| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ampG | azo3976 | azo3975 | azo3976 | AmpG protein. Probably acts as a permease in the beta-lactamase induction system and in peptidoglycan recycling.Belong to the BT1 family of proteins. Presence of DUF domains and signail peptide. 11 tranmembrane helices.36% identity and 50% similarity to E.coli AmpG protein.(JW0423) 2A0125: AmpG-related permease; Family membership. | Probable uracil-DNA glycosylase. Has PF03167,Uracil DNA glycosylase superfamily;IPR005122 UDNA_glycsylseSF; Uracil-DNA glycosylase is a DNA repair enzyme that excises uracil residues from DNA by cleaving the N-glycosylic bond. Uracil in DNA can arise as a result of misincorportation of dUMP residues by DNA polymerase or deamination of cytosine. The sequence of uracil-DNA glycosylase is extremely well conserved. | 0.700 |
| azo0649 | azo3976 | azo0649 | azo3976 | Conserved hypothetical protein. Homology to ebA1795 of Azoarcus sp. EbN1 of 46% (gnl|keqq|eba:ebA1795(KEGG)). No domains predicted. No TMHs. | Probable uracil-DNA glycosylase. Has PF03167,Uracil DNA glycosylase superfamily;IPR005122 UDNA_glycsylseSF; Uracil-DNA glycosylase is a DNA repair enzyme that excises uracil residues from DNA by cleaving the N-glycosylic bond. Uracil in DNA can arise as a result of misincorportation of dUMP residues by DNA polymerase or deamination of cytosine. The sequence of uracil-DNA glycosylase is extremely well conserved. | 0.401 |
| azo1711 | azo3976 | azo1711 | azo3976 | Conserved hypothetical glycoprotease. Homology to yeaZ of N. europae of 41% (trembl|Q82US9). InterPro: Glycoprotease (M22) metallo-protease family (IPR000905). Tigrfam: gcp: metalloendopeptidase putative glycoprotease family. Pfam: Glyocprotease family. no signal peptide. no TMHs; Family membership. | Probable uracil-DNA glycosylase. Has PF03167,Uracil DNA glycosylase superfamily;IPR005122 UDNA_glycsylseSF; Uracil-DNA glycosylase is a DNA repair enzyme that excises uracil residues from DNA by cleaving the N-glycosylic bond. Uracil in DNA can arise as a result of misincorportation of dUMP residues by DNA polymerase or deamination of cytosine. The sequence of uracil-DNA glycosylase is extremely well conserved. | 0.477 |
| azo3976 | ampG | azo3976 | azo3975 | Probable uracil-DNA glycosylase. Has PF03167,Uracil DNA glycosylase superfamily;IPR005122 UDNA_glycsylseSF; Uracil-DNA glycosylase is a DNA repair enzyme that excises uracil residues from DNA by cleaving the N-glycosylic bond. Uracil in DNA can arise as a result of misincorportation of dUMP residues by DNA polymerase or deamination of cytosine. The sequence of uracil-DNA glycosylase is extremely well conserved. | AmpG protein. Probably acts as a permease in the beta-lactamase induction system and in peptidoglycan recycling.Belong to the BT1 family of proteins. Presence of DUF domains and signail peptide. 11 tranmembrane helices.36% identity and 50% similarity to E.coli AmpG protein.(JW0423) 2A0125: AmpG-related permease; Family membership. | 0.700 |
| azo3976 | azo0649 | azo3976 | azo0649 | Probable uracil-DNA glycosylase. Has PF03167,Uracil DNA glycosylase superfamily;IPR005122 UDNA_glycsylseSF; Uracil-DNA glycosylase is a DNA repair enzyme that excises uracil residues from DNA by cleaving the N-glycosylic bond. Uracil in DNA can arise as a result of misincorportation of dUMP residues by DNA polymerase or deamination of cytosine. The sequence of uracil-DNA glycosylase is extremely well conserved. | Conserved hypothetical protein. Homology to ebA1795 of Azoarcus sp. EbN1 of 46% (gnl|keqq|eba:ebA1795(KEGG)). No domains predicted. No TMHs. | 0.401 |
| azo3976 | azo1711 | azo3976 | azo1711 | Probable uracil-DNA glycosylase. Has PF03167,Uracil DNA glycosylase superfamily;IPR005122 UDNA_glycsylseSF; Uracil-DNA glycosylase is a DNA repair enzyme that excises uracil residues from DNA by cleaving the N-glycosylic bond. Uracil in DNA can arise as a result of misincorportation of dUMP residues by DNA polymerase or deamination of cytosine. The sequence of uracil-DNA glycosylase is extremely well conserved. | Conserved hypothetical glycoprotease. Homology to yeaZ of N. europae of 41% (trembl|Q82US9). InterPro: Glycoprotease (M22) metallo-protease family (IPR000905). Tigrfam: gcp: metalloendopeptidase putative glycoprotease family. Pfam: Glyocprotease family. no signal peptide. no TMHs; Family membership. | 0.477 |
| azo3976 | azo3977 | azo3976 | azo3977 | Probable uracil-DNA glycosylase. Has PF03167,Uracil DNA glycosylase superfamily;IPR005122 UDNA_glycsylseSF; Uracil-DNA glycosylase is a DNA repair enzyme that excises uracil residues from DNA by cleaving the N-glycosylic bond. Uracil in DNA can arise as a result of misincorportation of dUMP residues by DNA polymerase or deamination of cytosine. The sequence of uracil-DNA glycosylase is extremely well conserved. | Putative carbonic anhydrase; Reversible hydration of carbon dioxide. Belongs to the beta-class carbonic anhydrase family. | 0.465 |
| azo3976 | flgC | azo3976 | azo2739 | Probable uracil-DNA glycosylase. Has PF03167,Uracil DNA glycosylase superfamily;IPR005122 UDNA_glycsylseSF; Uracil-DNA glycosylase is a DNA repair enzyme that excises uracil residues from DNA by cleaving the N-glycosylic bond. Uracil in DNA can arise as a result of misincorportation of dUMP residues by DNA polymerase or deamination of cytosine. The sequence of uracil-DNA glycosylase is extremely well conserved. | Flagellar basal-body rod protein flgC. The rod has been shown to consist of four different, yet evolutionary related proteins: in the distal portion of the rod there are about 26 subunits of protein flgG and in the proximal portion there are about six subunits each of proteins flgB, flgC, and flgF. These four proteins contain a highly conserved asparagine-rich domain at their N terminus. InterPro: Flagella basal body rod protein no signal peptide no TMHs; High confidence in function and specificity. | 0.554 |
| azo3976 | ssb | azo3976 | azo3385 | Probable uracil-DNA glycosylase. Has PF03167,Uracil DNA glycosylase superfamily;IPR005122 UDNA_glycsylseSF; Uracil-DNA glycosylase is a DNA repair enzyme that excises uracil residues from DNA by cleaving the N-glycosylic bond. Uracil in DNA can arise as a result of misincorportation of dUMP residues by DNA polymerase or deamination of cytosine. The sequence of uracil-DNA glycosylase is extremely well conserved. | Single-strand DNA-binding protein; Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism. | 0.614 |
| azo3977 | azo3976 | azo3977 | azo3976 | Putative carbonic anhydrase; Reversible hydration of carbon dioxide. Belongs to the beta-class carbonic anhydrase family. | Probable uracil-DNA glycosylase. Has PF03167,Uracil DNA glycosylase superfamily;IPR005122 UDNA_glycsylseSF; Uracil-DNA glycosylase is a DNA repair enzyme that excises uracil residues from DNA by cleaving the N-glycosylic bond. Uracil in DNA can arise as a result of misincorportation of dUMP residues by DNA polymerase or deamination of cytosine. The sequence of uracil-DNA glycosylase is extremely well conserved. | 0.465 |
| flgC | azo3976 | azo2739 | azo3976 | Flagellar basal-body rod protein flgC. The rod has been shown to consist of four different, yet evolutionary related proteins: in the distal portion of the rod there are about 26 subunits of protein flgG and in the proximal portion there are about six subunits each of proteins flgB, flgC, and flgF. These four proteins contain a highly conserved asparagine-rich domain at their N terminus. InterPro: Flagella basal body rod protein no signal peptide no TMHs; High confidence in function and specificity. | Probable uracil-DNA glycosylase. Has PF03167,Uracil DNA glycosylase superfamily;IPR005122 UDNA_glycsylseSF; Uracil-DNA glycosylase is a DNA repair enzyme that excises uracil residues from DNA by cleaving the N-glycosylic bond. Uracil in DNA can arise as a result of misincorportation of dUMP residues by DNA polymerase or deamination of cytosine. The sequence of uracil-DNA glycosylase is extremely well conserved. | 0.554 |
| ssb | azo3976 | azo3385 | azo3976 | Single-strand DNA-binding protein; Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism. | Probable uracil-DNA glycosylase. Has PF03167,Uracil DNA glycosylase superfamily;IPR005122 UDNA_glycsylseSF; Uracil-DNA glycosylase is a DNA repair enzyme that excises uracil residues from DNA by cleaving the N-glycosylic bond. Uracil in DNA can arise as a result of misincorportation of dUMP residues by DNA polymerase or deamination of cytosine. The sequence of uracil-DNA glycosylase is extremely well conserved. | 0.614 |