| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CAZ94181.1 | CAZ94183.1 | ZOBELLIA_108 | ZOBELLIA_110 | Conserved hypothetical lipoprotein; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Conserved hypothetical protein. | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 29 and 30; Localized in the periplasmic space; Conserved hypothetical protein. | 0.913 |
| CAZ94181.1 | ccpA1 | ZOBELLIA_108 | ZOBELLIA_109 | Conserved hypothetical lipoprotein; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Conserved hypothetical protein. | Di-heme cytochrome c peroxidase (CCP) reduces hydrogen peroxide to water using c-type heme as an oxidizable substrate. However, since it possesses two, instead of one, heme prosthetic groups, CCPs reduce hydrogen peroxide without the need to generate semi-stable free radicals. The two heme groups have significantly different redox potentials. CCP is structured into two domains, each containing one c-type haem group, with a calcium-binding site at the domain interface. Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 17 and 18; Localized in the cytoplasmic [...] | 0.915 |
| CAZ94183.1 | CAZ94181.1 | ZOBELLIA_110 | ZOBELLIA_108 | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 29 and 30; Localized in the periplasmic space; Conserved hypothetical protein. | Conserved hypothetical lipoprotein; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Conserved hypothetical protein. | 0.913 |
| CAZ94183.1 | CAZ94184.1 | ZOBELLIA_110 | ZOBELLIA_111 | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 29 and 30; Localized in the periplasmic space; Conserved hypothetical protein. | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 18 and 20; Localized in the periplasmic space; Conserved hypothetical protein. | 0.444 |
| CAZ94183.1 | ccpA1 | ZOBELLIA_110 | ZOBELLIA_109 | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 29 and 30; Localized in the periplasmic space; Conserved hypothetical protein. | Di-heme cytochrome c peroxidase (CCP) reduces hydrogen peroxide to water using c-type heme as an oxidizable substrate. However, since it possesses two, instead of one, heme prosthetic groups, CCPs reduce hydrogen peroxide without the need to generate semi-stable free radicals. The two heme groups have significantly different redox potentials. CCP is structured into two domains, each containing one c-type haem group, with a calcium-binding site at the domain interface. Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 17 and 18; Localized in the cytoplasmic [...] | 0.945 |
| CAZ94184.1 | CAZ94183.1 | ZOBELLIA_111 | ZOBELLIA_110 | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 18 and 20; Localized in the periplasmic space; Conserved hypothetical protein. | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 29 and 30; Localized in the periplasmic space; Conserved hypothetical protein. | 0.444 |
| CAZ94184.1 | ccpA1 | ZOBELLIA_111 | ZOBELLIA_109 | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 18 and 20; Localized in the periplasmic space; Conserved hypothetical protein. | Di-heme cytochrome c peroxidase (CCP) reduces hydrogen peroxide to water using c-type heme as an oxidizable substrate. However, since it possesses two, instead of one, heme prosthetic groups, CCPs reduce hydrogen peroxide without the need to generate semi-stable free radicals. The two heme groups have significantly different redox potentials. CCP is structured into two domains, each containing one c-type haem group, with a calcium-binding site at the domain interface. Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 17 and 18; Localized in the cytoplasmic [...] | 0.437 |
| ccoNO | ccpA1 | ZOBELLIA_2257 | ZOBELLIA_109 | Fusion of the subunits CcoN and CcoO of the Cytochrome cbb3 oxidase. Converts the ferrocytochrome to ferricytochrome. Belongs to the ccoNOQP operon. Contains 13 transmembrane helices; Localized in the cytoplasmic membrane; High confidence in function and specificity. | Di-heme cytochrome c peroxidase (CCP) reduces hydrogen peroxide to water using c-type heme as an oxidizable substrate. However, since it possesses two, instead of one, heme prosthetic groups, CCPs reduce hydrogen peroxide without the need to generate semi-stable free radicals. The two heme groups have significantly different redox potentials. CCP is structured into two domains, each containing one c-type haem group, with a calcium-binding site at the domain interface. Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 17 and 18; Localized in the cytoplasmic [...] | 0.459 |
| ccpA1 | CAZ94181.1 | ZOBELLIA_109 | ZOBELLIA_108 | Di-heme cytochrome c peroxidase (CCP) reduces hydrogen peroxide to water using c-type heme as an oxidizable substrate. However, since it possesses two, instead of one, heme prosthetic groups, CCPs reduce hydrogen peroxide without the need to generate semi-stable free radicals. The two heme groups have significantly different redox potentials. CCP is structured into two domains, each containing one c-type haem group, with a calcium-binding site at the domain interface. Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 17 and 18; Localized in the cytoplasmic [...] | Conserved hypothetical lipoprotein; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Conserved hypothetical protein. | 0.915 |
| ccpA1 | CAZ94183.1 | ZOBELLIA_109 | ZOBELLIA_110 | Di-heme cytochrome c peroxidase (CCP) reduces hydrogen peroxide to water using c-type heme as an oxidizable substrate. However, since it possesses two, instead of one, heme prosthetic groups, CCPs reduce hydrogen peroxide without the need to generate semi-stable free radicals. The two heme groups have significantly different redox potentials. CCP is structured into two domains, each containing one c-type haem group, with a calcium-binding site at the domain interface. Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 17 and 18; Localized in the cytoplasmic [...] | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 29 and 30; Localized in the periplasmic space; Conserved hypothetical protein. | 0.945 |
| ccpA1 | CAZ94184.1 | ZOBELLIA_109 | ZOBELLIA_111 | Di-heme cytochrome c peroxidase (CCP) reduces hydrogen peroxide to water using c-type heme as an oxidizable substrate. However, since it possesses two, instead of one, heme prosthetic groups, CCPs reduce hydrogen peroxide without the need to generate semi-stable free radicals. The two heme groups have significantly different redox potentials. CCP is structured into two domains, each containing one c-type haem group, with a calcium-binding site at the domain interface. Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 17 and 18; Localized in the cytoplasmic [...] | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 18 and 20; Localized in the periplasmic space; Conserved hypothetical protein. | 0.437 |
| ccpA1 | ccoNO | ZOBELLIA_109 | ZOBELLIA_2257 | Di-heme cytochrome c peroxidase (CCP) reduces hydrogen peroxide to water using c-type heme as an oxidizable substrate. However, since it possesses two, instead of one, heme prosthetic groups, CCPs reduce hydrogen peroxide without the need to generate semi-stable free radicals. The two heme groups have significantly different redox potentials. CCP is structured into two domains, each containing one c-type haem group, with a calcium-binding site at the domain interface. Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 17 and 18; Localized in the cytoplasmic [...] | Fusion of the subunits CcoN and CcoO of the Cytochrome cbb3 oxidase. Converts the ferrocytochrome to ferricytochrome. Belongs to the ccoNOQP operon. Contains 13 transmembrane helices; Localized in the cytoplasmic membrane; High confidence in function and specificity. | 0.459 |