node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CUQ77432.1 | drrA | ERS852451_02031 | ERS852451_02032 | ABC-type transport system involved in multi-copper enzyme maturation%2C permease component. | Daunorubicin/doxorubicin resistance ATP-binding protein DrrA. | 0.798 |
CUQ77432.1 | ydcR | ERS852451_02031 | ERS852451_02033 | ABC-type transport system involved in multi-copper enzyme maturation%2C permease component. | Uncharacterized HTH-type transcriptional regulator ydcR. | 0.752 |
CUQ77642.1 | drrA | ERS852451_02121 | ERS852451_02032 | ABC-type transport system involved in multi-copper enzyme maturation%2C permease component. | Daunorubicin/doxorubicin resistance ATP-binding protein DrrA. | 0.897 |
artQ_1 | drrA | ERS852451_00215 | ERS852451_02032 | Arginine transport system permease protein ArtQ. | Daunorubicin/doxorubicin resistance ATP-binding protein DrrA. | 0.718 |
artQ_1 | pleC | ERS852451_00215 | ERS852451_01959 | Arginine transport system permease protein ArtQ. | Non-motile and phage-resistance protein. | 0.939 |
atpA_1 | atpA_2 | ERS852451_00032 | ERS852451_02489 | ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | ATP synthase subunit alpha; 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from [...] | 0.997 |
atpA_1 | atpD_1 | ERS852451_00032 | ERS852451_00034 | ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | 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 |
atpA_1 | atpD_2 | ERS852451_00032 | ERS852451_02491 | ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | 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. | 0.998 |
atpA_1 | drrA | ERS852451_00032 | ERS852451_02032 | ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | Daunorubicin/doxorubicin resistance ATP-binding protein DrrA. | 0.495 |
atpA_2 | atpA_1 | ERS852451_02489 | ERS852451_00032 | ATP synthase subunit alpha; 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from [...] | ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | 0.997 |
atpA_2 | atpD_1 | ERS852451_02489 | ERS852451_00034 | ATP synthase subunit alpha; 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from [...] | 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 |
atpA_2 | atpD_2 | ERS852451_02489 | ERS852451_02491 | ATP synthase subunit alpha; 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from [...] | 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 |
atpA_2 | drrA | ERS852451_02489 | ERS852451_02032 | ATP synthase subunit alpha; 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from [...] | Daunorubicin/doxorubicin resistance ATP-binding protein DrrA. | 0.866 |
atpD_1 | atpA_1 | ERS852451_00034 | ERS852451_00032 | 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. | ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | 0.999 |
atpD_1 | atpA_2 | ERS852451_00034 | ERS852451_02489 | 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. | ATP synthase subunit alpha; 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from [...] | 0.999 |
atpD_1 | atpD_2 | ERS852451_00034 | ERS852451_02491 | 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. | 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. | 0.546 |
atpD_1 | drrA | ERS852451_00034 | ERS852451_02032 | 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. | Daunorubicin/doxorubicin resistance ATP-binding protein DrrA. | 0.501 |
atpD_2 | atpA_1 | ERS852451_02491 | ERS852451_00032 | 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. | ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | 0.998 |
atpD_2 | atpA_2 | ERS852451_02491 | ERS852451_02489 | 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. | ATP synthase subunit alpha; 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. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from [...] | 0.999 |
atpD_2 | atpD_1 | ERS852451_02491 | ERS852451_00034 | 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. | 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. | 0.546 |