| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AKA39560.1 | AKA39562.1 | UGYR_15020 | UGYR_15030 | Anti-anti-sigma factor; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the anti-sigma-factor antagonist family. | Serine/threonine protein kinase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.998 |
| AKA39560.1 | AKA39915.1 | UGYR_15020 | UGYR_05220 | Anti-anti-sigma factor; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the anti-sigma-factor antagonist family. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.724 |
| AKA39560.1 | bfr | UGYR_15020 | UGYR_11315 | Anti-anti-sigma factor; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the anti-sigma-factor antagonist family. | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | 0.753 |
| AKA39562.1 | AKA39560.1 | UGYR_15030 | UGYR_15020 | Serine/threonine protein kinase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Anti-anti-sigma factor; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the anti-sigma-factor antagonist family. | 0.998 |
| AKA39562.1 | bfr | UGYR_15030 | UGYR_11315 | Serine/threonine protein kinase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | 0.443 |
| AKA39915.1 | AKA39560.1 | UGYR_05220 | UGYR_15020 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Anti-anti-sigma factor; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the anti-sigma-factor antagonist family. | 0.724 |
| AKA39915.1 | bfr | UGYR_05220 | UGYR_11315 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | 0.684 |
| bfr | AKA39560.1 | UGYR_11315 | UGYR_15020 | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | Anti-anti-sigma factor; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the anti-sigma-factor antagonist family. | 0.753 |
| bfr | AKA39562.1 | UGYR_11315 | UGYR_15030 | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | Serine/threonine protein kinase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.443 |
| bfr | AKA39915.1 | UGYR_11315 | UGYR_05220 | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.684 |
| bfr | dps | UGYR_11315 | UGYR_15950 | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | DNA starvation/stationary phase protection protein Dps; During stationary phase, binds the chromosome non- specifically, forming a highly ordered and stable dps-DNA co-crystal within which chromosomal DNA is condensed and protected from diverse damages. It protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral, which can be released after reduction. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction; Belongs to the Dps family. | 0.534 |
| bfr | glcA | UGYR_11315 | UGYR_00315 | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | PTS glucose-specific subunit IIBC; Phosphoenolpyruvate-dependent sugar phosphotransferase system; catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane; IIB is phosphorylated by IIA and then transfers the phosphoryl group to the sugar; IIC forms the translocation channel; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.470 |
| bfr | hcr | UGYR_11315 | UGYR_16350 | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | HCP oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.505 |
| bfr | hemH | UGYR_11315 | UGYR_14730 | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. | 0.916 |
| bfr | nuoD | UGYR_11315 | UGYR_04790 | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | NADH:ubiquinone oxidoreductase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the C-terminal section; belongs to the complex I 49 kDa subunit family. | 0.510 |
| bfr | pheS | UGYR_11315 | UGYR_02530 | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | phenylalanyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. | 0.445 |
| bfr | psiF | UGYR_11315 | UGYR_15620 | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | Phosphate starvation-inducible protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.477 |
| dps | bfr | UGYR_15950 | UGYR_11315 | DNA starvation/stationary phase protection protein Dps; During stationary phase, binds the chromosome non- specifically, forming a highly ordered and stable dps-DNA co-crystal within which chromosomal DNA is condensed and protected from diverse damages. It protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral, which can be released after reduction. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction; Belongs to the Dps family. | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | 0.534 |
| glcA | bfr | UGYR_00315 | UGYR_11315 | PTS glucose-specific subunit IIBC; Phosphoenolpyruvate-dependent sugar phosphotransferase system; catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane; IIB is phosphorylated by IIA and then transfers the phosphoryl group to the sugar; IIC forms the translocation channel; Derived by automated computational analysis using gene prediction method: Protein Homology. | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | 0.470 |
| hcr | bfr | UGYR_16350 | UGYR_11315 | HCP oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | 0.505 |
