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 |
| Rmet_1031 | fdx-2 | Rmet_1031 | Rmet_1030 | Conserved hypothetical protein. | Ferredoxin, 2Fe-2S type. | 0.995 |
| Rmet_1031 | hscA | Rmet_1031 | Rmet_1029 | Conserved hypothetical protein. | DnaK-like molecular chaperone specific for IscU; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.923 |
| Rmet_1031 | hscB | Rmet_1031 | Rmet_1028 | Conserved hypothetical protein. | DnaJ-like molecular chaperone specific for IscU; Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA; Belongs to the HscB family. | 0.967 |
| Rmet_1031 | iscS | Rmet_1031 | Rmet_1025 | Conserved hypothetical protein. | Cysteine desulfurase (tRNA sulfurtransferase), PLP-dependent; Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins. | 0.853 |
| Rmet_1031 | iscU | Rmet_1031 | Rmet_1026 | Conserved hypothetical protein. | FeS cluster assembly scaffold protein; A scaffold on which IscS assembles Fe-S clusters. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters. | 0.915 |
| Rmet_1823 | groL | Rmet_1823 | Rmet_0616 | Conserved hypothetical protein. | Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.793 |
| Rmet_1823 | grpE | Rmet_1823 | Rmet_1004 | Conserved hypothetical protein. | Heat shock/stress protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of AT [...] | 0.932 |
| Rmet_1823 | hscA | Rmet_1823 | Rmet_1029 | Conserved hypothetical protein. | DnaK-like molecular chaperone specific for IscU; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.952 |
| Rmet_1823 | htpG | Rmet_1823 | Rmet_2506 | Conserved hypothetical protein. | Molecular chaperone HSP90 family; Molecular chaperone. Has ATPase activity. | 0.932 |
| dnaJ | groL | Rmet_2921 | Rmet_0616 | Chaperone Hsp40, co-chaperone with DnaK; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interaction [...] | Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.916 |
| dnaJ | grpE | Rmet_2921 | Rmet_1004 | Chaperone Hsp40, co-chaperone with DnaK; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interaction [...] | Heat shock/stress protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of AT [...] | 0.973 |
| dnaJ | hscA | Rmet_2921 | Rmet_1029 | Chaperone Hsp40, co-chaperone with DnaK; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interaction [...] | DnaK-like molecular chaperone specific for IscU; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.987 |
| dnaJ | htpG | Rmet_2921 | Rmet_2506 | Chaperone Hsp40, co-chaperone with DnaK; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interaction [...] | Molecular chaperone HSP90 family; Molecular chaperone. Has ATPase activity. | 0.979 |
| fdx-2 | Rmet_1031 | Rmet_1030 | Rmet_1031 | Ferredoxin, 2Fe-2S type. | Conserved hypothetical protein. | 0.995 |
| fdx-2 | hscA | Rmet_1030 | Rmet_1029 | Ferredoxin, 2Fe-2S type. | DnaK-like molecular chaperone specific for IscU; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.966 |
| fdx-2 | hscB | Rmet_1030 | Rmet_1028 | Ferredoxin, 2Fe-2S type. | DnaJ-like molecular chaperone specific for IscU; Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA; Belongs to the HscB family. | 0.991 |
| fdx-2 | iscS | Rmet_1030 | Rmet_1025 | Ferredoxin, 2Fe-2S type. | Cysteine desulfurase (tRNA sulfurtransferase), PLP-dependent; Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins. | 0.958 |
| fdx-2 | iscU | Rmet_1030 | Rmet_1026 | Ferredoxin, 2Fe-2S type. | FeS cluster assembly scaffold protein; A scaffold on which IscS assembles Fe-S clusters. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters. | 0.986 |
| groL | Rmet_1823 | Rmet_0616 | Rmet_1823 | Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Conserved hypothetical protein. | 0.793 |
| groL | dnaJ | Rmet_0616 | Rmet_2921 | Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Chaperone Hsp40, co-chaperone with DnaK; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interaction [...] | 0.916 |
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