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 |
| Swoo_1175 | msrQ | Swoo_1175 | Swoo_2618 | PFAM: oxidoreductase molybdopterin binding; Mo-co oxidoreductase dimerisation domain; KEGG: spl:Spea_0981 oxidoreductase molybdopterin binding. | Ferric reductase domain protein transmembrane component domain; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the r [...] | 0.774 |
| Swoo_1890 | msrQ | Swoo_1890 | Swoo_2618 | PFAM: DoxX family protein; KEGG: sse:Ssed_2748 DoxX family protein. | Ferric reductase domain protein transmembrane component domain; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the r [...] | 0.484 |
| Swoo_2617 | msrQ | Swoo_2617 | Swoo_2618 | PFAM: histidine kinase HAMP region domain protein; chemotaxis sensory transducer; Cache type 2 domain protein; KEGG: sse:Ssed_1983 methyl-accepting chemotaxis sensory transducer. | Ferric reductase domain protein transmembrane component domain; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the r [...] | 0.438 |
| Swoo_2949 | msrP | Swoo_2949 | Swoo_2619 | PFAM: aldehyde oxidase and xanthine dehydrogenase molybdopterin binding; KEGG: slo:Shew_2265 aldehyde oxidase and xanthine dehydrogenase, molybdopterin binding. | Oxidoreductase molybdopterin binding; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce b [...] | 0.422 |
| Swoo_2949 | msrQ | Swoo_2949 | Swoo_2618 | PFAM: aldehyde oxidase and xanthine dehydrogenase molybdopterin binding; KEGG: slo:Shew_2265 aldehyde oxidase and xanthine dehydrogenase, molybdopterin binding. | Ferric reductase domain protein transmembrane component domain; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the r [...] | 0.410 |
| Swoo_3324 | msrQ | Swoo_3324 | Swoo_2618 | KEGG: sse:Ssed_1331 hypothetical protein. | Ferric reductase domain protein transmembrane component domain; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the r [...] | 0.437 |
| msrP | Swoo_2949 | Swoo_2619 | Swoo_2949 | Oxidoreductase molybdopterin binding; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce b [...] | PFAM: aldehyde oxidase and xanthine dehydrogenase molybdopterin binding; KEGG: slo:Shew_2265 aldehyde oxidase and xanthine dehydrogenase, molybdopterin binding. | 0.422 |
| msrP | msrQ | Swoo_2619 | Swoo_2618 | Oxidoreductase molybdopterin binding; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce b [...] | Ferric reductase domain protein transmembrane component domain; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the r [...] | 0.994 |
| msrQ | Swoo_1175 | Swoo_2618 | Swoo_1175 | Ferric reductase domain protein transmembrane component domain; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the r [...] | PFAM: oxidoreductase molybdopterin binding; Mo-co oxidoreductase dimerisation domain; KEGG: spl:Spea_0981 oxidoreductase molybdopterin binding. | 0.774 |
| msrQ | Swoo_1890 | Swoo_2618 | Swoo_1890 | Ferric reductase domain protein transmembrane component domain; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the r [...] | PFAM: DoxX family protein; KEGG: sse:Ssed_2748 DoxX family protein. | 0.484 |
| msrQ | Swoo_2617 | Swoo_2618 | Swoo_2617 | Ferric reductase domain protein transmembrane component domain; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the r [...] | PFAM: histidine kinase HAMP region domain protein; chemotaxis sensory transducer; Cache type 2 domain protein; KEGG: sse:Ssed_1983 methyl-accepting chemotaxis sensory transducer. | 0.438 |
| msrQ | Swoo_2949 | Swoo_2618 | Swoo_2949 | Ferric reductase domain protein transmembrane component domain; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the r [...] | PFAM: aldehyde oxidase and xanthine dehydrogenase molybdopterin binding; KEGG: slo:Shew_2265 aldehyde oxidase and xanthine dehydrogenase, molybdopterin binding. | 0.410 |
| msrQ | Swoo_3324 | Swoo_2618 | Swoo_3324 | Ferric reductase domain protein transmembrane component domain; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the r [...] | KEGG: sse:Ssed_1331 hypothetical protein. | 0.437 |
| msrQ | msrP | Swoo_2618 | Swoo_2619 | Ferric reductase domain protein transmembrane component domain; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the r [...] | Oxidoreductase molybdopterin binding; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce b [...] | 0.994 |