node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
OIJ21803.1 | prmC | BKP45_03650 | BKP45_03665 | threonylcarbamoyl-AMP synthase; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. | protein-(glutamine-N5) methyltransferase, release factor-specific; Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif; Belongs to the protein N5-glutamine methyltransferase family. PrmC subfamily. | 0.879 |
atpA | atpC | BKP45_03570 | BKP45_03555 | F0F1 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. | F0F1 ATP synthase subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane. | 0.999 |
atpA | atpD | BKP45_03570 | BKP45_03560 | F0F1 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. | F0F1 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 | atpE | BKP45_03570 | BKP45_03585 | F0F1 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 F0 subunit C; 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 |
atpA | atpG | BKP45_03570 | BKP45_03565 | F0F1 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. | F0F1 ATP synthase subunit gamma; 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 |
atpA | atpH | BKP45_03570 | BKP45_03575 | F0F1 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. | Hypothetical 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 |
atpA | prmC | BKP45_03570 | BKP45_03665 | F0F1 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. | protein-(glutamine-N5) methyltransferase, release factor-specific; Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif; Belongs to the protein N5-glutamine methyltransferase family. PrmC subfamily. | 0.810 |
atpC | atpA | BKP45_03555 | BKP45_03570 | F0F1 ATP synthase subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane. | F0F1 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 |
atpC | atpD | BKP45_03555 | BKP45_03560 | F0F1 ATP synthase subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane. | F0F1 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 | BKP45_03555 | BKP45_03585 | F0F1 ATP synthase subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane. | ATP synthase F0 subunit C; 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 | BKP45_03555 | BKP45_03565 | F0F1 ATP synthase subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane. | F0F1 ATP synthase subunit gamma; 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 | BKP45_03555 | BKP45_03575 | F0F1 ATP synthase subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane. | Hypothetical 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 | prmC | BKP45_03555 | BKP45_03665 | F0F1 ATP synthase subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane. | protein-(glutamine-N5) methyltransferase, release factor-specific; Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif; Belongs to the protein N5-glutamine methyltransferase family. PrmC subfamily. | 0.825 |
atpD | atpA | BKP45_03560 | BKP45_03570 | F0F1 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. | F0F1 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 | atpC | BKP45_03560 | BKP45_03555 | F0F1 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. | F0F1 ATP synthase subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane. | 0.999 |
atpD | atpE | BKP45_03560 | BKP45_03585 | F0F1 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 F0 subunit C; 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 | atpG | BKP45_03560 | BKP45_03565 | F0F1 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. | F0F1 ATP synthase subunit gamma; 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 | atpH | BKP45_03560 | BKP45_03575 | F0F1 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. | Hypothetical 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 | prmC | BKP45_03560 | BKP45_03665 | F0F1 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. | protein-(glutamine-N5) methyltransferase, release factor-specific; Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif; Belongs to the protein N5-glutamine methyltransferase family. PrmC subfamily. | 0.826 |
atpE | atpA | BKP45_03585 | BKP45_03570 | ATP synthase F0 subunit C; 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. | F0F1 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 |