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 |
| CAZ95894.1 | sufD | ZOBELLIA_1841 | ZOBELLIA_1840 | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 20 and 21; Localized in the periplasmic space; Hypothetical protein. | The protein SufD is part of the SufBCD complex which acts synergistically with sufE to stimulate the cysteine desulfurase activity (SufS). The sufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation. Required for the stability of the fhuF protein; Localized in the cytoplasm; High confidence in function and specificity. | 0.481 |
| CAZ95894.1 | sufE | ZOBELLIA_1841 | ZOBELLIA_1843 | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 20 and 21; Localized in the periplasmic space; Hypothetical protein. | The protein SufE is a component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. SufE is an homodimeric scaffold protein that accepts sulfur atom from the cysteine desulfurase SufS and donates it to SufA. Cysteine desulfuration mobilizes sulfur from L-cysteine to yield L-alanine and constitutes an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules; Localized in the cytoplasm; High confidence in function and specificity. | 0.416 |
| CAZ95894.1 | sufS | ZOBELLIA_1841 | ZOBELLIA_1842 | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 20 and 21; Localized in the periplasmic space; Hypothetical protein. | Cysteine desulfurase; Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine. | 0.554 |
| sufD | CAZ95894.1 | ZOBELLIA_1840 | ZOBELLIA_1841 | The protein SufD is part of the SufBCD complex which acts synergistically with sufE to stimulate the cysteine desulfurase activity (SufS). The sufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation. Required for the stability of the fhuF protein; Localized in the cytoplasm; High confidence in function and specificity. | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 20 and 21; Localized in the periplasmic space; Hypothetical protein. | 0.481 |
| sufD | sufE | ZOBELLIA_1840 | ZOBELLIA_1843 | The protein SufD is part of the SufBCD complex which acts synergistically with sufE to stimulate the cysteine desulfurase activity (SufS). The sufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation. Required for the stability of the fhuF protein; Localized in the cytoplasm; High confidence in function and specificity. | The protein SufE is a component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. SufE is an homodimeric scaffold protein that accepts sulfur atom from the cysteine desulfurase SufS and donates it to SufA. Cysteine desulfuration mobilizes sulfur from L-cysteine to yield L-alanine and constitutes an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules; Localized in the cytoplasm; High confidence in function and specificity. | 0.802 |
| sufD | sufS | ZOBELLIA_1840 | ZOBELLIA_1842 | The protein SufD is part of the SufBCD complex which acts synergistically with sufE to stimulate the cysteine desulfurase activity (SufS). The sufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation. Required for the stability of the fhuF protein; Localized in the cytoplasm; High confidence in function and specificity. | Cysteine desulfurase; Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine. | 0.994 |
| sufE | CAZ95894.1 | ZOBELLIA_1843 | ZOBELLIA_1841 | The protein SufE is a component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. SufE is an homodimeric scaffold protein that accepts sulfur atom from the cysteine desulfurase SufS and donates it to SufA. Cysteine desulfuration mobilizes sulfur from L-cysteine to yield L-alanine and constitutes an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules; Localized in the cytoplasm; High confidence in function and specificity. | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 20 and 21; Localized in the periplasmic space; Hypothetical protein. | 0.416 |
| sufE | sufD | ZOBELLIA_1843 | ZOBELLIA_1840 | The protein SufE is a component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. SufE is an homodimeric scaffold protein that accepts sulfur atom from the cysteine desulfurase SufS and donates it to SufA. Cysteine desulfuration mobilizes sulfur from L-cysteine to yield L-alanine and constitutes an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules; Localized in the cytoplasm; High confidence in function and specificity. | The protein SufD is part of the SufBCD complex which acts synergistically with sufE to stimulate the cysteine desulfurase activity (SufS). The sufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation. Required for the stability of the fhuF protein; Localized in the cytoplasm; High confidence in function and specificity. | 0.802 |
| sufE | sufS | ZOBELLIA_1843 | ZOBELLIA_1842 | The protein SufE is a component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. SufE is an homodimeric scaffold protein that accepts sulfur atom from the cysteine desulfurase SufS and donates it to SufA. Cysteine desulfuration mobilizes sulfur from L-cysteine to yield L-alanine and constitutes an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules; Localized in the cytoplasm; High confidence in function and specificity. | Cysteine desulfurase; Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine. | 0.989 |
| sufS | CAZ95894.1 | ZOBELLIA_1842 | ZOBELLIA_1841 | Cysteine desulfurase; Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine. | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 20 and 21; Localized in the periplasmic space; Hypothetical protein. | 0.554 |
| sufS | sufD | ZOBELLIA_1842 | ZOBELLIA_1840 | Cysteine desulfurase; Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine. | The protein SufD is part of the SufBCD complex which acts synergistically with sufE to stimulate the cysteine desulfurase activity (SufS). The sufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation. Required for the stability of the fhuF protein; Localized in the cytoplasm; High confidence in function and specificity. | 0.994 |
| sufS | sufE | ZOBELLIA_1842 | ZOBELLIA_1843 | Cysteine desulfurase; Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine. | The protein SufE is a component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. SufE is an homodimeric scaffold protein that accepts sulfur atom from the cysteine desulfurase SufS and donates it to SufA. Cysteine desulfuration mobilizes sulfur from L-cysteine to yield L-alanine and constitutes an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules; Localized in the cytoplasm; High confidence in function and specificity. | 0.989 |