node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
EIJ37620.1 | EIJ38595.1 | JoomaDRAFT_0579 | JoomaDRAFT_1583 | PFAM: Cytochrome c; Cytochrome C oxidase, mono-heme subunit/FixO; TIGRFAM: cytochrome c oxidase, cbb3-type, subunit II. | Heme/copper-type cytochrome/quinol 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). | 0.982 |
EIJ37620.1 | EIJ38596.1 | JoomaDRAFT_0579 | JoomaDRAFT_1584 | PFAM: Cytochrome c; Cytochrome C oxidase, mono-heme subunit/FixO; TIGRFAM: cytochrome c oxidase, cbb3-type, subunit II. | Heme/copper-type cytochrome/quinol oxidase, subunit 1; PFAM: Cytochrome C and Quinol oxidase polypeptide I; Belongs to the heme-copper respiratory oxidase family. | 0.944 |
EIJ37620.1 | EIJ38726.1 | JoomaDRAFT_0579 | JoomaDRAFT_1719 | PFAM: Cytochrome c; Cytochrome C oxidase, mono-heme subunit/FixO; TIGRFAM: cytochrome c oxidase, cbb3-type, subunit II. | Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III. | 0.983 |
EIJ37620.1 | EIJ38727.1 | JoomaDRAFT_0579 | JoomaDRAFT_1720 | PFAM: Cytochrome c; Cytochrome C oxidase, mono-heme subunit/FixO; TIGRFAM: cytochrome c oxidase, cbb3-type, subunit II. | Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III. | 0.983 |
EIJ37620.1 | EIJ38815.1 | JoomaDRAFT_0579 | JoomaDRAFT_1810 | PFAM: Cytochrome c; Cytochrome C oxidase, mono-heme subunit/FixO; TIGRFAM: cytochrome c oxidase, cbb3-type, subunit II. | Cytochrome c, mono- and diheme variants family; PFAM: Cytochrome c; TIGRFAM: cytochrome c oxidase, cbb3-type, subunit III. | 0.993 |
EIJ37620.1 | EIJ38816.1 | JoomaDRAFT_0579 | JoomaDRAFT_1811 | PFAM: Cytochrome c; Cytochrome C oxidase, mono-heme subunit/FixO; TIGRFAM: cytochrome c oxidase, cbb3-type, subunit II. | PFAM: Cbb3-type cytochrome oxidase component FixQ. | 0.955 |
EIJ37620.1 | EIJ38826.1 | JoomaDRAFT_0579 | JoomaDRAFT_1821 | PFAM: Cytochrome c; Cytochrome C oxidase, mono-heme subunit/FixO; TIGRFAM: cytochrome c oxidase, cbb3-type, subunit II. | Hypothetical protein. | 0.944 |
EIJ37620.1 | ctaB | JoomaDRAFT_0579 | JoomaDRAFT_1718 | PFAM: Cytochrome c; Cytochrome C oxidase, mono-heme subunit/FixO; TIGRFAM: cytochrome c oxidase, cbb3-type, subunit II. | Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. | 0.918 |
EIJ38595.1 | EIJ37620.1 | JoomaDRAFT_1583 | JoomaDRAFT_0579 | Heme/copper-type cytochrome/quinol 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). | PFAM: Cytochrome c; Cytochrome C oxidase, mono-heme subunit/FixO; TIGRFAM: cytochrome c oxidase, cbb3-type, subunit II. | 0.982 |
EIJ38595.1 | EIJ38596.1 | JoomaDRAFT_1583 | JoomaDRAFT_1584 | Heme/copper-type cytochrome/quinol 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 1; PFAM: Cytochrome C and Quinol oxidase polypeptide I; Belongs to the heme-copper respiratory oxidase family. | 0.999 |
EIJ38595.1 | EIJ38726.1 | JoomaDRAFT_1583 | JoomaDRAFT_1719 | Heme/copper-type cytochrome/quinol 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; PFAM: Cytochrome c oxidase subunit III. | 0.999 |
EIJ38595.1 | EIJ38727.1 | JoomaDRAFT_1583 | JoomaDRAFT_1720 | Heme/copper-type cytochrome/quinol 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; PFAM: Cytochrome c oxidase subunit III. | 0.999 |
EIJ38595.1 | EIJ38728.1 | JoomaDRAFT_1583 | JoomaDRAFT_1721 | Heme/copper-type cytochrome/quinol 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). | Hypothetical protein. | 0.955 |
EIJ38595.1 | EIJ38815.1 | JoomaDRAFT_1583 | JoomaDRAFT_1810 | Heme/copper-type cytochrome/quinol 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, mono- and diheme variants family; PFAM: Cytochrome c; TIGRFAM: cytochrome c oxidase, cbb3-type, subunit III. | 0.979 |
EIJ38595.1 | EIJ38816.1 | JoomaDRAFT_1583 | JoomaDRAFT_1811 | Heme/copper-type cytochrome/quinol 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). | PFAM: Cbb3-type cytochrome oxidase component FixQ. | 0.982 |
EIJ38595.1 | EIJ38826.1 | JoomaDRAFT_1583 | JoomaDRAFT_1821 | Heme/copper-type cytochrome/quinol 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). | Hypothetical protein. | 0.994 |
EIJ38595.1 | atpB | JoomaDRAFT_1583 | JoomaDRAFT_1367 | Heme/copper-type cytochrome/quinol 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). | F0F1-type ATP synthase, alpha subunit; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Belongs to the ATPase A chain family. | 0.904 |
EIJ38595.1 | ctaB | JoomaDRAFT_1583 | JoomaDRAFT_1718 | Heme/copper-type cytochrome/quinol 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). | Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. | 0.993 |
EIJ38596.1 | EIJ37620.1 | JoomaDRAFT_1584 | JoomaDRAFT_0579 | Heme/copper-type cytochrome/quinol oxidase, subunit 1; PFAM: Cytochrome C and Quinol oxidase polypeptide I; Belongs to the heme-copper respiratory oxidase family. | PFAM: Cytochrome c; Cytochrome C oxidase, mono-heme subunit/FixO; TIGRFAM: cytochrome c oxidase, cbb3-type, subunit II. | 0.944 |
EIJ38596.1 | EIJ38595.1 | JoomaDRAFT_1584 | JoomaDRAFT_1583 | Heme/copper-type cytochrome/quinol oxidase, subunit 1; PFAM: Cytochrome C and Quinol oxidase polypeptide I; Belongs to the heme-copper respiratory oxidase family. | Heme/copper-type cytochrome/quinol 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). | 0.999 |