| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CAZ94656.1 | CAZ94657.1 | ZOBELLIA_585 | ZOBELLIA_586 | Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Hypothetical protein. | Conserved hypothetical membrane protein; Contains a N-terminal transmembrane helix; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 0.531 |
| CAZ94656.1 | cvrA | ZOBELLIA_585 | ZOBELLIA_584 | Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Hypothetical protein. | Cell volume regulation protein A participates in control of cell volume in low-osmolarity conditions. It belongs to the Na/H antiporters. This integral membrane protein also features a C-terminal TrkA-C domain which may bind an unidentified ligand and is predicted to adopt an all beta structure. Features eleven transmembrane helices; High confidence in function and specificity. | 0.633 |
| CAZ94657.1 | CAZ94656.1 | ZOBELLIA_586 | ZOBELLIA_585 | Conserved hypothetical membrane protein; Contains a N-terminal transmembrane helix; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Hypothetical protein. | 0.531 |
| CAZ94657.1 | cvrA | ZOBELLIA_586 | ZOBELLIA_584 | Conserved hypothetical membrane protein; Contains a N-terminal transmembrane helix; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | Cell volume regulation protein A participates in control of cell volume in low-osmolarity conditions. It belongs to the Na/H antiporters. This integral membrane protein also features a C-terminal TrkA-C domain which may bind an unidentified ligand and is predicted to adopt an all beta structure. Features eleven transmembrane helices; High confidence in function and specificity. | 0.446 |
| CAZ95728.1 | cvrA | ZOBELLIA_1674 | ZOBELLIA_584 | Sodium/hydrogen exchanger; Na/H antiporters are key transporters in maintaining the pH of actively metabolising cells. The molecular mechanisms of antiport are unclear. This integral membrane protein also contains a C-terminal TrkA- N domain which binds NAD and adopts a Rossmann fold, Contains twelve transmembrane helices; Belongs to the monovalent cation:proton antiporter 2 (CPA2) transporter family; Localized in the cytoplasmic membrane; Specificity unclear. | Cell volume regulation protein A participates in control of cell volume in low-osmolarity conditions. It belongs to the Na/H antiporters. This integral membrane protein also features a C-terminal TrkA-C domain which may bind an unidentified ligand and is predicted to adopt an all beta structure. Features eleven transmembrane helices; High confidence in function and specificity. | 0.485 |
| CAZ95728.1 | kefC | ZOBELLIA_1674 | ZOBELLIA_4256 | Sodium/hydrogen exchanger; Na/H antiporters are key transporters in maintaining the pH of actively metabolising cells. The molecular mechanisms of antiport are unclear. This integral membrane protein also contains a C-terminal TrkA- N domain which binds NAD and adopts a Rossmann fold, Contains twelve transmembrane helices; Belongs to the monovalent cation:proton antiporter 2 (CPA2) transporter family; Localized in the cytoplasmic membrane; Specificity unclear. | The K(+)/H(+) antiporter KefC is a Glutathione-regulated potassium-efflux system protein responsible for glutathione-gated K+ efflux. Activation of KefC K+ efflux system only occurs in the presence of glutathione and a reactive electrophile such as methylglyoxal or N-ethylmaleimide. KefC is important for cell survival during exposure to toxic metabolites, possibly because they can release K+, allowing H+ uptake. H+ uptake (acidification of the cytoplasm) accompanying or following K+ efflux may serve as a further protective mechanism against electrophile toxicity; Contains 12 transmembr [...] | 0.654 |
| arsB | arsC-2 | ZOBELLIA_583 | ZOBELLIA_582 | Arsenite resistance protein ArsB seems to confer resistance to arsenite by allowing cells to extrude this compound. Could be part of an arsenite extrusion pump. Belongs to the Sodium Bile acid symporter family; Contains ten transmembrane helices; Localized in the cytoplasmic membrane; High confidence in function and specificity. | Protein arsC reduces arsenate [As(V)] to arsenite [As(III)] (Arsenate reductase, EC 1.20.4.-) and dephosphorylates tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates (LMW protein-tyrosine-phosphatase, EC 3.1.3.48). Could switch between different functions in different circumstances. Localized in the cytoplasm; High confidence in function and specificity. | 0.904 |
| arsB | cvrA | ZOBELLIA_583 | ZOBELLIA_584 | Arsenite resistance protein ArsB seems to confer resistance to arsenite by allowing cells to extrude this compound. Could be part of an arsenite extrusion pump. Belongs to the Sodium Bile acid symporter family; Contains ten transmembrane helices; Localized in the cytoplasmic membrane; High confidence in function and specificity. | Cell volume regulation protein A participates in control of cell volume in low-osmolarity conditions. It belongs to the Na/H antiporters. This integral membrane protein also features a C-terminal TrkA-C domain which may bind an unidentified ligand and is predicted to adopt an all beta structure. Features eleven transmembrane helices; High confidence in function and specificity. | 0.466 |
| arsC-2 | arsB | ZOBELLIA_582 | ZOBELLIA_583 | Protein arsC reduces arsenate [As(V)] to arsenite [As(III)] (Arsenate reductase, EC 1.20.4.-) and dephosphorylates tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates (LMW protein-tyrosine-phosphatase, EC 3.1.3.48). Could switch between different functions in different circumstances. Localized in the cytoplasm; High confidence in function and specificity. | Arsenite resistance protein ArsB seems to confer resistance to arsenite by allowing cells to extrude this compound. Could be part of an arsenite extrusion pump. Belongs to the Sodium Bile acid symporter family; Contains ten transmembrane helices; Localized in the cytoplasmic membrane; High confidence in function and specificity. | 0.904 |
| arsC-2 | cvrA | ZOBELLIA_582 | ZOBELLIA_584 | Protein arsC reduces arsenate [As(V)] to arsenite [As(III)] (Arsenate reductase, EC 1.20.4.-) and dephosphorylates tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates (LMW protein-tyrosine-phosphatase, EC 3.1.3.48). Could switch between different functions in different circumstances. Localized in the cytoplasm; High confidence in function and specificity. | Cell volume regulation protein A participates in control of cell volume in low-osmolarity conditions. It belongs to the Na/H antiporters. This integral membrane protein also features a C-terminal TrkA-C domain which may bind an unidentified ligand and is predicted to adopt an all beta structure. Features eleven transmembrane helices; High confidence in function and specificity. | 0.451 |
| cvrA | CAZ94656.1 | ZOBELLIA_584 | ZOBELLIA_585 | Cell volume regulation protein A participates in control of cell volume in low-osmolarity conditions. It belongs to the Na/H antiporters. This integral membrane protein also features a C-terminal TrkA-C domain which may bind an unidentified ligand and is predicted to adopt an all beta structure. Features eleven transmembrane helices; High confidence in function and specificity. | Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Hypothetical protein. | 0.633 |
| cvrA | CAZ94657.1 | ZOBELLIA_584 | ZOBELLIA_586 | Cell volume regulation protein A participates in control of cell volume in low-osmolarity conditions. It belongs to the Na/H antiporters. This integral membrane protein also features a C-terminal TrkA-C domain which may bind an unidentified ligand and is predicted to adopt an all beta structure. Features eleven transmembrane helices; High confidence in function and specificity. | Conserved hypothetical membrane protein; Contains a N-terminal transmembrane helix; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 0.446 |
| cvrA | CAZ95728.1 | ZOBELLIA_584 | ZOBELLIA_1674 | Cell volume regulation protein A participates in control of cell volume in low-osmolarity conditions. It belongs to the Na/H antiporters. This integral membrane protein also features a C-terminal TrkA-C domain which may bind an unidentified ligand and is predicted to adopt an all beta structure. Features eleven transmembrane helices; High confidence in function and specificity. | Sodium/hydrogen exchanger; Na/H antiporters are key transporters in maintaining the pH of actively metabolising cells. The molecular mechanisms of antiport are unclear. This integral membrane protein also contains a C-terminal TrkA- N domain which binds NAD and adopts a Rossmann fold, Contains twelve transmembrane helices; Belongs to the monovalent cation:proton antiporter 2 (CPA2) transporter family; Localized in the cytoplasmic membrane; Specificity unclear. | 0.485 |
| cvrA | arsB | ZOBELLIA_584 | ZOBELLIA_583 | Cell volume regulation protein A participates in control of cell volume in low-osmolarity conditions. It belongs to the Na/H antiporters. This integral membrane protein also features a C-terminal TrkA-C domain which may bind an unidentified ligand and is predicted to adopt an all beta structure. Features eleven transmembrane helices; High confidence in function and specificity. | Arsenite resistance protein ArsB seems to confer resistance to arsenite by allowing cells to extrude this compound. Could be part of an arsenite extrusion pump. Belongs to the Sodium Bile acid symporter family; Contains ten transmembrane helices; Localized in the cytoplasmic membrane; High confidence in function and specificity. | 0.466 |
| cvrA | arsC-2 | ZOBELLIA_584 | ZOBELLIA_582 | Cell volume regulation protein A participates in control of cell volume in low-osmolarity conditions. It belongs to the Na/H antiporters. This integral membrane protein also features a C-terminal TrkA-C domain which may bind an unidentified ligand and is predicted to adopt an all beta structure. Features eleven transmembrane helices; High confidence in function and specificity. | Protein arsC reduces arsenate [As(V)] to arsenite [As(III)] (Arsenate reductase, EC 1.20.4.-) and dephosphorylates tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates (LMW protein-tyrosine-phosphatase, EC 3.1.3.48). Could switch between different functions in different circumstances. Localized in the cytoplasm; High confidence in function and specificity. | 0.451 |
| cvrA | kefC | ZOBELLIA_584 | ZOBELLIA_4256 | Cell volume regulation protein A participates in control of cell volume in low-osmolarity conditions. It belongs to the Na/H antiporters. This integral membrane protein also features a C-terminal TrkA-C domain which may bind an unidentified ligand and is predicted to adopt an all beta structure. Features eleven transmembrane helices; High confidence in function and specificity. | The K(+)/H(+) antiporter KefC is a Glutathione-regulated potassium-efflux system protein responsible for glutathione-gated K+ efflux. Activation of KefC K+ efflux system only occurs in the presence of glutathione and a reactive electrophile such as methylglyoxal or N-ethylmaleimide. KefC is important for cell survival during exposure to toxic metabolites, possibly because they can release K+, allowing H+ uptake. H+ uptake (acidification of the cytoplasm) accompanying or following K+ efflux may serve as a further protective mechanism against electrophile toxicity; Contains 12 transmembr [...] | 0.406 |
| kefC | CAZ95728.1 | ZOBELLIA_4256 | ZOBELLIA_1674 | The K(+)/H(+) antiporter KefC is a Glutathione-regulated potassium-efflux system protein responsible for glutathione-gated K+ efflux. Activation of KefC K+ efflux system only occurs in the presence of glutathione and a reactive electrophile such as methylglyoxal or N-ethylmaleimide. KefC is important for cell survival during exposure to toxic metabolites, possibly because they can release K+, allowing H+ uptake. H+ uptake (acidification of the cytoplasm) accompanying or following K+ efflux may serve as a further protective mechanism against electrophile toxicity; Contains 12 transmembr [...] | Sodium/hydrogen exchanger; Na/H antiporters are key transporters in maintaining the pH of actively metabolising cells. The molecular mechanisms of antiport are unclear. This integral membrane protein also contains a C-terminal TrkA- N domain which binds NAD and adopts a Rossmann fold, Contains twelve transmembrane helices; Belongs to the monovalent cation:proton antiporter 2 (CPA2) transporter family; Localized in the cytoplasmic membrane; Specificity unclear. | 0.654 |
| kefC | cvrA | ZOBELLIA_4256 | ZOBELLIA_584 | The K(+)/H(+) antiporter KefC is a Glutathione-regulated potassium-efflux system protein responsible for glutathione-gated K+ efflux. Activation of KefC K+ efflux system only occurs in the presence of glutathione and a reactive electrophile such as methylglyoxal or N-ethylmaleimide. KefC is important for cell survival during exposure to toxic metabolites, possibly because they can release K+, allowing H+ uptake. H+ uptake (acidification of the cytoplasm) accompanying or following K+ efflux may serve as a further protective mechanism against electrophile toxicity; Contains 12 transmembr [...] | Cell volume regulation protein A participates in control of cell volume in low-osmolarity conditions. It belongs to the Na/H antiporters. This integral membrane protein also features a C-terminal TrkA-C domain which may bind an unidentified ligand and is predicted to adopt an all beta structure. Features eleven transmembrane helices; High confidence in function and specificity. | 0.406 |