| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CAZ98561.1 | CAZ98563.1 | ZOBELLIA_4426 | ZOBELLIA_4428 | Conserved hypothetical protein; Localized in the cytoplasm. | Protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. The active site of the metallo-beta-lactamase domain is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | 0.790 |
| CAZ98561.1 | CAZ98564.1 | ZOBELLIA_4426 | ZOBELLIA_4429 | Conserved hypothetical protein; Localized in the cytoplasm. | Pseudogene of protein; This protein corresponds to a central fragment of an hypothetical protein from Kordia algicida and is likely an inactive pseudogene; Localized in the cytoplasm; Hypothetical protein. | 0.540 |
| CAZ98561.1 | CAZ98565.1 | ZOBELLIA_4426 | ZOBELLIA_4430 | Conserved hypothetical protein; Localized in the cytoplasm. | Putative protein. | 0.505 |
| CAZ98561.1 | dpsA4 | ZOBELLIA_4426 | ZOBELLIA_4427 | Conserved hypothetical protein; Localized in the cytoplasm. | DNA protection during starvation protein; Dsp protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction; Forms a homododecamer and the 12 subunits form a hollow sphere into which the mineral iron core of up to 500 Fe(3+) can be deposited; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the Dps family. | 0.762 |
| CAZ98563.1 | CAZ98561.1 | ZOBELLIA_4428 | ZOBELLIA_4426 | Protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. The active site of the metallo-beta-lactamase domain is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | Conserved hypothetical protein; Localized in the cytoplasm. | 0.790 |
| CAZ98563.1 | CAZ98564.1 | ZOBELLIA_4428 | ZOBELLIA_4429 | Protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. The active site of the metallo-beta-lactamase domain is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | Pseudogene of protein; This protein corresponds to a central fragment of an hypothetical protein from Kordia algicida and is likely an inactive pseudogene; Localized in the cytoplasm; Hypothetical protein. | 0.548 |
| CAZ98563.1 | CAZ98565.1 | ZOBELLIA_4428 | ZOBELLIA_4430 | Protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. The active site of the metallo-beta-lactamase domain is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | Putative protein. | 0.512 |
| CAZ98563.1 | dpsA4 | ZOBELLIA_4428 | ZOBELLIA_4427 | Protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. The active site of the metallo-beta-lactamase domain is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | DNA protection during starvation protein; Dsp protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction; Forms a homododecamer and the 12 subunits form a hollow sphere into which the mineral iron core of up to 500 Fe(3+) can be deposited; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the Dps family. | 0.782 |
| CAZ98564.1 | CAZ98561.1 | ZOBELLIA_4429 | ZOBELLIA_4426 | Pseudogene of protein; This protein corresponds to a central fragment of an hypothetical protein from Kordia algicida and is likely an inactive pseudogene; Localized in the cytoplasm; Hypothetical protein. | Conserved hypothetical protein; Localized in the cytoplasm. | 0.540 |
| CAZ98564.1 | CAZ98563.1 | ZOBELLIA_4429 | ZOBELLIA_4428 | Pseudogene of protein; This protein corresponds to a central fragment of an hypothetical protein from Kordia algicida and is likely an inactive pseudogene; Localized in the cytoplasm; Hypothetical protein. | Protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. The active site of the metallo-beta-lactamase domain is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | 0.548 |
| CAZ98564.1 | CAZ98565.1 | ZOBELLIA_4429 | ZOBELLIA_4430 | Pseudogene of protein; This protein corresponds to a central fragment of an hypothetical protein from Kordia algicida and is likely an inactive pseudogene; Localized in the cytoplasm; Hypothetical protein. | Putative protein. | 0.718 |
| CAZ98564.1 | dpsA4 | ZOBELLIA_4429 | ZOBELLIA_4427 | Pseudogene of protein; This protein corresponds to a central fragment of an hypothetical protein from Kordia algicida and is likely an inactive pseudogene; Localized in the cytoplasm; Hypothetical protein. | DNA protection during starvation protein; Dsp protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction; Forms a homododecamer and the 12 subunits form a hollow sphere into which the mineral iron core of up to 500 Fe(3+) can be deposited; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the Dps family. | 0.548 |
| CAZ98565.1 | CAZ98561.1 | ZOBELLIA_4430 | ZOBELLIA_4426 | Putative protein. | Conserved hypothetical protein; Localized in the cytoplasm. | 0.505 |
| CAZ98565.1 | CAZ98563.1 | ZOBELLIA_4430 | ZOBELLIA_4428 | Putative protein. | Protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. The active site of the metallo-beta-lactamase domain is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | 0.512 |
| CAZ98565.1 | CAZ98564.1 | ZOBELLIA_4430 | ZOBELLIA_4429 | Putative protein. | Pseudogene of protein; This protein corresponds to a central fragment of an hypothetical protein from Kordia algicida and is likely an inactive pseudogene; Localized in the cytoplasm; Hypothetical protein. | 0.718 |
| CAZ98565.1 | dpsA4 | ZOBELLIA_4430 | ZOBELLIA_4427 | Putative protein. | DNA protection during starvation protein; Dsp protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction; Forms a homododecamer and the 12 subunits form a hollow sphere into which the mineral iron core of up to 500 Fe(3+) can be deposited; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the Dps family. | 0.512 |
| dpsA4 | CAZ98561.1 | ZOBELLIA_4427 | ZOBELLIA_4426 | DNA protection during starvation protein; Dsp protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction; Forms a homododecamer and the 12 subunits form a hollow sphere into which the mineral iron core of up to 500 Fe(3+) can be deposited; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the Dps family. | Conserved hypothetical protein; Localized in the cytoplasm. | 0.762 |
| dpsA4 | CAZ98563.1 | ZOBELLIA_4427 | ZOBELLIA_4428 | DNA protection during starvation protein; Dsp protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction; Forms a homododecamer and the 12 subunits form a hollow sphere into which the mineral iron core of up to 500 Fe(3+) can be deposited; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the Dps family. | Protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. The active site of the metallo-beta-lactamase domain is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | 0.782 |
| dpsA4 | CAZ98564.1 | ZOBELLIA_4427 | ZOBELLIA_4429 | DNA protection during starvation protein; Dsp protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction; Forms a homododecamer and the 12 subunits form a hollow sphere into which the mineral iron core of up to 500 Fe(3+) can be deposited; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the Dps family. | Pseudogene of protein; This protein corresponds to a central fragment of an hypothetical protein from Kordia algicida and is likely an inactive pseudogene; Localized in the cytoplasm; Hypothetical protein. | 0.548 |
| dpsA4 | CAZ98565.1 | ZOBELLIA_4427 | ZOBELLIA_4430 | DNA protection during starvation protein; Dsp protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction; Forms a homododecamer and the 12 subunits form a hollow sphere into which the mineral iron core of up to 500 Fe(3+) can be deposited; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the Dps family. | Putative protein. | 0.512 |