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 |
| EGJ26597.1 | EGJ27846.1 | STRPO_1544 | STRPO_1541 | M protein trans-acting positive regulator; Identified by match to protein family HMM PF05043; match to protein family HMM PF08270. | Deoxyguanosine kinase; Identified by match to protein family HMM PF01712. | 0.543 |
| EGJ26597.1 | dus | STRPO_1544 | STRPO_1542 | M protein trans-acting positive regulator; Identified by match to protein family HMM PF05043; match to protein family HMM PF08270. | Putative tRNA-dihydrouridine synthase B; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family. | 0.574 |
| EGJ26597.1 | hslO | STRPO_1544 | STRPO_1543 | M protein trans-acting positive regulator; Identified by match to protein family HMM PF05043; match to protein family HMM PF08270. | Chaperonin HslO; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.578 |
| EGJ26930.1 | fbpS | STRPO_1927 | STRPO_0147 | S4 domain protein; Identified by match to protein family HMM PF01479. | Fibronectin-binding protein A, N-terminal domain protein; An automated process has identified a potential problem with this gene model; the current end5 and/or the end3 may need to extended or the current gene model may need to be merged with a neighboring gene model; the current gene model (or a revised gene model) may contain a frame shift; identified by match to protein family HMM PF05670; match to protein family HMM PF05833. | 0.566 |
| EGJ26930.1 | hslO | STRPO_1927 | STRPO_1543 | S4 domain protein; Identified by match to protein family HMM PF01479. | Chaperonin HslO; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.497 |
| EGJ26930.1 | mrnC | STRPO_1927 | STRPO_1724 | S4 domain protein; Identified by match to protein family HMM PF01479. | RNase3 domain protein; Involved in correct processing of both the 5' and 3' ends of 23S rRNA precursor. Processes 30S rRNA precursor transcript even in absence of ribonuclease 3 (Rnc); Rnc processes 30S rRNA into smaller rRNA precursors; Belongs to the MrnC RNase family. | 0.762 |
| EGJ27355.1 | fbpS | STRPO_1398 | STRPO_0147 | S4 domain protein; Identified by match to protein family HMM PF01479. | Fibronectin-binding protein A, N-terminal domain protein; An automated process has identified a potential problem with this gene model; the current end5 and/or the end3 may need to extended or the current gene model may need to be merged with a neighboring gene model; the current gene model (or a revised gene model) may contain a frame shift; identified by match to protein family HMM PF05670; match to protein family HMM PF05833. | 0.928 |
| EGJ27355.1 | grpE | STRPO_1398 | STRPO_1063 | S4 domain protein; Identified by match to protein family HMM PF01479. | Co-chaperone GrpE; 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 ATP-depend [...] | 0.496 |
| EGJ27355.1 | hslO | STRPO_1398 | STRPO_1543 | S4 domain protein; Identified by match to protein family HMM PF01479. | Chaperonin HslO; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.785 |
| EGJ27846.1 | EGJ26597.1 | STRPO_1541 | STRPO_1544 | Deoxyguanosine kinase; Identified by match to protein family HMM PF01712. | M protein trans-acting positive regulator; Identified by match to protein family HMM PF05043; match to protein family HMM PF08270. | 0.543 |
| EGJ27846.1 | dus | STRPO_1541 | STRPO_1542 | Deoxyguanosine kinase; Identified by match to protein family HMM PF01712. | Putative tRNA-dihydrouridine synthase B; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family. | 0.761 |
| EGJ27846.1 | hslO | STRPO_1541 | STRPO_1543 | Deoxyguanosine kinase; Identified by match to protein family HMM PF01712. | Chaperonin HslO; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.750 |
| dnaJ | groL | STRPO_1061 | STRPO_1292 | 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 [...] | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.907 |
| dnaJ | grpE | STRPO_1061 | STRPO_1063 | 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 [...] | Co-chaperone GrpE; 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 ATP-depend [...] | 0.990 |
| dnaJ | hslO | STRPO_1061 | STRPO_1543 | 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 [...] | Chaperonin HslO; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.482 |
| dus | EGJ26597.1 | STRPO_1542 | STRPO_1544 | Putative tRNA-dihydrouridine synthase B; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family. | M protein trans-acting positive regulator; Identified by match to protein family HMM PF05043; match to protein family HMM PF08270. | 0.574 |
| dus | EGJ27846.1 | STRPO_1542 | STRPO_1541 | Putative tRNA-dihydrouridine synthase B; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family. | Deoxyguanosine kinase; Identified by match to protein family HMM PF01712. | 0.761 |
| dus | hslO | STRPO_1542 | STRPO_1543 | Putative tRNA-dihydrouridine synthase B; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family. | Chaperonin HslO; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.818 |
| fbpS | EGJ26930.1 | STRPO_0147 | STRPO_1927 | Fibronectin-binding protein A, N-terminal domain protein; An automated process has identified a potential problem with this gene model; the current end5 and/or the end3 may need to extended or the current gene model may need to be merged with a neighboring gene model; the current gene model (or a revised gene model) may contain a frame shift; identified by match to protein family HMM PF05670; match to protein family HMM PF05833. | S4 domain protein; Identified by match to protein family HMM PF01479. | 0.566 |
| fbpS | EGJ27355.1 | STRPO_0147 | STRPO_1398 | Fibronectin-binding protein A, N-terminal domain protein; An automated process has identified a potential problem with this gene model; the current end5 and/or the end3 may need to extended or the current gene model may need to be merged with a neighboring gene model; the current gene model (or a revised gene model) may contain a frame shift; identified by match to protein family HMM PF05670; match to protein family HMM PF05833. | S4 domain protein; Identified by match to protein family HMM PF01479. | 0.928 |
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