node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
atpB | atpC | ERS852502_02399 | ERS852502_02392 | F-ATPase subunit 6; 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. | F-ATPase epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. | 0.999 |
atpB | atpD_1 | ERS852502_02399 | ERS852502_02393 | F-ATPase subunit 6; 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. | ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | 0.999 |
atpB | atpE | ERS852502_02399 | ERS852502_02398 | F-ATPase subunit 6; 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. | Lipid-binding protein; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.999 |
atpB | atpG | ERS852502_02399 | ERS852502_02394 | F-ATPase subunit 6; 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. | Na(+)-translocating ATPase gamma chain; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. | 0.999 |
atpB | atpH | ERS852502_02399 | ERS852502_02396 | F-ATPase subunit 6; 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. | F-type ATPase subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.999 |
atpC | atpB | ERS852502_02392 | ERS852502_02399 | F-ATPase epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. | F-ATPase subunit 6; 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. | 0.999 |
atpC | atpD_1 | ERS852502_02392 | ERS852502_02393 | F-ATPase epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. | ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | 0.999 |
atpC | atpE | ERS852502_02392 | ERS852502_02398 | F-ATPase epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. | Lipid-binding protein; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.999 |
atpC | atpG | ERS852502_02392 | ERS852502_02394 | F-ATPase epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. | Na(+)-translocating ATPase gamma chain; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. | 0.999 |
atpC | atpH | ERS852502_02392 | ERS852502_02396 | F-ATPase epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. | F-type ATPase subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.999 |
atpD_1 | atpB | ERS852502_02393 | ERS852502_02399 | ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | F-ATPase subunit 6; 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. | 0.999 |
atpD_1 | atpC | ERS852502_02393 | ERS852502_02392 | ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | F-ATPase epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. | 0.999 |
atpD_1 | atpE | ERS852502_02393 | ERS852502_02398 | ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | Lipid-binding protein; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.999 |
atpD_1 | atpG | ERS852502_02393 | ERS852502_02394 | ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | Na(+)-translocating ATPase gamma chain; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. | 0.999 |
atpD_1 | atpH | ERS852502_02393 | ERS852502_02396 | ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | F-type ATPase subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.999 |
atpE | atpB | ERS852502_02398 | ERS852502_02399 | Lipid-binding protein; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | F-ATPase subunit 6; 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. | 0.999 |
atpE | atpC | ERS852502_02398 | ERS852502_02392 | Lipid-binding protein; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | F-ATPase epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. | 0.999 |
atpE | atpD_1 | ERS852502_02398 | ERS852502_02393 | Lipid-binding protein; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | 0.999 |
atpE | atpG | ERS852502_02398 | ERS852502_02394 | Lipid-binding protein; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | Na(+)-translocating ATPase gamma chain; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. | 0.999 |
atpE | atpH | ERS852502_02398 | ERS852502_02396 | Lipid-binding protein; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | F-type ATPase subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.999 |