node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CAZ94368.1 | CAZ97575.1 | ZOBELLIA_295 | ZOBELLIA_3437 | This protein belongs to the Heavy metal transport protein family. The Heavy-Metal-Associated (HMA) domain contains two conserved cysteines that are probably involved in metal binding. Its structure comprises our- stranded antiparallel beta-sheet and two alpha helices packed in an alpha-beta sandwich fold. Somes of these HMA proteins are involved in bacterial resistance to toxic metals, such as lead and cadmium. Localized in the cytoplasm; Specificity unclear. | TonB-dependent Receptor; Protein localized in the outer membrane involved in uptake of macromolecules that are too large to diffuse via the outer membrane porins channels or are encountered at very low concentrations; Contains a carboxypeptidase regulatory domain (21-95) and the Plug module (109-215) acting as a channel gate; The signal peptide is cleaved between the residues 20 and 21; Family membership. | 0.433 |
CAZ94368.1 | CAZ97624.1 | ZOBELLIA_295 | ZOBELLIA_3486 | This protein belongs to the Heavy metal transport protein family. The Heavy-Metal-Associated (HMA) domain contains two conserved cysteines that are probably involved in metal binding. Its structure comprises our- stranded antiparallel beta-sheet and two alpha helices packed in an alpha-beta sandwich fold. Somes of these HMA proteins are involved in bacterial resistance to toxic metals, such as lead and cadmium. Localized in the cytoplasm; Specificity unclear. | Conserved hypothetical protein; Localized in the cytoplasm. | 0.664 |
CAZ97570.1 | CAZ97571.1 | ZOBELLIA_3432 | ZOBELLIA_3433 | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria (type I secretion system); Signal peptide cleaved between the residues 19 and 20; Localized in the outer membrane; Family membership. | These membrane fusion proteins (MFP) belong to a multidrug efflux pump system that confer the resistance to compounds such as antibiotics, solvents or heavy metals; Proteins of the MFP family function as 'adaptors', connecting a ABC transporters, localized in the cytoplasmic membrane, with a porin or channel localized in outer membrane; The MFP proteins seem to be anchored in the cytoplasmique membrane by a N-terminal transmembrane region; Family membership. | 0.928 |
CAZ97570.1 | CAZ97572.1 | ZOBELLIA_3432 | ZOBELLIA_3434 | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria (type I secretion system); Signal peptide cleaved between the residues 19 and 20; Localized in the outer membrane; Family membership. | Multidrug efflux transporter; Integral membrane protein involved in drug resistance that belongs to the acrB/acrD/acrF family; Contains 12 transmembrane segments and two large periplasmic domains (each exceeding 300 residues) between helices 1 and 2, and helices 7 and 8. The three transmembrane domains form a large, 30-wide central cavity that spans the cytoplasmic membrane and extends to the cytoplasm; Localized in the cytoplasmic membrane; Family membership; Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family. | 0.893 |
CAZ97570.1 | CAZ97573.1 | ZOBELLIA_3432 | ZOBELLIA_3435 | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria (type I secretion system); Signal peptide cleaved between the residues 19 and 20; Localized in the outer membrane; Family membership. | Conserved hypothetical protein; Localized in the cytoplasm. | 0.861 |
CAZ97570.1 | CAZ97575.1 | ZOBELLIA_3432 | ZOBELLIA_3437 | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria (type I secretion system); Signal peptide cleaved between the residues 19 and 20; Localized in the outer membrane; Family membership. | TonB-dependent Receptor; Protein localized in the outer membrane involved in uptake of macromolecules that are too large to diffuse via the outer membrane porins channels or are encountered at very low concentrations; Contains a carboxypeptidase regulatory domain (21-95) and the Plug module (109-215) acting as a channel gate; The signal peptide is cleaved between the residues 20 and 21; Family membership. | 0.675 |
CAZ97570.1 | CAZ97576.1 | ZOBELLIA_3432 | ZOBELLIA_3438 | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria (type I secretion system); Signal peptide cleaved between the residues 19 and 20; Localized in the outer membrane; Family membership. | Conserved hypothetical protein; Localized in the cytoplasm. | 0.412 |
CAZ97570.1 | CAZ97624.1 | ZOBELLIA_3432 | ZOBELLIA_3486 | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria (type I secretion system); Signal peptide cleaved between the residues 19 and 20; Localized in the outer membrane; Family membership. | Conserved hypothetical protein; Localized in the cytoplasm. | 0.693 |
CAZ97571.1 | CAZ97570.1 | ZOBELLIA_3433 | ZOBELLIA_3432 | These membrane fusion proteins (MFP) belong to a multidrug efflux pump system that confer the resistance to compounds such as antibiotics, solvents or heavy metals; Proteins of the MFP family function as 'adaptors', connecting a ABC transporters, localized in the cytoplasmic membrane, with a porin or channel localized in outer membrane; The MFP proteins seem to be anchored in the cytoplasmique membrane by a N-terminal transmembrane region; Family membership. | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria (type I secretion system); Signal peptide cleaved between the residues 19 and 20; Localized in the outer membrane; Family membership. | 0.928 |
CAZ97571.1 | CAZ97572.1 | ZOBELLIA_3433 | ZOBELLIA_3434 | These membrane fusion proteins (MFP) belong to a multidrug efflux pump system that confer the resistance to compounds such as antibiotics, solvents or heavy metals; Proteins of the MFP family function as 'adaptors', connecting a ABC transporters, localized in the cytoplasmic membrane, with a porin or channel localized in outer membrane; The MFP proteins seem to be anchored in the cytoplasmique membrane by a N-terminal transmembrane region; Family membership. | Multidrug efflux transporter; Integral membrane protein involved in drug resistance that belongs to the acrB/acrD/acrF family; Contains 12 transmembrane segments and two large periplasmic domains (each exceeding 300 residues) between helices 1 and 2, and helices 7 and 8. The three transmembrane domains form a large, 30-wide central cavity that spans the cytoplasmic membrane and extends to the cytoplasm; Localized in the cytoplasmic membrane; Family membership; Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family. | 0.925 |
CAZ97571.1 | CAZ97573.1 | ZOBELLIA_3433 | ZOBELLIA_3435 | These membrane fusion proteins (MFP) belong to a multidrug efflux pump system that confer the resistance to compounds such as antibiotics, solvents or heavy metals; Proteins of the MFP family function as 'adaptors', connecting a ABC transporters, localized in the cytoplasmic membrane, with a porin or channel localized in outer membrane; The MFP proteins seem to be anchored in the cytoplasmique membrane by a N-terminal transmembrane region; Family membership. | Conserved hypothetical protein; Localized in the cytoplasm. | 0.889 |
CAZ97571.1 | CAZ97575.1 | ZOBELLIA_3433 | ZOBELLIA_3437 | These membrane fusion proteins (MFP) belong to a multidrug efflux pump system that confer the resistance to compounds such as antibiotics, solvents or heavy metals; Proteins of the MFP family function as 'adaptors', connecting a ABC transporters, localized in the cytoplasmic membrane, with a porin or channel localized in outer membrane; The MFP proteins seem to be anchored in the cytoplasmique membrane by a N-terminal transmembrane region; Family membership. | TonB-dependent Receptor; Protein localized in the outer membrane involved in uptake of macromolecules that are too large to diffuse via the outer membrane porins channels or are encountered at very low concentrations; Contains a carboxypeptidase regulatory domain (21-95) and the Plug module (109-215) acting as a channel gate; The signal peptide is cleaved between the residues 20 and 21; Family membership. | 0.622 |
CAZ97571.1 | CAZ97624.1 | ZOBELLIA_3433 | ZOBELLIA_3486 | These membrane fusion proteins (MFP) belong to a multidrug efflux pump system that confer the resistance to compounds such as antibiotics, solvents or heavy metals; Proteins of the MFP family function as 'adaptors', connecting a ABC transporters, localized in the cytoplasmic membrane, with a porin or channel localized in outer membrane; The MFP proteins seem to be anchored in the cytoplasmique membrane by a N-terminal transmembrane region; Family membership. | Conserved hypothetical protein; Localized in the cytoplasm. | 0.646 |
CAZ97572.1 | CAZ97570.1 | ZOBELLIA_3434 | ZOBELLIA_3432 | Multidrug efflux transporter; Integral membrane protein involved in drug resistance that belongs to the acrB/acrD/acrF family; Contains 12 transmembrane segments and two large periplasmic domains (each exceeding 300 residues) between helices 1 and 2, and helices 7 and 8. The three transmembrane domains form a large, 30-wide central cavity that spans the cytoplasmic membrane and extends to the cytoplasm; Localized in the cytoplasmic membrane; Family membership; Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family. | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria (type I secretion system); Signal peptide cleaved between the residues 19 and 20; Localized in the outer membrane; Family membership. | 0.893 |
CAZ97572.1 | CAZ97571.1 | ZOBELLIA_3434 | ZOBELLIA_3433 | Multidrug efflux transporter; Integral membrane protein involved in drug resistance that belongs to the acrB/acrD/acrF family; Contains 12 transmembrane segments and two large periplasmic domains (each exceeding 300 residues) between helices 1 and 2, and helices 7 and 8. The three transmembrane domains form a large, 30-wide central cavity that spans the cytoplasmic membrane and extends to the cytoplasm; Localized in the cytoplasmic membrane; Family membership; Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family. | These membrane fusion proteins (MFP) belong to a multidrug efflux pump system that confer the resistance to compounds such as antibiotics, solvents or heavy metals; Proteins of the MFP family function as 'adaptors', connecting a ABC transporters, localized in the cytoplasmic membrane, with a porin or channel localized in outer membrane; The MFP proteins seem to be anchored in the cytoplasmique membrane by a N-terminal transmembrane region; Family membership. | 0.925 |
CAZ97572.1 | CAZ97573.1 | ZOBELLIA_3434 | ZOBELLIA_3435 | Multidrug efflux transporter; Integral membrane protein involved in drug resistance that belongs to the acrB/acrD/acrF family; Contains 12 transmembrane segments and two large periplasmic domains (each exceeding 300 residues) between helices 1 and 2, and helices 7 and 8. The three transmembrane domains form a large, 30-wide central cavity that spans the cytoplasmic membrane and extends to the cytoplasm; Localized in the cytoplasmic membrane; Family membership; Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family. | Conserved hypothetical protein; Localized in the cytoplasm. | 0.945 |
CAZ97572.1 | CAZ97575.1 | ZOBELLIA_3434 | ZOBELLIA_3437 | Multidrug efflux transporter; Integral membrane protein involved in drug resistance that belongs to the acrB/acrD/acrF family; Contains 12 transmembrane segments and two large periplasmic domains (each exceeding 300 residues) between helices 1 and 2, and helices 7 and 8. The three transmembrane domains form a large, 30-wide central cavity that spans the cytoplasmic membrane and extends to the cytoplasm; Localized in the cytoplasmic membrane; Family membership; Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family. | TonB-dependent Receptor; Protein localized in the outer membrane involved in uptake of macromolecules that are too large to diffuse via the outer membrane porins channels or are encountered at very low concentrations; Contains a carboxypeptidase regulatory domain (21-95) and the Plug module (109-215) acting as a channel gate; The signal peptide is cleaved between the residues 20 and 21; Family membership. | 0.445 |
CAZ97572.1 | CAZ97624.1 | ZOBELLIA_3434 | ZOBELLIA_3486 | Multidrug efflux transporter; Integral membrane protein involved in drug resistance that belongs to the acrB/acrD/acrF family; Contains 12 transmembrane segments and two large periplasmic domains (each exceeding 300 residues) between helices 1 and 2, and helices 7 and 8. The three transmembrane domains form a large, 30-wide central cavity that spans the cytoplasmic membrane and extends to the cytoplasm; Localized in the cytoplasmic membrane; Family membership; Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family. | Conserved hypothetical protein; Localized in the cytoplasm. | 0.609 |
CAZ97573.1 | CAZ97570.1 | ZOBELLIA_3435 | ZOBELLIA_3432 | Conserved hypothetical protein; Localized in the cytoplasm. | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria (type I secretion system); Signal peptide cleaved between the residues 19 and 20; Localized in the outer membrane; Family membership. | 0.861 |
CAZ97573.1 | CAZ97571.1 | ZOBELLIA_3435 | ZOBELLIA_3433 | Conserved hypothetical protein; Localized in the cytoplasm. | These membrane fusion proteins (MFP) belong to a multidrug efflux pump system that confer the resistance to compounds such as antibiotics, solvents or heavy metals; Proteins of the MFP family function as 'adaptors', connecting a ABC transporters, localized in the cytoplasmic membrane, with a porin or channel localized in outer membrane; The MFP proteins seem to be anchored in the cytoplasmique membrane by a N-terminal transmembrane region; Family membership. | 0.889 |