node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CAZ94686.1 | CAZ95263.1 | ZOBELLIA_615 | ZOBELLIA_1207 | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 22 and 23; Localized in the periplasmic space; Conserved hypothetical protein. | N-Acetylmuramoyl-L-alanine amidase hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in peptidoglycan; Contains a signal peptide cleaved between the residues 27 and 28; Localized in the periplasmic space; High confidence in function and specificity. | 0.533 |
CAZ94686.1 | CAZ95760.1 | ZOBELLIA_615 | ZOBELLIA_1707 | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 22 and 23; Localized in the periplasmic space; Conserved hypothetical protein. | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 22 and 23; Localized in the periplasmic space; Conserved hypothetical protein. | 0.480 |
CAZ94686.1 | CAZ98294.1 | ZOBELLIA_615 | ZOBELLIA_4159 | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 22 and 23; Localized in the periplasmic space; Conserved hypothetical protein. | Conserved hypothetical protein; Localized in the cytoplasm. | 0.665 |
CAZ94707.1 | CAZ95263.1 | ZOBELLIA_636 | ZOBELLIA_1207 | 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. | N-Acetylmuramoyl-L-alanine amidase hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in peptidoglycan; Contains a signal peptide cleaved between the residues 27 and 28; Localized in the periplasmic space; High confidence in function and specificity. | 0.403 |
CAZ94707.1 | CAZ95760.1 | ZOBELLIA_636 | ZOBELLIA_1707 | 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 periplasmic protein; Contains a signal peptide cleaved between the residues 22 and 23; Localized in the periplasmic space; Conserved hypothetical protein. | 0.611 |
CAZ94707.1 | CAZ98294.1 | ZOBELLIA_636 | ZOBELLIA_4159 | 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. | 0.588 |
CAZ95263.1 | CAZ94686.1 | ZOBELLIA_1207 | ZOBELLIA_615 | N-Acetylmuramoyl-L-alanine amidase hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in peptidoglycan; Contains a signal peptide cleaved between the residues 27 and 28; Localized in the periplasmic space; High confidence in function and specificity. | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 22 and 23; Localized in the periplasmic space; Conserved hypothetical protein. | 0.533 |
CAZ95263.1 | CAZ94707.1 | ZOBELLIA_1207 | ZOBELLIA_636 | N-Acetylmuramoyl-L-alanine amidase hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in peptidoglycan; Contains a signal peptide cleaved between the residues 27 and 28; Localized in the periplasmic space; High confidence in function and specificity. | 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. | 0.403 |
CAZ95263.1 | CAZ95760.1 | ZOBELLIA_1207 | ZOBELLIA_1707 | N-Acetylmuramoyl-L-alanine amidase hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in peptidoglycan; Contains a signal peptide cleaved between the residues 27 and 28; Localized in the periplasmic space; High confidence in function and specificity. | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 22 and 23; Localized in the periplasmic space; Conserved hypothetical protein. | 0.640 |
CAZ95263.1 | CAZ98294.1 | ZOBELLIA_1207 | ZOBELLIA_4159 | N-Acetylmuramoyl-L-alanine amidase hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in peptidoglycan; Contains a signal peptide cleaved between the residues 27 and 28; Localized in the periplasmic space; High confidence in function and specificity. | Conserved hypothetical protein; Localized in the cytoplasm. | 0.568 |
CAZ95760.1 | CAZ94686.1 | ZOBELLIA_1707 | ZOBELLIA_615 | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 22 and 23; Localized in the periplasmic space; Conserved hypothetical protein. | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 22 and 23; Localized in the periplasmic space; Conserved hypothetical protein. | 0.480 |
CAZ95760.1 | CAZ94707.1 | ZOBELLIA_1707 | ZOBELLIA_636 | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 22 and 23; Localized in the periplasmic space; Conserved 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. | 0.611 |
CAZ95760.1 | CAZ95263.1 | ZOBELLIA_1707 | ZOBELLIA_1207 | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 22 and 23; Localized in the periplasmic space; Conserved hypothetical protein. | N-Acetylmuramoyl-L-alanine amidase hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in peptidoglycan; Contains a signal peptide cleaved between the residues 27 and 28; Localized in the periplasmic space; High confidence in function and specificity. | 0.640 |
CAZ95760.1 | CAZ98294.1 | ZOBELLIA_1707 | ZOBELLIA_4159 | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 22 and 23; Localized in the periplasmic space; Conserved hypothetical protein. | Conserved hypothetical protein; Localized in the cytoplasm. | 0.553 |
CAZ95760.1 | CAZ98310.1 | ZOBELLIA_1707 | ZOBELLIA_4175 | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 22 and 23; Localized in the periplasmic space; Conserved hypothetical protein. | Conserved protein containing a von Willebrand factor type A (vWF) domain. vWF domains adopt a classic alpha/beta Rossmann fold and usually contains an unusual metal ion coordination site at its surface. Its exact function is unknown. Features a signal peptide cleaved between the residues 23 and 24. Localized in the periplasm; Family membership. | 0.763 |
CAZ98294.1 | CAZ94686.1 | ZOBELLIA_4159 | ZOBELLIA_615 | Conserved hypothetical protein; Localized in the cytoplasm. | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 22 and 23; Localized in the periplasmic space; Conserved hypothetical protein. | 0.665 |
CAZ98294.1 | CAZ94707.1 | ZOBELLIA_4159 | ZOBELLIA_636 | Conserved hypothetical protein; Localized in the cytoplasm. | 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. | 0.588 |
CAZ98294.1 | CAZ95263.1 | ZOBELLIA_4159 | ZOBELLIA_1207 | Conserved hypothetical protein; Localized in the cytoplasm. | N-Acetylmuramoyl-L-alanine amidase hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in peptidoglycan; Contains a signal peptide cleaved between the residues 27 and 28; Localized in the periplasmic space; High confidence in function and specificity. | 0.568 |
CAZ98294.1 | CAZ95760.1 | ZOBELLIA_4159 | ZOBELLIA_1707 | Conserved hypothetical protein; Localized in the cytoplasm. | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 22 and 23; Localized in the periplasmic space; Conserved hypothetical protein. | 0.553 |
CAZ98294.1 | CAZ98310.1 | ZOBELLIA_4159 | ZOBELLIA_4175 | Conserved hypothetical protein; Localized in the cytoplasm. | Conserved protein containing a von Willebrand factor type A (vWF) domain. vWF domains adopt a classic alpha/beta Rossmann fold and usually contains an unusual metal ion coordination site at its surface. Its exact function is unknown. Features a signal peptide cleaved between the residues 23 and 24. Localized in the periplasm; Family membership. | 0.738 |