node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CAZ95377.1 | CAZ95553.1 | ZOBELLIA_1321 | ZOBELLIA_1497 | Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 0.467 |
CAZ95377.1 | batC | ZOBELLIA_1321 | ZOBELLIA_1500 | Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | The protein BatC is a conserved protein belonging to the Bat operon (Bacteroides aerotolerance). Its exact function is unknown. Contains three N-terminal Tetratricopeptide repeats; Signal peptide cleaved between the residues 18 and 19; Localized in the periplasmic space; Function unclear. | 0.504 |
CAZ95551.1 | CAZ95552.1 | ZOBELLIA_1495 | ZOBELLIA_1496 | MoxR-like ATPases have been proposed to function with VWA domain proteins to form a chaperone system involved in the activation of proteins by primarily mediating the insertion of metal cofactors into the substrate molecules; Belongs to the MoxR-like family; Localized in the cytoplasm; Function unclear. | vWA domain protein; Conserved protein belonging to the von Willebrand factor type A (vWA) domain family. Some VWA domain proteins have been proposed to function with MoxR-like ATPases to form a chaperone system involved in the activation of proteins by primarily mediating the insertion of metal cofactors into the substrate molecules; Localized in the cytoplasm; Family membership. | 0.936 |
CAZ95551.1 | CAZ95553.1 | ZOBELLIA_1495 | ZOBELLIA_1497 | MoxR-like ATPases have been proposed to function with VWA domain proteins to form a chaperone system involved in the activation of proteins by primarily mediating the insertion of metal cofactors into the substrate molecules; Belongs to the MoxR-like family; Localized in the cytoplasm; Function unclear. | Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 0.696 |
CAZ95551.1 | batA | ZOBELLIA_1495 | ZOBELLIA_1498 | MoxR-like ATPases have been proposed to function with VWA domain proteins to form a chaperone system involved in the activation of proteins by primarily mediating the insertion of metal cofactors into the substrate molecules; Belongs to the MoxR-like family; Localized in the cytoplasm; Function unclear. | The protein BatA is a membrane protein belonging to the Bat operon (Bacteroides aerotolerance). Its exact function is unknown. Contains two N-terminal a transmembrane helices, three von Willebrand factor type A domain and a C-terminal transmembrane helix; Localized in the cytoplasmic membrane; Function unclear. | 0.905 |
CAZ95551.1 | batB | ZOBELLIA_1495 | ZOBELLIA_1499 | MoxR-like ATPases have been proposed to function with VWA domain proteins to form a chaperone system involved in the activation of proteins by primarily mediating the insertion of metal cofactors into the substrate molecules; Belongs to the MoxR-like family; Localized in the cytoplasm; Function unclear. | The protein BatB is a membrane protein belonging to the Bat operon (Bacteroides aerotolerance). Its exact function is unknown; Contains two N-terminal a transmembrane helices, three von Willebrand factor type A domain and a C-terminal transmembrane helix; Localized in the cytoplasmic membrane; Function unclear. | 0.877 |
CAZ95551.1 | batC | ZOBELLIA_1495 | ZOBELLIA_1500 | MoxR-like ATPases have been proposed to function with VWA domain proteins to form a chaperone system involved in the activation of proteins by primarily mediating the insertion of metal cofactors into the substrate molecules; Belongs to the MoxR-like family; Localized in the cytoplasm; Function unclear. | The protein BatC is a conserved protein belonging to the Bat operon (Bacteroides aerotolerance). Its exact function is unknown. Contains three N-terminal Tetratricopeptide repeats; Signal peptide cleaved between the residues 18 and 19; Localized in the periplasmic space; Function unclear. | 0.689 |
CAZ95551.1 | batD | ZOBELLIA_1495 | ZOBELLIA_1501 | MoxR-like ATPases have been proposed to function with VWA domain proteins to form a chaperone system involved in the activation of proteins by primarily mediating the insertion of metal cofactors into the substrate molecules; Belongs to the MoxR-like family; Localized in the cytoplasm; Function unclear. | The protein BatD is a membrane protein belonging to the Bat operon (Bacteroides aerotolerance). Its exact function is unknown. Contains a C-terminal transmembrane helices; Localized in the cytoplasmic membrane; Function unclear. | 0.634 |
CAZ95551.1 | batE | ZOBELLIA_1495 | ZOBELLIA_1502 | MoxR-like ATPases have been proposed to function with VWA domain proteins to form a chaperone system involved in the activation of proteins by primarily mediating the insertion of metal cofactors into the substrate molecules; Belongs to the MoxR-like family; Localized in the cytoplasm; Function unclear. | The protein BatE is a membrane protein belonging to the Bat operon (Bacteroides aerotolerance). Its exact function is unknown; Contains two N-terminal Tetratricopeptide repeats, two central transmembrane helices and a C-terminal bacterial SH3 domain; Localized in the cytoplasmic membrane; Function unclear. | 0.545 |
CAZ95552.1 | CAZ95551.1 | ZOBELLIA_1496 | ZOBELLIA_1495 | vWA domain protein; Conserved protein belonging to the von Willebrand factor type A (vWA) domain family. Some VWA domain proteins have been proposed to function with MoxR-like ATPases to form a chaperone system involved in the activation of proteins by primarily mediating the insertion of metal cofactors into the substrate molecules; Localized in the cytoplasm; Family membership. | MoxR-like ATPases have been proposed to function with VWA domain proteins to form a chaperone system involved in the activation of proteins by primarily mediating the insertion of metal cofactors into the substrate molecules; Belongs to the MoxR-like family; Localized in the cytoplasm; Function unclear. | 0.936 |
CAZ95552.1 | CAZ95553.1 | ZOBELLIA_1496 | ZOBELLIA_1497 | vWA domain protein; Conserved protein belonging to the von Willebrand factor type A (vWA) domain family. Some VWA domain proteins have been proposed to function with MoxR-like ATPases to form a chaperone system involved in the activation of proteins by primarily mediating the insertion of metal cofactors into the substrate molecules; Localized in the cytoplasm; Family membership. | Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 0.925 |
CAZ95552.1 | batA | ZOBELLIA_1496 | ZOBELLIA_1498 | vWA domain protein; Conserved protein belonging to the von Willebrand factor type A (vWA) domain family. Some VWA domain proteins have been proposed to function with MoxR-like ATPases to form a chaperone system involved in the activation of proteins by primarily mediating the insertion of metal cofactors into the substrate molecules; Localized in the cytoplasm; Family membership. | The protein BatA is a membrane protein belonging to the Bat operon (Bacteroides aerotolerance). Its exact function is unknown. Contains two N-terminal a transmembrane helices, three von Willebrand factor type A domain and a C-terminal transmembrane helix; Localized in the cytoplasmic membrane; Function unclear. | 0.961 |
CAZ95552.1 | batB | ZOBELLIA_1496 | ZOBELLIA_1499 | vWA domain protein; Conserved protein belonging to the von Willebrand factor type A (vWA) domain family. Some VWA domain proteins have been proposed to function with MoxR-like ATPases to form a chaperone system involved in the activation of proteins by primarily mediating the insertion of metal cofactors into the substrate molecules; Localized in the cytoplasm; Family membership. | The protein BatB is a membrane protein belonging to the Bat operon (Bacteroides aerotolerance). Its exact function is unknown; Contains two N-terminal a transmembrane helices, three von Willebrand factor type A domain and a C-terminal transmembrane helix; Localized in the cytoplasmic membrane; Function unclear. | 0.932 |
CAZ95552.1 | batC | ZOBELLIA_1496 | ZOBELLIA_1500 | vWA domain protein; Conserved protein belonging to the von Willebrand factor type A (vWA) domain family. Some VWA domain proteins have been proposed to function with MoxR-like ATPases to form a chaperone system involved in the activation of proteins by primarily mediating the insertion of metal cofactors into the substrate molecules; Localized in the cytoplasm; Family membership. | The protein BatC is a conserved protein belonging to the Bat operon (Bacteroides aerotolerance). Its exact function is unknown. Contains three N-terminal Tetratricopeptide repeats; Signal peptide cleaved between the residues 18 and 19; Localized in the periplasmic space; Function unclear. | 0.907 |
CAZ95552.1 | batD | ZOBELLIA_1496 | ZOBELLIA_1501 | vWA domain protein; Conserved protein belonging to the von Willebrand factor type A (vWA) domain family. Some VWA domain proteins have been proposed to function with MoxR-like ATPases to form a chaperone system involved in the activation of proteins by primarily mediating the insertion of metal cofactors into the substrate molecules; Localized in the cytoplasm; Family membership. | The protein BatD is a membrane protein belonging to the Bat operon (Bacteroides aerotolerance). Its exact function is unknown. Contains a C-terminal transmembrane helices; Localized in the cytoplasmic membrane; Function unclear. | 0.906 |
CAZ95552.1 | batE | ZOBELLIA_1496 | ZOBELLIA_1502 | vWA domain protein; Conserved protein belonging to the von Willebrand factor type A (vWA) domain family. Some VWA domain proteins have been proposed to function with MoxR-like ATPases to form a chaperone system involved in the activation of proteins by primarily mediating the insertion of metal cofactors into the substrate molecules; Localized in the cytoplasm; Family membership. | The protein BatE is a membrane protein belonging to the Bat operon (Bacteroides aerotolerance). Its exact function is unknown; Contains two N-terminal Tetratricopeptide repeats, two central transmembrane helices and a C-terminal bacterial SH3 domain; Localized in the cytoplasmic membrane; Function unclear. | 0.887 |
CAZ95553.1 | CAZ95377.1 | ZOBELLIA_1497 | ZOBELLIA_1321 | Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 0.467 |
CAZ95553.1 | CAZ95551.1 | ZOBELLIA_1497 | ZOBELLIA_1495 | Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | MoxR-like ATPases have been proposed to function with VWA domain proteins to form a chaperone system involved in the activation of proteins by primarily mediating the insertion of metal cofactors into the substrate molecules; Belongs to the MoxR-like family; Localized in the cytoplasm; Function unclear. | 0.696 |
CAZ95553.1 | CAZ95552.1 | ZOBELLIA_1497 | ZOBELLIA_1496 | Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | vWA domain protein; Conserved protein belonging to the von Willebrand factor type A (vWA) domain family. Some VWA domain proteins have been proposed to function with MoxR-like ATPases to form a chaperone system involved in the activation of proteins by primarily mediating the insertion of metal cofactors into the substrate molecules; Localized in the cytoplasm; Family membership. | 0.925 |
CAZ95553.1 | batA | ZOBELLIA_1497 | ZOBELLIA_1498 | Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | The protein BatA is a membrane protein belonging to the Bat operon (Bacteroides aerotolerance). Its exact function is unknown. Contains two N-terminal a transmembrane helices, three von Willebrand factor type A domain and a C-terminal transmembrane helix; Localized in the cytoplasmic membrane; Function unclear. | 0.921 |