Export your current network:
... as a vector graphic:
SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc
... as short tabular text output:
TSV: tab separated values - can be opened in Excel and Cytoscape (lists only one-way edges: A-B)
... as tabular text output:
TSV: tab separated values - can be opened in Excel (lists reciprocal edges: A-B,B-A)
... as an XML summary:
structured XML interaction data, according to the 'PSI-MI' data standard
... protein node degrees:
node degree of proteins in your network (given the current score cut-off)
... network coordinates:
a flat-file format describing the coordinates and colors of nodes in the network
... protein sequences:
MFA: multi-fasta format - containing the aminoacid sequences in the network
... protein annotations:
a tab-delimited file describing the names, domains and descriptions of proteins in your network
... functional annotations:
a tab-delimited file containing all known functional terms of proteins in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CAZ97344.1 | arcB | ZOBELLIA_3206 | ZOBELLIA_4271 | Protein containing C-terminal leucine-rich repeats. Leucine-rich repeats consist of 2-45 motifs of 20-30 amino acids in length that generally folds into a horseshoe shape; Localized in the cytoplasm. | The Ornithine cyclodeaminase catalyses the deamination of ornithine to proline; The reaction uses the NAD as cofactor and is stimulated by the presence of ADP or ATP and is inhibited by O(2); Belongs to the mu- crystallin protein family; Localized in the cytoplasm; High confidence in function and specificity. | 0.507 |
| CAZ98148.1 | arcB | ZOBELLIA_4012 | ZOBELLIA_4271 | Proline racemase catalyzes the interconversion of L-and D-proline. It forms a homodimer. Localized in the cytoplasm; High confidence in function and specificity. | The Ornithine cyclodeaminase catalyses the deamination of ornithine to proline; The reaction uses the NAD as cofactor and is stimulated by the presence of ADP or ATP and is inhibited by O(2); Belongs to the mu- crystallin protein family; Localized in the cytoplasm; High confidence in function and specificity. | 0.650 |
| CAZ98404.1 | CAZ98405.1 | ZOBELLIA_4269 | ZOBELLIA_4270 | This enzyme belongs to the acid phosphatase/vanadium-dependent haloperoxidase family; Seems to have an uncleavable signal peptide; Possibly localized in the cytoplasmic membrane; Family membership. | The transcriptional regulators with the marR-type HTH domain control a variety of biological functions, including resistance to multiple antibiotics, household disinfectants, organic solvents, oxidative stress agents. Many of the marR-like regulators respond to aromatic compounds; Contains a DNA-binding, winged helix-turn-helix (wHTH) domain; Localized in the cytoplasm; Family membership. | 0.473 |
| CAZ98404.1 | arcB | ZOBELLIA_4269 | ZOBELLIA_4271 | This enzyme belongs to the acid phosphatase/vanadium-dependent haloperoxidase family; Seems to have an uncleavable signal peptide; Possibly localized in the cytoplasmic membrane; Family membership. | The Ornithine cyclodeaminase catalyses the deamination of ornithine to proline; The reaction uses the NAD as cofactor and is stimulated by the presence of ADP or ATP and is inhibited by O(2); Belongs to the mu- crystallin protein family; Localized in the cytoplasm; High confidence in function and specificity. | 0.473 |
| CAZ98405.1 | CAZ98404.1 | ZOBELLIA_4270 | ZOBELLIA_4269 | The transcriptional regulators with the marR-type HTH domain control a variety of biological functions, including resistance to multiple antibiotics, household disinfectants, organic solvents, oxidative stress agents. Many of the marR-like regulators respond to aromatic compounds; Contains a DNA-binding, winged helix-turn-helix (wHTH) domain; Localized in the cytoplasm; Family membership. | This enzyme belongs to the acid phosphatase/vanadium-dependent haloperoxidase family; Seems to have an uncleavable signal peptide; Possibly localized in the cytoplasmic membrane; Family membership. | 0.473 |
| CAZ98405.1 | CAZ98407.1 | ZOBELLIA_4270 | ZOBELLIA_4272 | The transcriptional regulators with the marR-type HTH domain control a variety of biological functions, including resistance to multiple antibiotics, household disinfectants, organic solvents, oxidative stress agents. Many of the marR-like regulators respond to aromatic compounds; Contains a DNA-binding, winged helix-turn-helix (wHTH) domain; Localized in the cytoplasm; Family membership. | Conserved hypothetical protein; Lipoprotein belonging to the spore coat protein H family; Signal peptide cleaved between the residues 19 and 20; Localized in the outer membrane. | 0.441 |
| CAZ98405.1 | arcB | ZOBELLIA_4270 | ZOBELLIA_4271 | The transcriptional regulators with the marR-type HTH domain control a variety of biological functions, including resistance to multiple antibiotics, household disinfectants, organic solvents, oxidative stress agents. Many of the marR-like regulators respond to aromatic compounds; Contains a DNA-binding, winged helix-turn-helix (wHTH) domain; Localized in the cytoplasm; Family membership. | The Ornithine cyclodeaminase catalyses the deamination of ornithine to proline; The reaction uses the NAD as cofactor and is stimulated by the presence of ADP or ATP and is inhibited by O(2); Belongs to the mu- crystallin protein family; Localized in the cytoplasm; High confidence in function and specificity. | 0.782 |
| CAZ98407.1 | CAZ98405.1 | ZOBELLIA_4272 | ZOBELLIA_4270 | Conserved hypothetical protein; Lipoprotein belonging to the spore coat protein H family; Signal peptide cleaved between the residues 19 and 20; Localized in the outer membrane. | The transcriptional regulators with the marR-type HTH domain control a variety of biological functions, including resistance to multiple antibiotics, household disinfectants, organic solvents, oxidative stress agents. Many of the marR-like regulators respond to aromatic compounds; Contains a DNA-binding, winged helix-turn-helix (wHTH) domain; Localized in the cytoplasm; Family membership. | 0.441 |
| CAZ98407.1 | arcB | ZOBELLIA_4272 | ZOBELLIA_4271 | Conserved hypothetical protein; Lipoprotein belonging to the spore coat protein H family; Signal peptide cleaved between the residues 19 and 20; Localized in the outer membrane. | The Ornithine cyclodeaminase catalyses the deamination of ornithine to proline; The reaction uses the NAD as cofactor and is stimulated by the presence of ADP or ATP and is inhibited by O(2); Belongs to the mu- crystallin protein family; Localized in the cytoplasm; High confidence in function and specificity. | 0.441 |
| arcB | CAZ97344.1 | ZOBELLIA_4271 | ZOBELLIA_3206 | The Ornithine cyclodeaminase catalyses the deamination of ornithine to proline; The reaction uses the NAD as cofactor and is stimulated by the presence of ADP or ATP and is inhibited by O(2); Belongs to the mu- crystallin protein family; Localized in the cytoplasm; High confidence in function and specificity. | Protein containing C-terminal leucine-rich repeats. Leucine-rich repeats consist of 2-45 motifs of 20-30 amino acids in length that generally folds into a horseshoe shape; Localized in the cytoplasm. | 0.507 |
| arcB | CAZ98148.1 | ZOBELLIA_4271 | ZOBELLIA_4012 | The Ornithine cyclodeaminase catalyses the deamination of ornithine to proline; The reaction uses the NAD as cofactor and is stimulated by the presence of ADP or ATP and is inhibited by O(2); Belongs to the mu- crystallin protein family; Localized in the cytoplasm; High confidence in function and specificity. | Proline racemase catalyzes the interconversion of L-and D-proline. It forms a homodimer. Localized in the cytoplasm; High confidence in function and specificity. | 0.650 |
| arcB | CAZ98404.1 | ZOBELLIA_4271 | ZOBELLIA_4269 | The Ornithine cyclodeaminase catalyses the deamination of ornithine to proline; The reaction uses the NAD as cofactor and is stimulated by the presence of ADP or ATP and is inhibited by O(2); Belongs to the mu- crystallin protein family; Localized in the cytoplasm; High confidence in function and specificity. | This enzyme belongs to the acid phosphatase/vanadium-dependent haloperoxidase family; Seems to have an uncleavable signal peptide; Possibly localized in the cytoplasmic membrane; Family membership. | 0.473 |
| arcB | CAZ98405.1 | ZOBELLIA_4271 | ZOBELLIA_4270 | The Ornithine cyclodeaminase catalyses the deamination of ornithine to proline; The reaction uses the NAD as cofactor and is stimulated by the presence of ADP or ATP and is inhibited by O(2); Belongs to the mu- crystallin protein family; Localized in the cytoplasm; High confidence in function and specificity. | The transcriptional regulators with the marR-type HTH domain control a variety of biological functions, including resistance to multiple antibiotics, household disinfectants, organic solvents, oxidative stress agents. Many of the marR-like regulators respond to aromatic compounds; Contains a DNA-binding, winged helix-turn-helix (wHTH) domain; Localized in the cytoplasm; Family membership. | 0.782 |
| arcB | CAZ98407.1 | ZOBELLIA_4271 | ZOBELLIA_4272 | The Ornithine cyclodeaminase catalyses the deamination of ornithine to proline; The reaction uses the NAD as cofactor and is stimulated by the presence of ADP or ATP and is inhibited by O(2); Belongs to the mu- crystallin protein family; Localized in the cytoplasm; High confidence in function and specificity. | Conserved hypothetical protein; Lipoprotein belonging to the spore coat protein H family; Signal peptide cleaved between the residues 19 and 20; Localized in the outer membrane. | 0.441 |