| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CAZ94707.1 | CAZ95076.1 | ZOBELLIA_636 | ZOBELLIA_1019 | Conserved protein containing two N-terminal Calx-beta motifs separated by a CUB domain and followed by a C-terminal beta helix fold domain of unknown function. Calx-beta motifs are involved in calcium-binding. CUB domains contain four conserved cysteines which probably form two disulfide bridges. The structure of the CUB domain has been predicted to be a beta-barrel; Conserved hypothetical protein. | Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 22 and 23; Localized in the outer membrane; Hypothetical protein. | 0.427 |
| CAZ94707.1 | CAZ95328.1 | ZOBELLIA_636 | ZOBELLIA_1272 | Conserved protein containing two N-terminal Calx-beta motifs separated by a CUB domain and followed by a C-terminal beta helix fold domain of unknown function. Calx-beta motifs are involved in calcium-binding. CUB domains contain four conserved cysteines which probably form two disulfide bridges. The structure of the CUB domain has been predicted to be a beta-barrel; Conserved hypothetical protein. | Glycoside hydrolase, family GH114; Glycoside hydrolases hydrolyse the glycosidic bond between two or more carbohydrates or between a carbohydrate and a non-carbohydrate moiety. Belongs to the family 114 of the glycoside hydrolases. Family GH114 contains endo-alpha-1,4-polygalactosaminidases, but the specificity of this protein is unclear. Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 29 and 30. Localized in the outer membrane; Specificity unclear. | 0.425 |
| CAZ94707.1 | CAZ96813.1 | ZOBELLIA_636 | ZOBELLIA_2663 | Conserved protein containing two N-terminal Calx-beta motifs separated by a CUB domain and followed by a C-terminal beta helix fold domain of unknown function. Calx-beta motifs are involved in calcium-binding. CUB domains contain four conserved cysteines which probably form two disulfide bridges. The structure of the CUB domain has been predicted to be a beta-barrel; Conserved hypothetical protein. | CBM6 containing protein; Conserved protein featuring a N-terminal conserved domain of unknown function, a central PKD domain and a C-terminal carbohydrate binding module of the family 6. Features a signal peptide cleaved between the residues 21 and 22. Localized in the periplasm; Conserved hypothetical protein. | 0.432 |
| CAZ94707.1 | CAZ96814.1 | ZOBELLIA_636 | ZOBELLIA_2664 | Conserved protein containing two N-terminal Calx-beta motifs separated by a CUB domain and followed by a C-terminal beta helix fold domain of unknown function. Calx-beta motifs are involved in calcium-binding. CUB domains contain four conserved cysteines which probably form two disulfide bridges. The structure of the CUB domain has been predicted to be a beta-barrel; Conserved hypothetical protein. | Beta-helix fold protein; This protein likely adopts a right handed parallel beta-helix fold. Displays also a C-terminal PKD domain; Signal peptide cleaved between the residues 28 and 29; Localized in the periplasmic space; Function unclear. | 0.759 |
| CAZ94707.1 | CAZ96815.1 | ZOBELLIA_636 | ZOBELLIA_2665 | Conserved protein containing two N-terminal Calx-beta motifs separated by a CUB domain and followed by a C-terminal beta helix fold domain of unknown function. Calx-beta motifs are involved in calcium-binding. CUB domains contain four conserved cysteines which probably form two disulfide bridges. The structure of the CUB domain has been predicted to be a beta-barrel; Conserved hypothetical protein. | Modular protein containing a N-terminal domain adopting a parallel beta-helix fold and a C-terminal carbohydrate binding module of the family 13 (CBM13). The N-terminal domain is distantly related to the polysaccharide lyases of the family 9 (PL9). Features a signal peptide cleaved between residues 26 and 27. Localized in the periplasm; Specificity unclear. | 0.616 |
| CAZ94707.1 | CAZ97788.1 | ZOBELLIA_636 | ZOBELLIA_3650 | Conserved protein containing two N-terminal Calx-beta motifs separated by a CUB domain and followed by a C-terminal beta helix fold domain of unknown function. Calx-beta motifs are involved in calcium-binding. CUB domains contain four conserved cysteines which probably form two disulfide bridges. The structure of the CUB domain has been predicted to be a beta-barrel; Conserved hypothetical protein. | Conserved hypothetical protein; Contains a N-terminal DUF 11 domain. Protein that would bind calcium ions by several EF-hand calcium-binding domains or/and by trombospondin type III domains; Signal peptide cleaved between the residues 27 and 28; Putatively localized in the outer membrane. | 0.523 |
| CAZ94707.1 | CAZ98344.1 | ZOBELLIA_636 | ZOBELLIA_4209 | Conserved protein containing two N-terminal Calx-beta motifs separated by a CUB domain and followed by a C-terminal beta helix fold domain of unknown function. Calx-beta motifs are involved in calcium-binding. CUB domains contain four conserved cysteines which probably form two disulfide bridges. The structure of the CUB domain has been predicted to be a beta-barrel; Conserved hypothetical protein. | Conserved hypothetical protein; Putatively contains a C-terminal Globin-like domain; Probably localized in the cytoplasm. | 0.548 |
| CAZ94707.1 | CAZ98552.1 | ZOBELLIA_636 | ZOBELLIA_4417 | Conserved protein containing two N-terminal Calx-beta motifs separated by a CUB domain and followed by a C-terminal beta helix fold domain of unknown function. Calx-beta motifs are involved in calcium-binding. CUB domains contain four conserved cysteines which probably form two disulfide bridges. The structure of the CUB domain has been predicted to be a beta-barrel; Conserved hypothetical protein. | Conserved hypothetical protein; Localized in the cytoplasm. | 0.404 |
| CAZ95076.1 | CAZ94707.1 | ZOBELLIA_1019 | ZOBELLIA_636 | Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 22 and 23; Localized in the outer membrane; Hypothetical protein. | Conserved protein containing two N-terminal Calx-beta motifs separated by a CUB domain and followed by a C-terminal beta helix fold domain of unknown function. Calx-beta motifs are involved in calcium-binding. CUB domains contain four conserved cysteines which probably form two disulfide bridges. The structure of the CUB domain has been predicted to be a beta-barrel; Conserved hypothetical protein. | 0.427 |
| CAZ95076.1 | CAZ95328.1 | ZOBELLIA_1019 | ZOBELLIA_1272 | Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 22 and 23; Localized in the outer membrane; Hypothetical protein. | Glycoside hydrolase, family GH114; Glycoside hydrolases hydrolyse the glycosidic bond between two or more carbohydrates or between a carbohydrate and a non-carbohydrate moiety. Belongs to the family 114 of the glycoside hydrolases. Family GH114 contains endo-alpha-1,4-polygalactosaminidases, but the specificity of this protein is unclear. Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 29 and 30. Localized in the outer membrane; Specificity unclear. | 0.767 |
| CAZ95076.1 | CAZ96813.1 | ZOBELLIA_1019 | ZOBELLIA_2663 | Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 22 and 23; Localized in the outer membrane; Hypothetical protein. | CBM6 containing protein; Conserved protein featuring a N-terminal conserved domain of unknown function, a central PKD domain and a C-terminal carbohydrate binding module of the family 6. Features a signal peptide cleaved between the residues 21 and 22. Localized in the periplasm; Conserved hypothetical protein. | 0.589 |
| CAZ95076.1 | CAZ96814.1 | ZOBELLIA_1019 | ZOBELLIA_2664 | Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 22 and 23; Localized in the outer membrane; Hypothetical protein. | Beta-helix fold protein; This protein likely adopts a right handed parallel beta-helix fold. Displays also a C-terminal PKD domain; Signal peptide cleaved between the residues 28 and 29; Localized in the periplasmic space; Function unclear. | 0.770 |
| CAZ95076.1 | CAZ96815.1 | ZOBELLIA_1019 | ZOBELLIA_2665 | Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 22 and 23; Localized in the outer membrane; Hypothetical protein. | Modular protein containing a N-terminal domain adopting a parallel beta-helix fold and a C-terminal carbohydrate binding module of the family 13 (CBM13). The N-terminal domain is distantly related to the polysaccharide lyases of the family 9 (PL9). Features a signal peptide cleaved between residues 26 and 27. Localized in the periplasm; Specificity unclear. | 0.771 |
| CAZ95076.1 | CAZ97788.1 | ZOBELLIA_1019 | ZOBELLIA_3650 | Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 22 and 23; Localized in the outer membrane; Hypothetical protein. | Conserved hypothetical protein; Contains a N-terminal DUF 11 domain. Protein that would bind calcium ions by several EF-hand calcium-binding domains or/and by trombospondin type III domains; Signal peptide cleaved between the residues 27 and 28; Putatively localized in the outer membrane. | 0.772 |
| CAZ95076.1 | CAZ98344.1 | ZOBELLIA_1019 | ZOBELLIA_4209 | Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 22 and 23; Localized in the outer membrane; Hypothetical protein. | Conserved hypothetical protein; Putatively contains a C-terminal Globin-like domain; Probably localized in the cytoplasm. | 0.741 |
| CAZ95076.1 | CAZ98552.1 | ZOBELLIA_1019 | ZOBELLIA_4417 | Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 22 and 23; Localized in the outer membrane; Hypothetical protein. | Conserved hypothetical protein; Localized in the cytoplasm. | 0.764 |
| CAZ95076.1 | agaD | ZOBELLIA_1019 | ZOBELLIA_4243 | Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 22 and 23; Localized in the outer membrane; Hypothetical protein. | Beta-agarase D, family GH16; Cleaves the beta-1,4-linkages between beta-D-galactose and alpha-L-3,6-anhydro-galactose residues in agarose. Cleaves agarose in a random manner with retention of the anomeric-bond configuration, producing beta-anomers that give rise progressively to alpha-anomers when mutarotation takes place. Requires at least 4 consecutive agarose units and is highly intolerant to modifications. | 0.642 |
| CAZ95076.1 | pcaC | ZOBELLIA_1019 | ZOBELLIA_4479 | Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 22 and 23; Localized in the outer membrane; Hypothetical protein. | Modular protein displaying a N-terminal 4-carboxymuconolactone decarboxylase (CMD) domain and a C-terminal conserved domain of unknown function. CMD is involved in protocatechuate catabolism. It converts the 2-carboxy-2,5-dihydro-5-oxofuran-2-acetate to 4,5-dihydro-5-oxofuran-2-acetate; Localized in the cytoplasm:; High confidence in function and specificity. | 0.662 |
| CAZ95328.1 | CAZ94707.1 | ZOBELLIA_1272 | ZOBELLIA_636 | Glycoside hydrolase, family GH114; Glycoside hydrolases hydrolyse the glycosidic bond between two or more carbohydrates or between a carbohydrate and a non-carbohydrate moiety. Belongs to the family 114 of the glycoside hydrolases. Family GH114 contains endo-alpha-1,4-polygalactosaminidases, but the specificity of this protein is unclear. Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 29 and 30. Localized in the outer membrane; Specificity unclear. | Conserved protein containing two N-terminal Calx-beta motifs separated by a CUB domain and followed by a C-terminal beta helix fold domain of unknown function. Calx-beta motifs are involved in calcium-binding. CUB domains contain four conserved cysteines which probably form two disulfide bridges. The structure of the CUB domain has been predicted to be a beta-barrel; Conserved hypothetical protein. | 0.425 |
| CAZ95328.1 | CAZ95076.1 | ZOBELLIA_1272 | ZOBELLIA_1019 | Glycoside hydrolase, family GH114; Glycoside hydrolases hydrolyse the glycosidic bond between two or more carbohydrates or between a carbohydrate and a non-carbohydrate moiety. Belongs to the family 114 of the glycoside hydrolases. Family GH114 contains endo-alpha-1,4-polygalactosaminidases, but the specificity of this protein is unclear. Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 29 and 30. Localized in the outer membrane; Specificity unclear. | Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 22 and 23; Localized in the outer membrane; Hypothetical protein. | 0.767 |