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 |
| CAZ94233.1 | CAZ96406.1 | ZOBELLIA_160 | ZOBELLIA_2250 | Similar to ASPIC and UnbV protein containing FG-GAP repeats; ASPIC and UnbV sequences are found associated with tetratrico peptide repeat in several paralogous proteins in Rhodopirellula baltica and with FG-GAP repeats in several eukaryotic integrin-like proteins and in several other bacterial proteins; The FG-GAP repeats are found in the N terminus of integrin alpha chains, a region that has been shown to be important for ligand binding; The FG-GAP repeat has been predicted to fold into a beta propeller structure; Contain a uncleavable signal peptide that Would localizes the protein i [...] | Vanadium-dependent Haloperoxidases catalyze the oxidation of halides such as bromide or chloride by hydrogen peroxide, which results in subsequent halogenation of organic substrates, or halide-assisted disproportionation of hydrogen peroxide forming dioxygen. They are likely to participate in the biosynthesis of halogenated natural products, such as volatile halogenated hydrocarbons, chiral halogenated terpenes, acetogenins and indoles; Signal peptide cleaved between the residues 21 and 22; localized in the periplasmic space; Specificity unclear. | 0.578 |
| CAZ94346.1 | CAZ96406.1 | ZOBELLIA_273 | ZOBELLIA_2250 | Similar to ASPIC and UnbV protein containing FG-GAP repeats; ASPIC and UnbV sequences are found associated with tetratrico peptide repeat in several paralogous proteins in Rhodopirellula baltica and with FG-GAP repeats in several eukaryotic integrin-like proteins and in several other bacterial proteins. The FG-GAP repeat has been predicted to fold into a beta propeller structure. The FG- GAP repeats are found in the N terminus of integrin alpha chains, a region that has been shown to be important for ligand binding; Contains a signal peptide of lipoprotein cleaved between the residues [...] | Vanadium-dependent Haloperoxidases catalyze the oxidation of halides such as bromide or chloride by hydrogen peroxide, which results in subsequent halogenation of organic substrates, or halide-assisted disproportionation of hydrogen peroxide forming dioxygen. They are likely to participate in the biosynthesis of halogenated natural products, such as volatile halogenated hydrocarbons, chiral halogenated terpenes, acetogenins and indoles; Signal peptide cleaved between the residues 21 and 22; localized in the periplasmic space; Specificity unclear. | 0.546 |
| CAZ96406.1 | CAZ94233.1 | ZOBELLIA_2250 | ZOBELLIA_160 | Vanadium-dependent Haloperoxidases catalyze the oxidation of halides such as bromide or chloride by hydrogen peroxide, which results in subsequent halogenation of organic substrates, or halide-assisted disproportionation of hydrogen peroxide forming dioxygen. They are likely to participate in the biosynthesis of halogenated natural products, such as volatile halogenated hydrocarbons, chiral halogenated terpenes, acetogenins and indoles; Signal peptide cleaved between the residues 21 and 22; localized in the periplasmic space; Specificity unclear. | Similar to ASPIC and UnbV protein containing FG-GAP repeats; ASPIC and UnbV sequences are found associated with tetratrico peptide repeat in several paralogous proteins in Rhodopirellula baltica and with FG-GAP repeats in several eukaryotic integrin-like proteins and in several other bacterial proteins; The FG-GAP repeats are found in the N terminus of integrin alpha chains, a region that has been shown to be important for ligand binding; The FG-GAP repeat has been predicted to fold into a beta propeller structure; Contain a uncleavable signal peptide that Would localizes the protein i [...] | 0.578 |
| CAZ96406.1 | CAZ94346.1 | ZOBELLIA_2250 | ZOBELLIA_273 | Vanadium-dependent Haloperoxidases catalyze the oxidation of halides such as bromide or chloride by hydrogen peroxide, which results in subsequent halogenation of organic substrates, or halide-assisted disproportionation of hydrogen peroxide forming dioxygen. They are likely to participate in the biosynthesis of halogenated natural products, such as volatile halogenated hydrocarbons, chiral halogenated terpenes, acetogenins and indoles; Signal peptide cleaved between the residues 21 and 22; localized in the periplasmic space; Specificity unclear. | Similar to ASPIC and UnbV protein containing FG-GAP repeats; ASPIC and UnbV sequences are found associated with tetratrico peptide repeat in several paralogous proteins in Rhodopirellula baltica and with FG-GAP repeats in several eukaryotic integrin-like proteins and in several other bacterial proteins. The FG-GAP repeat has been predicted to fold into a beta propeller structure. The FG- GAP repeats are found in the N terminus of integrin alpha chains, a region that has been shown to be important for ligand binding; Contains a signal peptide of lipoprotein cleaved between the residues [...] | 0.546 |
| CAZ96406.1 | CAZ96407.1 | ZOBELLIA_2250 | ZOBELLIA_2251 | Vanadium-dependent Haloperoxidases catalyze the oxidation of halides such as bromide or chloride by hydrogen peroxide, which results in subsequent halogenation of organic substrates, or halide-assisted disproportionation of hydrogen peroxide forming dioxygen. They are likely to participate in the biosynthesis of halogenated natural products, such as volatile halogenated hydrocarbons, chiral halogenated terpenes, acetogenins and indoles; Signal peptide cleaved between the residues 21 and 22; localized in the periplasmic space; Specificity unclear. | Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 0.603 |
| CAZ96406.1 | CAZ96566.1 | ZOBELLIA_2250 | ZOBELLIA_2413 | Vanadium-dependent Haloperoxidases catalyze the oxidation of halides such as bromide or chloride by hydrogen peroxide, which results in subsequent halogenation of organic substrates, or halide-assisted disproportionation of hydrogen peroxide forming dioxygen. They are likely to participate in the biosynthesis of halogenated natural products, such as volatile halogenated hydrocarbons, chiral halogenated terpenes, acetogenins and indoles; Signal peptide cleaved between the residues 21 and 22; localized in the periplasmic space; Specificity unclear. | ASPIC and UnbV sequences are found associated with tetratrico peptide repeat in several paralogous proteins in the bacteria Rhodopirellula baltica and with FG-GAP repeats in several eukaryotic integrin-like proteins and in several bacterial proteins. In integrins, the FG-GAP repeats are a important region for ligand binding; Contains a putatif lipoprotein signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Function unclear. | 0.642 |
| CAZ96406.1 | CAZ98831.1 | ZOBELLIA_2250 | ZOBELLIA_4696 | Vanadium-dependent Haloperoxidases catalyze the oxidation of halides such as bromide or chloride by hydrogen peroxide, which results in subsequent halogenation of organic substrates, or halide-assisted disproportionation of hydrogen peroxide forming dioxygen. They are likely to participate in the biosynthesis of halogenated natural products, such as volatile halogenated hydrocarbons, chiral halogenated terpenes, acetogenins and indoles; Signal peptide cleaved between the residues 21 and 22; localized in the periplasmic space; Specificity unclear. | Similar to ASPIC and UnbV protein containing FG-GAP repeats; ASPIC and UnbV sequences are found associated with tetratrico peptide repeat in several paralogous proteins in Rhodopirellula baltica and with FG-GAP repeats in several eukaryotic integrin-like proteins and in several other bacterial proteins. The FG-GAP repeat has been predicted to fold into a beta propeller structure. The FG- GAP repeats are found in the N terminus of integrin alpha chains, a region that has been shown to be important for ligand binding; Contains a signal peptide uncleavable (residues 5 to 23) that would lo [...] | 0.617 |
| CAZ96406.1 | CAZ98832.1 | ZOBELLIA_2250 | ZOBELLIA_4697 | Vanadium-dependent Haloperoxidases catalyze the oxidation of halides such as bromide or chloride by hydrogen peroxide, which results in subsequent halogenation of organic substrates, or halide-assisted disproportionation of hydrogen peroxide forming dioxygen. They are likely to participate in the biosynthesis of halogenated natural products, such as volatile halogenated hydrocarbons, chiral halogenated terpenes, acetogenins and indoles; Signal peptide cleaved between the residues 21 and 22; localized in the periplasmic space; Specificity unclear. | Similar to ASPIC and UnbV protein containing FG-GAP repeats; ASPIC and UnbV sequences are found associated with tetratrico peptide repeat in several paralogous proteins in Rhodopirellula baltica and with FG-GAP repeats in several eukaryotic integrin-like proteins and in several other bacterial proteins. The FG-GAP repeat has been predicted to fold into a beta propeller structure. The FG- GAP repeats are found in the N terminus of integrin alpha chains, a region that has been shown to be important for ligand binding; Contains a signal peptide of lipoprotein cleaved between the residues [...] | 0.559 |
| CAZ96406.1 | cat2 | ZOBELLIA_2250 | ZOBELLIA_2249 | Vanadium-dependent Haloperoxidases catalyze the oxidation of halides such as bromide or chloride by hydrogen peroxide, which results in subsequent halogenation of organic substrates, or halide-assisted disproportionation of hydrogen peroxide forming dioxygen. They are likely to participate in the biosynthesis of halogenated natural products, such as volatile halogenated hydrocarbons, chiral halogenated terpenes, acetogenins and indoles; Signal peptide cleaved between the residues 21 and 22; localized in the periplasmic space; Specificity unclear. | Catalysis of the transfer of a coenzyme A (CoA) group to 4-hydroxybutyrate; High confidence in function and specificity. | 0.491 |
| CAZ96406.1 | ccdA | ZOBELLIA_2250 | ZOBELLIA_2252 | Vanadium-dependent Haloperoxidases catalyze the oxidation of halides such as bromide or chloride by hydrogen peroxide, which results in subsequent halogenation of organic substrates, or halide-assisted disproportionation of hydrogen peroxide forming dioxygen. They are likely to participate in the biosynthesis of halogenated natural products, such as volatile halogenated hydrocarbons, chiral halogenated terpenes, acetogenins and indoles; Signal peptide cleaved between the residues 21 and 22; localized in the periplasmic space; Specificity unclear. | Belongs to the DsbD family. Like the Cytochrome C biogenesis protein CcdA from Bacillus subtilis, this protein is limited to the transmembrane region of DsbD. Preceded by the cytochrome cbb3 oxidase operon. Features six transmembrane helices. Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 0.541 |
| CAZ96406.1 | ccoG | ZOBELLIA_2250 | ZOBELLIA_2254 | Vanadium-dependent Haloperoxidases catalyze the oxidation of halides such as bromide or chloride by hydrogen peroxide, which results in subsequent halogenation of organic substrates, or halide-assisted disproportionation of hydrogen peroxide forming dioxygen. They are likely to participate in the biosynthesis of halogenated natural products, such as volatile halogenated hydrocarbons, chiral halogenated terpenes, acetogenins and indoles; Signal peptide cleaved between the residues 21 and 22; localized in the periplasmic space; Specificity unclear. | 4Fe-4S ferredoxin; Belongs to the ccoGHIS operon. Features five transmembrane helices. Localized in the cytoplasmic membrane; High confidence in function and specificity. | 0.512 |
| CAZ96406.1 | ccoH | ZOBELLIA_2250 | ZOBELLIA_2253 | Vanadium-dependent Haloperoxidases catalyze the oxidation of halides such as bromide or chloride by hydrogen peroxide, which results in subsequent halogenation of organic substrates, or halide-assisted disproportionation of hydrogen peroxide forming dioxygen. They are likely to participate in the biosynthesis of halogenated natural products, such as volatile halogenated hydrocarbons, chiral halogenated terpenes, acetogenins and indoles; Signal peptide cleaved between the residues 21 and 22; localized in the periplasmic space; Specificity unclear. | Protein that consists of a FixH family domain. Could be a cytochrome cbb3 oxidase maturation protein; Contains one N-terminal transmembrane helix; Localized in the cytoplasmic membrane; Family membership. | 0.541 |
| CAZ96407.1 | CAZ96406.1 | ZOBELLIA_2251 | ZOBELLIA_2250 | Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | Vanadium-dependent Haloperoxidases catalyze the oxidation of halides such as bromide or chloride by hydrogen peroxide, which results in subsequent halogenation of organic substrates, or halide-assisted disproportionation of hydrogen peroxide forming dioxygen. They are likely to participate in the biosynthesis of halogenated natural products, such as volatile halogenated hydrocarbons, chiral halogenated terpenes, acetogenins and indoles; Signal peptide cleaved between the residues 21 and 22; localized in the periplasmic space; Specificity unclear. | 0.603 |
| CAZ96407.1 | ccdA | ZOBELLIA_2251 | ZOBELLIA_2252 | Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | Belongs to the DsbD family. Like the Cytochrome C biogenesis protein CcdA from Bacillus subtilis, this protein is limited to the transmembrane region of DsbD. Preceded by the cytochrome cbb3 oxidase operon. Features six transmembrane helices. Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 0.689 |
| CAZ96407.1 | ccoG | ZOBELLIA_2251 | ZOBELLIA_2254 | Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 4Fe-4S ferredoxin; Belongs to the ccoGHIS operon. Features five transmembrane helices. Localized in the cytoplasmic membrane; High confidence in function and specificity. | 0.649 |
| CAZ96407.1 | ccoH | ZOBELLIA_2251 | ZOBELLIA_2253 | Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | Protein that consists of a FixH family domain. Could be a cytochrome cbb3 oxidase maturation protein; Contains one N-terminal transmembrane helix; Localized in the cytoplasmic membrane; Family membership. | 0.760 |
| CAZ96566.1 | CAZ96406.1 | ZOBELLIA_2413 | ZOBELLIA_2250 | ASPIC and UnbV sequences are found associated with tetratrico peptide repeat in several paralogous proteins in the bacteria Rhodopirellula baltica and with FG-GAP repeats in several eukaryotic integrin-like proteins and in several bacterial proteins. In integrins, the FG-GAP repeats are a important region for ligand binding; Contains a putatif lipoprotein signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Function unclear. | Vanadium-dependent Haloperoxidases catalyze the oxidation of halides such as bromide or chloride by hydrogen peroxide, which results in subsequent halogenation of organic substrates, or halide-assisted disproportionation of hydrogen peroxide forming dioxygen. They are likely to participate in the biosynthesis of halogenated natural products, such as volatile halogenated hydrocarbons, chiral halogenated terpenes, acetogenins and indoles; Signal peptide cleaved between the residues 21 and 22; localized in the periplasmic space; Specificity unclear. | 0.642 |
| CAZ98831.1 | CAZ96406.1 | ZOBELLIA_4696 | ZOBELLIA_2250 | Similar to ASPIC and UnbV protein containing FG-GAP repeats; ASPIC and UnbV sequences are found associated with tetratrico peptide repeat in several paralogous proteins in Rhodopirellula baltica and with FG-GAP repeats in several eukaryotic integrin-like proteins and in several other bacterial proteins. The FG-GAP repeat has been predicted to fold into a beta propeller structure. The FG- GAP repeats are found in the N terminus of integrin alpha chains, a region that has been shown to be important for ligand binding; Contains a signal peptide uncleavable (residues 5 to 23) that would lo [...] | Vanadium-dependent Haloperoxidases catalyze the oxidation of halides such as bromide or chloride by hydrogen peroxide, which results in subsequent halogenation of organic substrates, or halide-assisted disproportionation of hydrogen peroxide forming dioxygen. They are likely to participate in the biosynthesis of halogenated natural products, such as volatile halogenated hydrocarbons, chiral halogenated terpenes, acetogenins and indoles; Signal peptide cleaved between the residues 21 and 22; localized in the periplasmic space; Specificity unclear. | 0.617 |
| CAZ98831.1 | CAZ98832.1 | ZOBELLIA_4696 | ZOBELLIA_4697 | Similar to ASPIC and UnbV protein containing FG-GAP repeats; ASPIC and UnbV sequences are found associated with tetratrico peptide repeat in several paralogous proteins in Rhodopirellula baltica and with FG-GAP repeats in several eukaryotic integrin-like proteins and in several other bacterial proteins. The FG-GAP repeat has been predicted to fold into a beta propeller structure. The FG- GAP repeats are found in the N terminus of integrin alpha chains, a region that has been shown to be important for ligand binding; Contains a signal peptide uncleavable (residues 5 to 23) that would lo [...] | Similar to ASPIC and UnbV protein containing FG-GAP repeats; ASPIC and UnbV sequences are found associated with tetratrico peptide repeat in several paralogous proteins in Rhodopirellula baltica and with FG-GAP repeats in several eukaryotic integrin-like proteins and in several other bacterial proteins. The FG-GAP repeat has been predicted to fold into a beta propeller structure. The FG- GAP repeats are found in the N terminus of integrin alpha chains, a region that has been shown to be important for ligand binding; Contains a signal peptide of lipoprotein cleaved between the residues [...] | 0.744 |
| CAZ98832.1 | CAZ96406.1 | ZOBELLIA_4697 | ZOBELLIA_2250 | Similar to ASPIC and UnbV protein containing FG-GAP repeats; ASPIC and UnbV sequences are found associated with tetratrico peptide repeat in several paralogous proteins in Rhodopirellula baltica and with FG-GAP repeats in several eukaryotic integrin-like proteins and in several other bacterial proteins. The FG-GAP repeat has been predicted to fold into a beta propeller structure. The FG- GAP repeats are found in the N terminus of integrin alpha chains, a region that has been shown to be important for ligand binding; Contains a signal peptide of lipoprotein cleaved between the residues [...] | Vanadium-dependent Haloperoxidases catalyze the oxidation of halides such as bromide or chloride by hydrogen peroxide, which results in subsequent halogenation of organic substrates, or halide-assisted disproportionation of hydrogen peroxide forming dioxygen. They are likely to participate in the biosynthesis of halogenated natural products, such as volatile halogenated hydrocarbons, chiral halogenated terpenes, acetogenins and indoles; Signal peptide cleaved between the residues 21 and 22; localized in the periplasmic space; Specificity unclear. | 0.559 |
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