydrogenase; Belongs to the LDH/MDH superfamily. | uracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | 0.437 |
| nfo | ACF07400.1 | MARTH_orf342 | MARTH_orf613 | Endonuclease IV; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate. | 5'-3' exonuclease, exo domain of DNA polymerase I. | 0.821 |
| nfo | fpg | MARTH_orf342 | MARTH_orf656 | Endonuclease IV; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate. | formamidopyrimidine-DNA glycosylase, MutM; Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. | 0.498 |
| nfo | ung | MARTH_orf342 | MARTH_orf815 | Endonuclease IV; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate. | uracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | 0.576 |
| pepA1 | fmt | MARTH_orf812 | MARTH_orf816 | Leucyl aminopeptidase; Belongs to the peptidase M17 family. | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | 0.400 |
| pepA1 | pepA2 | MARTH_orf812 | MARTH_orf813 | Leucyl aminopeptidase; Belongs to the peptidase M17 family. | Leucyl aminopeptidase; Belongs to the peptidase M17 family. | 0.978 |
| pepA1 | ung | MARTH_orf812 | MARTH_orf815 | Leucyl aminopeptidase; Belongs to the peptidase M17 family. | uracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | 0.466 |
| pepA2 | fmt | MARTH_orf813 | MARTH_orf816 | Leucyl aminopeptidase; Belongs to the peptidase M17 family. | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | 0.400 |