node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SMF38038.1 | SMF49093.1 | SAMN06295900_106127 | SAMN06295900_108124 | Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | NosR/NirI family transcriptional regulator, nitrous oxide reductase regulator. | 0.668 |
SMF38038.1 | SMF52558.1 | SAMN06295900_106127 | SAMN06295900_10962 | Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Cytochrome c. | 0.733 |
SMF38038.1 | SMF55219.1 | SAMN06295900_106127 | SAMN06295900_11034 | Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Heme/copper-type cytochrome/quinol oxidase, subunit 3. | 0.999 |
SMF38038.1 | SMF55252.1 | SAMN06295900_106127 | SAMN06295900_11036 | Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Cytochrome c oxidase subunit 2. | 0.999 |
SMF38038.1 | SMF57966.1 | SAMN06295900_106127 | SAMN06295900_11152 | Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Nitric oxide reductase, NorZ apoprotein. | 0.963 |
SMF38038.1 | SMF62572.1 | SAMN06295900_106127 | SAMN06295900_11312 | Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | DMSO/TMAO reductase YedYZ, molybdopterin-dependent catalytic subunit. | 0.817 |
SMF38038.1 | SMF70717.1 | SAMN06295900_106127 | SAMN06295900_11694 | Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | DMSO/TMAO reductase YedYZ, molybdopterin-dependent catalytic subunit. | 0.817 |
SMF38038.1 | SMF77856.1 | SAMN06295900_106127 | SAMN06295900_12024 | Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | CDP-4-dehydro-6-deoxyglucose reductase. | 0.473 |
SMF38038.1 | msrP | SAMN06295900_106127 | SAMN06295900_107178 | Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Sulfoxide reductase catalytic subunit YedY; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to re [...] | 0.817 |
SMF49093.1 | SMF38038.1 | SAMN06295900_108124 | SAMN06295900_106127 | NosR/NirI family transcriptional regulator, nitrous oxide reductase regulator. | Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.668 |
SMF49093.1 | SMF52558.1 | SAMN06295900_108124 | SAMN06295900_10962 | NosR/NirI family transcriptional regulator, nitrous oxide reductase regulator. | Cytochrome c. | 0.779 |
SMF49093.1 | SMF55219.1 | SAMN06295900_108124 | SAMN06295900_11034 | NosR/NirI family transcriptional regulator, nitrous oxide reductase regulator. | Heme/copper-type cytochrome/quinol oxidase, subunit 3. | 0.552 |
SMF49093.1 | SMF55252.1 | SAMN06295900_108124 | SAMN06295900_11036 | NosR/NirI family transcriptional regulator, nitrous oxide reductase regulator. | Cytochrome c oxidase subunit 2. | 0.509 |
SMF49093.1 | SMF57966.1 | SAMN06295900_108124 | SAMN06295900_11152 | NosR/NirI family transcriptional regulator, nitrous oxide reductase regulator. | Nitric oxide reductase, NorZ apoprotein. | 0.987 |
SMF52547.1 | SMF52558.1 | SAMN06295900_10961 | SAMN06295900_10962 | Osmotically-inducible protein OsmY, contains BON domain. | Cytochrome c. | 0.838 |
SMF52558.1 | SMF38038.1 | SAMN06295900_10962 | SAMN06295900_106127 | Cytochrome c. | Cytochrome c oxidase subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.733 |
SMF52558.1 | SMF49093.1 | SAMN06295900_10962 | SAMN06295900_108124 | Cytochrome c. | NosR/NirI family transcriptional regulator, nitrous oxide reductase regulator. | 0.779 |
SMF52558.1 | SMF52547.1 | SAMN06295900_10962 | SAMN06295900_10961 | Cytochrome c. | Osmotically-inducible protein OsmY, contains BON domain. | 0.838 |
SMF52558.1 | SMF55219.1 | SAMN06295900_10962 | SAMN06295900_11034 | Cytochrome c. | Heme/copper-type cytochrome/quinol oxidase, subunit 3. | 0.719 |
SMF52558.1 | SMF55252.1 | SAMN06295900_10962 | SAMN06295900_11036 | Cytochrome c. | Cytochrome c oxidase subunit 2. | 0.755 |