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 protiens in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AGB01369.1 | AGB03550.1 | Metfor_0290 | Metfor_2557 | PFAM: TCP-1/cpn60 chaperonin family; TIGRFAM: thermosome, various subunits, archaeal. | Molecular chaperone; PFAM: MreB/Mbl protein; Belongs to the heat shock protein 70 family. | 0.938 |
| AGB01369.1 | dnaJ | Metfor_0290 | Metfor_1652 | PFAM: TCP-1/cpn60 chaperonin family; TIGRFAM: thermosome, various subunits, archaeal. | Chaperone protein DnaJ; 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 interactions between DnaJ, D [...] | 0.936 |
| AGB01369.1 | dnaK | Metfor_0290 | Metfor_1653 | PFAM: TCP-1/cpn60 chaperonin family; TIGRFAM: thermosome, various subunits, archaeal. | Chaperone protein DnaK; Acts as a chaperone. | 0.938 |
| AGB01369.1 | grpE | Metfor_0290 | Metfor_1654 | PFAM: TCP-1/cpn60 chaperonin family; TIGRFAM: thermosome, various subunits, archaeal. | Molecular chaperone GrpE (heat shock 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. [...] | 0.957 |
| AGB01369.1 | pfdA | Metfor_0290 | Metfor_1107 | PFAM: TCP-1/cpn60 chaperonin family; TIGRFAM: thermosome, various subunits, archaeal. | Prefoldin alpha subunit/subunit 5; Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding. | 0.890 |
| AGB01369.1 | pfdB | Metfor_0290 | Metfor_1165 | PFAM: TCP-1/cpn60 chaperonin family; TIGRFAM: thermosome, various subunits, archaeal. | Prefoldin, beta subunit, archaeal; Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding. | 0.839 |
| AGB01369.1 | rpoD | Metfor_0290 | Metfor_0485 | PFAM: TCP-1/cpn60 chaperonin family; TIGRFAM: thermosome, various subunits, archaeal. | DNA-directed RNA polymerase, alpha subunit/40 kD subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.760 |
| AGB01369.1 | tfb | Metfor_0290 | Metfor_0346 | PFAM: TCP-1/cpn60 chaperonin family; TIGRFAM: thermosome, various subunits, archaeal. | Transcription initiation factor TFIIIB, Brf1 subunit/transcription initiation factor TFIIB; Stabilizes TBP binding to an archaeal box-A promoter. Also responsible for recruiting RNA polymerase II to the pre-initiation complex (DNA-TBP-TFIIB). | 0.562 |
| AGB01760.1 | AGB01763.1 | Metfor_0700 | Metfor_0703 | PFAM: Tetratricopeptide repeat. | PFAM: Aminotransferase class-III; TIGRFAM: acetylornithine and succinylornithine aminotransferases; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. | 0.442 |
| AGB01760.1 | AGB03550.1 | Metfor_0700 | Metfor_2557 | PFAM: Tetratricopeptide repeat. | Molecular chaperone; PFAM: MreB/Mbl protein; Belongs to the heat shock protein 70 family. | 0.808 |
| AGB01760.1 | dnaJ | Metfor_0700 | Metfor_1652 | PFAM: Tetratricopeptide repeat. | Chaperone protein DnaJ; 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 interactions between DnaJ, D [...] | 0.793 |
| AGB01760.1 | dnaK | Metfor_0700 | Metfor_1653 | PFAM: Tetratricopeptide repeat. | Chaperone protein DnaK; Acts as a chaperone. | 0.808 |
| AGB01760.1 | rpoD | Metfor_0700 | Metfor_0485 | PFAM: Tetratricopeptide repeat. | DNA-directed RNA polymerase, alpha subunit/40 kD subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.820 |
| AGB01763.1 | AGB01760.1 | Metfor_0703 | Metfor_0700 | PFAM: Aminotransferase class-III; TIGRFAM: acetylornithine and succinylornithine aminotransferases; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. | PFAM: Tetratricopeptide repeat. | 0.442 |
| AGB01763.1 | AGB02795.1 | Metfor_0703 | Metfor_1772 | PFAM: Aminotransferase class-III; TIGRFAM: acetylornithine and succinylornithine aminotransferases; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. | PFAM: Semialdehyde dehydrogenase, dimerisation domain; Semialdehyde dehydrogenase, NAD binding domain; TIGRFAM: aspartate-semialdehyde dehydrogenase (non-peptidoglycan organisms). | 0.634 |
| AGB01763.1 | argC | Metfor_0703 | Metfor_0084 | PFAM: Aminotransferase class-III; TIGRFAM: acetylornithine and succinylornithine aminotransferases; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. | N-acetyl-gamma-glutamyl-phosphate reductase, common form; Catalyzes the NADPH-dependent reduction of N-acetyl-5- glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. Belongs to the NAGSA dehydrogenase family. Type 1 subfamily. | 0.997 |
| AGB01763.1 | dnaJ | Metfor_0703 | Metfor_1652 | PFAM: Aminotransferase class-III; TIGRFAM: acetylornithine and succinylornithine aminotransferases; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. | Chaperone protein DnaJ; 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 interactions between DnaJ, D [...] | 0.736 |
| AGB01782.1 | AGB03550.1 | Metfor_0722 | Metfor_2557 | Thermosome subunit; PFAM: TCP-1/cpn60 chaperonin family; TIGRFAM: thermosome, various subunits, archaeal. | Molecular chaperone; PFAM: MreB/Mbl protein; Belongs to the heat shock protein 70 family. | 0.939 |
| AGB01782.1 | dnaJ | Metfor_0722 | Metfor_1652 | Thermosome subunit; PFAM: TCP-1/cpn60 chaperonin family; TIGRFAM: thermosome, various subunits, archaeal. | Chaperone protein DnaJ; 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 interactions between DnaJ, D [...] | 0.936 |
| AGB01782.1 | dnaK | Metfor_0722 | Metfor_1653 | Thermosome subunit; PFAM: TCP-1/cpn60 chaperonin family; TIGRFAM: thermosome, various subunits, archaeal. | Chaperone protein DnaK; Acts as a chaperone. | 0.940 |
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