| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CAZ94608.1 | CAZ94609.1 | ZOBELLIA_537 | ZOBELLIA_538 | Conserved membrane protein containing two UPF0126 domains. The conserved glycines are suggestive of an ion channel. Contains seven transmembrane helices; Localized in the cytoplasmic membrane; Family membership. | This family of proteins contain three highly conserved amino acids: one arginine and two aspartates, hence the name of RDD family. Contains three transmembrane helices. The arginine occurs at the N terminus of the first helix and the first aspartate occurs in the middle of this helix. The molecular function of this protein is unknown; Localized in the cytoplasmic membrane; Family membership. | 0.666 |
| CAZ94608.1 | CAZ94610.1 | ZOBELLIA_537 | ZOBELLIA_539 | Conserved membrane protein containing two UPF0126 domains. The conserved glycines are suggestive of an ion channel. Contains seven transmembrane helices; Localized in the cytoplasmic membrane; Family membership. | Conserved integral membrane protein belonging to the DUF95 family. Contains five transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 0.500 |
| CAZ94608.1 | CAZ94611.1 | ZOBELLIA_537 | ZOBELLIA_540 | Conserved membrane protein containing two UPF0126 domains. The conserved glycines are suggestive of an ion channel. Contains seven transmembrane helices; Localized in the cytoplasmic membrane; Family membership. | Conserved hypothetical membrane protein; Contains five transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 0.481 |
| CAZ94608.1 | CAZ94612.1 | ZOBELLIA_537 | ZOBELLIA_541 | Conserved membrane protein containing two UPF0126 domains. The conserved glycines are suggestive of an ion channel. Contains seven transmembrane helices; Localized in the cytoplasmic membrane; Family membership. | Conserved hypothetical membrane protein; Contains one central transmembrane helix; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 0.500 |
| CAZ94608.1 | CAZ94613.1 | ZOBELLIA_537 | ZOBELLIA_542 | Conserved membrane protein containing two UPF0126 domains. The conserved glycines are suggestive of an ion channel. Contains seven transmembrane helices; Localized in the cytoplasmic membrane; Family membership. | Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 0.500 |
| CAZ94608.1 | CAZ94614.1 | ZOBELLIA_537 | ZOBELLIA_543 | Conserved membrane protein containing two UPF0126 domains. The conserved glycines are suggestive of an ion channel. Contains seven transmembrane helices; Localized in the cytoplasmic membrane; Family membership. | ATPase belonging to the MoxR-like family. In Paracoccus denitrificans, MoxR is involved in the regulation of formation of active methanol dehydrogenase. 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; Localized in the cytoplasm; Specificity unclear. | 0.460 |
| CAZ94608.1 | CAZ94615.1 | ZOBELLIA_537 | ZOBELLIA_544 | Conserved membrane protein containing two UPF0126 domains. The conserved glycines are suggestive of an ion channel. Contains seven transmembrane helices; Localized in the cytoplasmic membrane; Family membership. | 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. Contains two N-terminal transmembrane helices; Localized in the cytoplasmic membrane; Function unclear. | 0.452 |
| CAZ94609.1 | CAZ94608.1 | ZOBELLIA_538 | ZOBELLIA_537 | This family of proteins contain three highly conserved amino acids: one arginine and two aspartates, hence the name of RDD family. Contains three transmembrane helices. The arginine occurs at the N terminus of the first helix and the first aspartate occurs in the middle of this helix. The molecular function of this protein is unknown; Localized in the cytoplasmic membrane; Family membership. | Conserved membrane protein containing two UPF0126 domains. The conserved glycines are suggestive of an ion channel. Contains seven transmembrane helices; Localized in the cytoplasmic membrane; Family membership. | 0.666 |
| CAZ94609.1 | CAZ94610.1 | ZOBELLIA_538 | ZOBELLIA_539 | This family of proteins contain three highly conserved amino acids: one arginine and two aspartates, hence the name of RDD family. Contains three transmembrane helices. The arginine occurs at the N terminus of the first helix and the first aspartate occurs in the middle of this helix. The molecular function of this protein is unknown; Localized in the cytoplasmic membrane; Family membership. | Conserved integral membrane protein belonging to the DUF95 family. Contains five transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 0.934 |
| CAZ94609.1 | CAZ94611.1 | ZOBELLIA_538 | ZOBELLIA_540 | This family of proteins contain three highly conserved amino acids: one arginine and two aspartates, hence the name of RDD family. Contains three transmembrane helices. The arginine occurs at the N terminus of the first helix and the first aspartate occurs in the middle of this helix. The molecular function of this protein is unknown; Localized in the cytoplasmic membrane; Family membership. | Conserved hypothetical membrane protein; Contains five transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 0.904 |
| CAZ94609.1 | CAZ94612.1 | ZOBELLIA_538 | ZOBELLIA_541 | This family of proteins contain three highly conserved amino acids: one arginine and two aspartates, hence the name of RDD family. Contains three transmembrane helices. The arginine occurs at the N terminus of the first helix and the first aspartate occurs in the middle of this helix. The molecular function of this protein is unknown; Localized in the cytoplasmic membrane; Family membership. | Conserved hypothetical membrane protein; Contains one central transmembrane helix; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 0.918 |
| CAZ94609.1 | CAZ94613.1 | ZOBELLIA_538 | ZOBELLIA_542 | This family of proteins contain three highly conserved amino acids: one arginine and two aspartates, hence the name of RDD family. Contains three transmembrane helices. The arginine occurs at the N terminus of the first helix and the first aspartate occurs in the middle of this helix. The molecular function of this protein is unknown; Localized in the cytoplasmic membrane; Family membership. | Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 0.918 |
| CAZ94609.1 | CAZ94614.1 | ZOBELLIA_538 | ZOBELLIA_543 | This family of proteins contain three highly conserved amino acids: one arginine and two aspartates, hence the name of RDD family. Contains three transmembrane helices. The arginine occurs at the N terminus of the first helix and the first aspartate occurs in the middle of this helix. The molecular function of this protein is unknown; Localized in the cytoplasmic membrane; Family membership. | ATPase belonging to the MoxR-like family. In Paracoccus denitrificans, MoxR is involved in the regulation of formation of active methanol dehydrogenase. 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; Localized in the cytoplasm; Specificity unclear. | 0.713 |
| CAZ94609.1 | CAZ94615.1 | ZOBELLIA_538 | ZOBELLIA_544 | This family of proteins contain three highly conserved amino acids: one arginine and two aspartates, hence the name of RDD family. Contains three transmembrane helices. The arginine occurs at the N terminus of the first helix and the first aspartate occurs in the middle of this helix. The molecular function of this protein is unknown; Localized in the cytoplasmic membrane; Family membership. | 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. Contains two N-terminal transmembrane helices; Localized in the cytoplasmic membrane; Function unclear. | 0.909 |
| CAZ94609.1 | CAZ94616.1 | ZOBELLIA_538 | ZOBELLIA_545 | This family of proteins contain three highly conserved amino acids: one arginine and two aspartates, hence the name of RDD family. Contains three transmembrane helices. The arginine occurs at the N terminus of the first helix and the first aspartate occurs in the middle of this helix. The molecular function of this protein is unknown; Localized in the cytoplasmic membrane; Family membership. | Putative protein. | 0.418 |
| CAZ94609.1 | CAZ94617.1 | ZOBELLIA_538 | ZOBELLIA_546 | This family of proteins contain three highly conserved amino acids: one arginine and two aspartates, hence the name of RDD family. Contains three transmembrane helices. The arginine occurs at the N terminus of the first helix and the first aspartate occurs in the middle of this helix. The molecular function of this protein is unknown; Localized in the cytoplasmic membrane; Family membership. | Hypothetical protein. Putatively localized in the cytoplasm. | 0.418 |
| CAZ94609.1 | hslR | ZOBELLIA_538 | ZOBELLIA_3015 | This family of proteins contain three highly conserved amino acids: one arginine and two aspartates, hence the name of RDD family. Contains three transmembrane helices. The arginine occurs at the N terminus of the first helix and the first aspartate occurs in the middle of this helix. The molecular function of this protein is unknown; Localized in the cytoplasmic membrane; Family membership. | Heat shock protein 15; HSP15 is involved in the recycling of free 50S ribosomal subunits that still carry a nascent chain. Binds RNA more specifically than DNA. Binds with very high affinity to the free 50S ribosomal subunit. Does not bind it when it is part of the 70S ribosome; Induced by heat shock; Contains a S4 RNA-binding domain; Belongs to the HSP15 family; Localized in the cytoplasm; High confidence in function and specificity. | 0.553 |
| CAZ94610.1 | CAZ94608.1 | ZOBELLIA_539 | ZOBELLIA_537 | Conserved integral membrane protein belonging to the DUF95 family. Contains five transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | Conserved membrane protein containing two UPF0126 domains. The conserved glycines are suggestive of an ion channel. Contains seven transmembrane helices; Localized in the cytoplasmic membrane; Family membership. | 0.500 |
| CAZ94610.1 | CAZ94609.1 | ZOBELLIA_539 | ZOBELLIA_538 | Conserved integral membrane protein belonging to the DUF95 family. Contains five transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | This family of proteins contain three highly conserved amino acids: one arginine and two aspartates, hence the name of RDD family. Contains three transmembrane helices. The arginine occurs at the N terminus of the first helix and the first aspartate occurs in the middle of this helix. The molecular function of this protein is unknown; Localized in the cytoplasmic membrane; Family membership. | 0.934 |
| CAZ94610.1 | CAZ94611.1 | ZOBELLIA_539 | ZOBELLIA_540 | Conserved integral membrane protein belonging to the DUF95 family. Contains five transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | Conserved hypothetical membrane protein; Contains five transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 0.949 |