node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
BC332_01589 | BC332_06226 | A0A2G3DET1 | A0A2G3DA93 | Photosystem I iron-sulfur center. | Cytochrome c1 1, heme protein, mitochondrial. | 0.867 |
BC332_01589 | BC332_08832 | A0A2G3DET1 | A0A2G3CYB9 | Photosystem I iron-sulfur center. | Cytochrome c1-1, heme protein, mitochondrial. | 0.867 |
BC332_01589 | BC332_10778 | A0A2G3DET1 | A0A2G3CLT0 | Photosystem I iron-sulfur center. | Photosystem II CP47 reaction center protein. | 0.880 |
BC332_01589 | BC332_16420 | A0A2G3DET1 | A0A2G3C928 | Photosystem I iron-sulfur center. | Cytochrome c1-1, heme protein, mitochondrial. | 0.867 |
BC332_01589 | BC332_17069 | A0A2G3DET1 | A0A2G3CAW2 | Photosystem I iron-sulfur center. | Cytochrome c oxidase subunit 3. | 0.952 |
BC332_01589 | BC332_17071 | A0A2G3DET1 | A0A2G3CAX3 | Photosystem I iron-sulfur center. | Cytochrome c oxidase subunit 3; Subunits I, II and III form the functional core of the enzyme complex. | 0.952 |
BC332_01589 | BC332_24195 | A0A2G3DET1 | A0A2G3BMK6 | Photosystem I iron-sulfur center. | Cytochrome b6-f complex iron-sulfur subunit; Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. | 0.940 |
BC332_01589 | BC332_26169 | A0A2G3DET1 | A0A2G3BFT0 | Photosystem I iron-sulfur center. | Cytochrome c oxidase subunit 3; Subunits I, II and III form the functional core of the enzyme complex. | 0.952 |
BC332_01589 | BC332_32308 | A0A2G3DET1 | A0A2G3AWZ1 | Photosystem I iron-sulfur center. | Photosystem II reaction center protein L. | 0.761 |
BC332_01589 | psbF | A0A2G3DET1 | A0A1L6Z646 | Photosystem I iron-sulfur center. | Cytochrome b559 subunit beta; This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. Belongs to the PsbE/PsbF family. | 0.785 |
BC332_06226 | BC332_01589 | A0A2G3DA93 | A0A2G3DET1 | Cytochrome c1 1, heme protein, mitochondrial. | Photosystem I iron-sulfur center. | 0.867 |
BC332_06226 | BC332_10778 | A0A2G3DA93 | A0A2G3CLT0 | Cytochrome c1 1, heme protein, mitochondrial. | Photosystem II CP47 reaction center protein. | 0.888 |
BC332_06226 | BC332_16420 | A0A2G3DA93 | A0A2G3C928 | Cytochrome c1 1, heme protein, mitochondrial. | Cytochrome c1-1, heme protein, mitochondrial. | 0.933 |
BC332_06226 | BC332_17069 | A0A2G3DA93 | A0A2G3CAW2 | Cytochrome c1 1, heme protein, mitochondrial. | Cytochrome c oxidase subunit 3. | 0.959 |
BC332_06226 | BC332_17071 | A0A2G3DA93 | A0A2G3CAX3 | Cytochrome c1 1, heme protein, mitochondrial. | Cytochrome c oxidase subunit 3; Subunits I, II and III form the functional core of the enzyme complex. | 0.959 |
BC332_06226 | BC332_24195 | A0A2G3DA93 | A0A2G3BMK6 | Cytochrome c1 1, heme protein, mitochondrial. | Cytochrome b6-f complex iron-sulfur subunit; Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. | 0.998 |
BC332_06226 | BC332_26169 | A0A2G3DA93 | A0A2G3BFT0 | Cytochrome c1 1, heme protein, mitochondrial. | Cytochrome c oxidase subunit 3; Subunits I, II and III form the functional core of the enzyme complex. | 0.959 |
BC332_08832 | BC332_01589 | A0A2G3CYB9 | A0A2G3DET1 | Cytochrome c1-1, heme protein, mitochondrial. | Photosystem I iron-sulfur center. | 0.867 |
BC332_08832 | BC332_10778 | A0A2G3CYB9 | A0A2G3CLT0 | Cytochrome c1-1, heme protein, mitochondrial. | Photosystem II CP47 reaction center protein. | 0.888 |
BC332_08832 | BC332_17069 | A0A2G3CYB9 | A0A2G3CAW2 | Cytochrome c1-1, heme protein, mitochondrial. | Cytochrome c oxidase subunit 3. | 0.959 |