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 annotation | node2 annotation | score |
| azo0798 | azo1830 | Hypothetical secreted protein. No homology to the data bank. No domains predicted. No TMHs. Signal peptide present. | Putative TonB-denpendent receptor; Similar to FepA, an iron regulated outer membrane protein. FepA is a receptor for the siderophore complex ferric enterobactin and for colcins B and D. INVOLVED IN THE INITIAL STEP OF IRON UPTAKE BY BINDING FERRIC ENTEROBACTIN THAT ALLOWS E. COLI TO EXTRACT IRON FROM THE ENVIRONMENT. ilvC: ketol-acid reductoisomerase; Function unclear. | 0.787 |
| azo0798 | azo1873 | Hypothetical secreted protein. No homology to the data bank. No domains predicted. No TMHs. Signal peptide present. | Hypothetical protein, 26% Identity to TrEMBL;Q9PFZ1. No domains, repeats, motifs or features could be predicted above threshold. | 0.420 |
| azo1830 | azo0798 | Putative TonB-denpendent receptor; Similar to FepA, an iron regulated outer membrane protein. FepA is a receptor for the siderophore complex ferric enterobactin and for colcins B and D. INVOLVED IN THE INITIAL STEP OF IRON UPTAKE BY BINDING FERRIC ENTEROBACTIN THAT ALLOWS E. COLI TO EXTRACT IRON FROM THE ENVIRONMENT. ilvC: ketol-acid reductoisomerase; Function unclear. | Hypothetical secreted protein. No homology to the data bank. No domains predicted. No TMHs. Signal peptide present. | 0.787 |
| azo1830 | azo1873 | Putative TonB-denpendent receptor; Similar to FepA, an iron regulated outer membrane protein. FepA is a receptor for the siderophore complex ferric enterobactin and for colcins B and D. INVOLVED IN THE INITIAL STEP OF IRON UPTAKE BY BINDING FERRIC ENTEROBACTIN THAT ALLOWS E. COLI TO EXTRACT IRON FROM THE ENVIRONMENT. ilvC: ketol-acid reductoisomerase; Function unclear. | Hypothetical protein, 26% Identity to TrEMBL;Q9PFZ1. No domains, repeats, motifs or features could be predicted above threshold. | 0.437 |
| azo1868 | azo1869 | Hypothetical protein, very weak homology with hits in the Database. No Motifs,domains, or Signal peptide present. | Putative Hypothetical protein. Very weak homology with hits in the Database. No signficant domains, motifs or Signal Peptide present. | 0.773 |
| azo1868 | azo1870 | Hypothetical protein, very weak homology with hits in the Database. No Motifs,domains, or Signal peptide present. | Endopeptidase Clp; Putative protease encoded ATP-dependent Clp protease family protein similar(30 Identity,45% similarity in function) to TrEMBL:Q8X866. IPR001907. Has pfam00574,CLP_protease, Clp protease. The Clp protease has an active site catalytic triad. In E. coli Clp protease, ser-111,his-136 and asp-185 form the catalytic triad. One member has lost all of these active site residues and is therefore inactive. Some members contain one or two large insertions. Peptidase family S49 domain present. Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a [...] | 0.773 |
| azo1868 | azo1871 | Hypothetical protein, very weak homology with hits in the Database. No Motifs,domains, or Signal peptide present. | Hypothetical protein. | 0.497 |
| azo1868 | azo1872 | Hypothetical protein, very weak homology with hits in the Database. No Motifs,domains, or Signal peptide present. | Hypothetical phage tail tape measure protein. Controls phage tail length no signal peptide. no TMH. | 0.497 |
| azo1868 | azo1873 | Hypothetical protein, very weak homology with hits in the Database. No Motifs,domains, or Signal peptide present. | Hypothetical protein, 26% Identity to TrEMBL;Q9PFZ1. No domains, repeats, motifs or features could be predicted above threshold. | 0.497 |
| azo1869 | azo1868 | Putative Hypothetical protein. Very weak homology with hits in the Database. No signficant domains, motifs or Signal Peptide present. | Hypothetical protein, very weak homology with hits in the Database. No Motifs,domains, or Signal peptide present. | 0.773 |
| azo1869 | azo1870 | Putative Hypothetical protein. Very weak homology with hits in the Database. No signficant domains, motifs or Signal Peptide present. | Endopeptidase Clp; Putative protease encoded ATP-dependent Clp protease family protein similar(30 Identity,45% similarity in function) to TrEMBL:Q8X866. IPR001907. Has pfam00574,CLP_protease, Clp protease. The Clp protease has an active site catalytic triad. In E. coli Clp protease, ser-111,his-136 and asp-185 form the catalytic triad. One member has lost all of these active site residues and is therefore inactive. Some members contain one or two large insertions. Peptidase family S49 domain present. Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a [...] | 0.773 |
| azo1869 | azo1871 | Putative Hypothetical protein. Very weak homology with hits in the Database. No signficant domains, motifs or Signal Peptide present. | Hypothetical protein. | 0.497 |
| azo1869 | azo1872 | Putative Hypothetical protein. Very weak homology with hits in the Database. No signficant domains, motifs or Signal Peptide present. | Hypothetical phage tail tape measure protein. Controls phage tail length no signal peptide. no TMH. | 0.497 |
| azo1869 | azo1873 | Putative Hypothetical protein. Very weak homology with hits in the Database. No signficant domains, motifs or Signal Peptide present. | Hypothetical protein, 26% Identity to TrEMBL;Q9PFZ1. No domains, repeats, motifs or features could be predicted above threshold. | 0.497 |
| azo1870 | azo1868 | Endopeptidase Clp; Putative protease encoded ATP-dependent Clp protease family protein similar(30 Identity,45% similarity in function) to TrEMBL:Q8X866. IPR001907. Has pfam00574,CLP_protease, Clp protease. The Clp protease has an active site catalytic triad. In E. coli Clp protease, ser-111,his-136 and asp-185 form the catalytic triad. One member has lost all of these active site residues and is therefore inactive. Some members contain one or two large insertions. Peptidase family S49 domain present. Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a [...] | Hypothetical protein, very weak homology with hits in the Database. No Motifs,domains, or Signal peptide present. | 0.773 |
| azo1870 | azo1869 | Endopeptidase Clp; Putative protease encoded ATP-dependent Clp protease family protein similar(30 Identity,45% similarity in function) to TrEMBL:Q8X866. IPR001907. Has pfam00574,CLP_protease, Clp protease. The Clp protease has an active site catalytic triad. In E. coli Clp protease, ser-111,his-136 and asp-185 form the catalytic triad. One member has lost all of these active site residues and is therefore inactive. Some members contain one or two large insertions. Peptidase family S49 domain present. Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a [...] | Putative Hypothetical protein. Very weak homology with hits in the Database. No signficant domains, motifs or Signal Peptide present. | 0.773 |
| azo1870 | azo1871 | Endopeptidase Clp; Putative protease encoded ATP-dependent Clp protease family protein similar(30 Identity,45% similarity in function) to TrEMBL:Q8X866. IPR001907. Has pfam00574,CLP_protease, Clp protease. The Clp protease has an active site catalytic triad. In E. coli Clp protease, ser-111,his-136 and asp-185 form the catalytic triad. One member has lost all of these active site residues and is therefore inactive. Some members contain one or two large insertions. Peptidase family S49 domain present. Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a [...] | Hypothetical protein. | 0.497 |
| azo1870 | azo1872 | Endopeptidase Clp; Putative protease encoded ATP-dependent Clp protease family protein similar(30 Identity,45% similarity in function) to TrEMBL:Q8X866. IPR001907. Has pfam00574,CLP_protease, Clp protease. The Clp protease has an active site catalytic triad. In E. coli Clp protease, ser-111,his-136 and asp-185 form the catalytic triad. One member has lost all of these active site residues and is therefore inactive. Some members contain one or two large insertions. Peptidase family S49 domain present. Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a [...] | Hypothetical phage tail tape measure protein. Controls phage tail length no signal peptide. no TMH. | 0.637 |
| azo1870 | azo1873 | Endopeptidase Clp; Putative protease encoded ATP-dependent Clp protease family protein similar(30 Identity,45% similarity in function) to TrEMBL:Q8X866. IPR001907. Has pfam00574,CLP_protease, Clp protease. The Clp protease has an active site catalytic triad. In E. coli Clp protease, ser-111,his-136 and asp-185 form the catalytic triad. One member has lost all of these active site residues and is therefore inactive. Some members contain one or two large insertions. Peptidase family S49 domain present. Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a [...] | Hypothetical protein, 26% Identity to TrEMBL;Q9PFZ1. No domains, repeats, motifs or features could be predicted above threshold. | 0.608 |
| azo1871 | azo1868 | Hypothetical protein. | Hypothetical protein, very weak homology with hits in the Database. No Motifs,domains, or Signal peptide present. | 0.497 |
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