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 |
| azo0378 | fhuA2 | azo0378 | azo2610 | Putative TonB-dependent receptor. Homology to bpp0186 ao B. parapertussis of 54% (trembl|Q7W206) The TonB protein interacts with outer membrane receptor proteins that carry out high-affinity binding and energy-dependent uptake of specific substrates into the periplasmic space. These substrates are either poorly permeable through the porin channels or are encountered at very low concentrations. In the absence of TonB these receptors bind their substrates but do not carry out active transport. Interpro: TonB-dependent receptor (IPR000531) Pfam: TonB-dependent receptor (PF00593) signal Pe [...] | In E.coli this receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. Signal peptide; Specificity unclear. | 0.490 |
| azo0378 | fyuA | azo0378 | azo2347 | Putative TonB-dependent receptor. Homology to bpp0186 ao B. parapertussis of 54% (trembl|Q7W206) The TonB protein interacts with outer membrane receptor proteins that carry out high-affinity binding and energy-dependent uptake of specific substrates into the periplasmic space. These substrates are either poorly permeable through the porin channels or are encountered at very low concentrations. In the absence of TonB these receptors bind their substrates but do not carry out active transport. Interpro: TonB-dependent receptor (IPR000531) Pfam: TonB-dependent receptor (PF00593) signal Pe [...] | Putative TonB-dependent receptor; Yersinia enterocolitica,iron-repressible outer membrane protein, FyuA. FyuA:RECEPTOR FOR THE BACTERIOCIN PESTICIN AND FOR THE SIDEROPHORE YERSINIABACTIN. TonB-dependent outer membrane receptor; Function unclear. | 0.439 |
| azo1830 | fhuA2 | azo1830 | azo2610 | 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. | In E.coli this receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. Signal peptide; Specificity unclear. | 0.418 |
| azo1830 | fyuA | azo1830 | azo2347 | 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. | Putative TonB-dependent receptor; Yersinia enterocolitica,iron-repressible outer membrane protein, FyuA. FyuA:RECEPTOR FOR THE BACTERIOCIN PESTICIN AND FOR THE SIDEROPHORE YERSINIABACTIN. TonB-dependent outer membrane receptor; Function unclear. | 0.572 |
| azo2156 | fhuA2 | azo2156 | azo2610 | TonB-dependent outer membrane receptor involved in the first step of iron internalization and metabolism. A short conserved region so called the tonB-box is present in the sequence. This domain is involved in the interaction of the receptor with the TonB protein. Similar to a E. coli iron(III) dicitrate transport protein fecA precursor. InterPro: TonB-dependent receptor protein arcC: carbamate kinase; Function unclear. | In E.coli this receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. Signal peptide; Specificity unclear. | 0.421 |
| azo2156 | fyuA | azo2156 | azo2347 | TonB-dependent outer membrane receptor involved in the first step of iron internalization and metabolism. A short conserved region so called the tonB-box is present in the sequence. This domain is involved in the interaction of the receptor with the TonB protein. Similar to a E. coli iron(III) dicitrate transport protein fecA precursor. InterPro: TonB-dependent receptor protein arcC: carbamate kinase; Function unclear. | Putative TonB-dependent receptor; Yersinia enterocolitica,iron-repressible outer membrane protein, FyuA. FyuA:RECEPTOR FOR THE BACTERIOCIN PESTICIN AND FOR THE SIDEROPHORE YERSINIABACTIN. TonB-dependent outer membrane receptor; Function unclear. | 0.581 |
| azo2156 | ybiX | azo2156 | azo0608 | TonB-dependent outer membrane receptor involved in the first step of iron internalization and metabolism. A short conserved region so called the tonB-box is present in the sequence. This domain is involved in the interaction of the receptor with the TonB protein. Similar to a E. coli iron(III) dicitrate transport protein fecA precursor. InterPro: TonB-dependent receptor protein arcC: carbamate kinase; Function unclear. | Putative PKHD-type hydroxylase protein, 69% Identity(82% simialrity) to SwissProt;P59727,Q8FJM69, (48% identity) Has SMART;SM00702, P4Hc,Prolyl 4-hydroxylase alpha subunit homologues: IPR006620; Pro_4_hyd_alph; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor. Has PF03171,2OG-Fe(II) oxygenase superfamily;IPR005123;This family contains members of the 2-oxoglutarate [...] | 0.439 |
| azo2608 | azo2609 | azo2608 | azo2609 | Conserved hypothetical protein; 42% Aldolase_II_N.Class II Aldolase and Adducin N-terminal domain. Pfam: PF00596; Aldolase_II; 1. TIGR: PP2871; High confidence in function and specificity. | Conserved hypothetical endonuclease/exonuclease/phosphatase family protein. Homology to RPBDRAFT_0804 of Rhodopseudomonas palustris HaA2 of 315. Pfam: Exo_endo_phos. Endonuclease/Exonuclease/phosphatase family. This large family of proteins includes magnesium dependent endonucleases and a large number of phosphatases involved in intracellular signalling. This family includes: AP endonuclease proteins EC:4.2.99.18 e.g APEX1_HUMAN, DNase I proteins EC:3.1.21.1 e.g. DNAS1_HUMAN, Synaptojanin an inositol-1,4,5-trisphosphate phosphatase EC:3.1.3.56 SYNJ1_HUMAN, Sphingomyelinase EC:3.1.4.12 [...] | 0.450 |
| azo2608 | fhuA2 | azo2608 | azo2610 | Conserved hypothetical protein; 42% Aldolase_II_N.Class II Aldolase and Adducin N-terminal domain. Pfam: PF00596; Aldolase_II; 1. TIGR: PP2871; High confidence in function and specificity. | In E.coli this receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. Signal peptide; Specificity unclear. | 0.402 |
| azo2609 | azo2608 | azo2609 | azo2608 | Conserved hypothetical endonuclease/exonuclease/phosphatase family protein. Homology to RPBDRAFT_0804 of Rhodopseudomonas palustris HaA2 of 315. Pfam: Exo_endo_phos. Endonuclease/Exonuclease/phosphatase family. This large family of proteins includes magnesium dependent endonucleases and a large number of phosphatases involved in intracellular signalling. This family includes: AP endonuclease proteins EC:4.2.99.18 e.g APEX1_HUMAN, DNase I proteins EC:3.1.21.1 e.g. DNAS1_HUMAN, Synaptojanin an inositol-1,4,5-trisphosphate phosphatase EC:3.1.3.56 SYNJ1_HUMAN, Sphingomyelinase EC:3.1.4.12 [...] | Conserved hypothetical protein; 42% Aldolase_II_N.Class II Aldolase and Adducin N-terminal domain. Pfam: PF00596; Aldolase_II; 1. TIGR: PP2871; High confidence in function and specificity. | 0.450 |
| azo2609 | fhuA2 | azo2609 | azo2610 | Conserved hypothetical endonuclease/exonuclease/phosphatase family protein. Homology to RPBDRAFT_0804 of Rhodopseudomonas palustris HaA2 of 315. Pfam: Exo_endo_phos. Endonuclease/Exonuclease/phosphatase family. This large family of proteins includes magnesium dependent endonucleases and a large number of phosphatases involved in intracellular signalling. This family includes: AP endonuclease proteins EC:4.2.99.18 e.g APEX1_HUMAN, DNase I proteins EC:3.1.21.1 e.g. DNAS1_HUMAN, Synaptojanin an inositol-1,4,5-trisphosphate phosphatase EC:3.1.3.56 SYNJ1_HUMAN, Sphingomyelinase EC:3.1.4.12 [...] | In E.coli this receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. Signal peptide; Specificity unclear. | 0.511 |
| azo2611 | fhuA2 | azo2611 | azo2610 | Conserved hypothetical membrane protein. Homology to rs00511 of R. solanacearum of 32% (trembl|Q8XUW6(SRS)). No domains predicted. singal peptide. 2 TMHs; Conserved hypothetical protein. | In E.coli this receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. Signal peptide; Specificity unclear. | 0.754 |
| fhuA2 | azo0378 | azo2610 | azo0378 | In E.coli this receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. Signal peptide; Specificity unclear. | Putative TonB-dependent receptor. Homology to bpp0186 ao B. parapertussis of 54% (trembl|Q7W206) The TonB protein interacts with outer membrane receptor proteins that carry out high-affinity binding and energy-dependent uptake of specific substrates into the periplasmic space. These substrates are either poorly permeable through the porin channels or are encountered at very low concentrations. In the absence of TonB these receptors bind their substrates but do not carry out active transport. Interpro: TonB-dependent receptor (IPR000531) Pfam: TonB-dependent receptor (PF00593) signal Pe [...] | 0.490 |
| fhuA2 | azo1830 | azo2610 | azo1830 | In E.coli this receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. Signal peptide; Specificity unclear. | 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. | 0.418 |
| fhuA2 | azo2156 | azo2610 | azo2156 | In E.coli this receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. Signal peptide; Specificity unclear. | TonB-dependent outer membrane receptor involved in the first step of iron internalization and metabolism. A short conserved region so called the tonB-box is present in the sequence. This domain is involved in the interaction of the receptor with the TonB protein. Similar to a E. coli iron(III) dicitrate transport protein fecA precursor. InterPro: TonB-dependent receptor protein arcC: carbamate kinase; Function unclear. | 0.421 |
| fhuA2 | azo2608 | azo2610 | azo2608 | In E.coli this receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. Signal peptide; Specificity unclear. | Conserved hypothetical protein; 42% Aldolase_II_N.Class II Aldolase and Adducin N-terminal domain. Pfam: PF00596; Aldolase_II; 1. TIGR: PP2871; High confidence in function and specificity. | 0.402 |
| fhuA2 | azo2609 | azo2610 | azo2609 | In E.coli this receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. Signal peptide; Specificity unclear. | Conserved hypothetical endonuclease/exonuclease/phosphatase family protein. Homology to RPBDRAFT_0804 of Rhodopseudomonas palustris HaA2 of 315. Pfam: Exo_endo_phos. Endonuclease/Exonuclease/phosphatase family. This large family of proteins includes magnesium dependent endonucleases and a large number of phosphatases involved in intracellular signalling. This family includes: AP endonuclease proteins EC:4.2.99.18 e.g APEX1_HUMAN, DNase I proteins EC:3.1.21.1 e.g. DNAS1_HUMAN, Synaptojanin an inositol-1,4,5-trisphosphate phosphatase EC:3.1.3.56 SYNJ1_HUMAN, Sphingomyelinase EC:3.1.4.12 [...] | 0.511 |
| fhuA2 | azo2611 | azo2610 | azo2611 | In E.coli this receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. Signal peptide; Specificity unclear. | Conserved hypothetical membrane protein. Homology to rs00511 of R. solanacearum of 32% (trembl|Q8XUW6(SRS)). No domains predicted. singal peptide. 2 TMHs; Conserved hypothetical protein. | 0.754 |
| fhuA2 | fyuA | azo2610 | azo2347 | In E.coli this receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. Signal peptide; Specificity unclear. | Putative TonB-dependent receptor; Yersinia enterocolitica,iron-repressible outer membrane protein, FyuA. FyuA:RECEPTOR FOR THE BACTERIOCIN PESTICIN AND FOR THE SIDEROPHORE YERSINIABACTIN. TonB-dependent outer membrane receptor; Function unclear. | 0.418 |
| fhuA2 | ybiX | azo2610 | azo0608 | In E.coli this receptor binds the ferrichrome-iron ligand. It interacts with the tonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. Signal peptide; Specificity unclear. | Putative PKHD-type hydroxylase protein, 69% Identity(82% simialrity) to SwissProt;P59727,Q8FJM69, (48% identity) Has SMART;SM00702, P4Hc,Prolyl 4-hydroxylase alpha subunit homologues: IPR006620; Pro_4_hyd_alph; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor. Has PF03171,2OG-Fe(II) oxygenase superfamily;IPR005123;This family contains members of the 2-oxoglutarate [...] | 0.756 |
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