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 |
| CAZ94367.1 | CAZ94368.1 | ZOBELLIA_294 | ZOBELLIA_295 | Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | This protein belongs to the Heavy metal transport protein family. The Heavy-Metal-Associated (HMA) domain contains two conserved cysteines that are probably involved in metal binding. Its structure comprises our- stranded antiparallel beta-sheet and two alpha helices packed in an alpha-beta sandwich fold. Somes of these HMA proteins are involved in bacterial resistance to toxic metals, such as lead and cadmium. Localized in the cytoplasm; Specificity unclear. | 0.554 |
| CAZ94367.1 | glpE2 | ZOBELLIA_294 | ZOBELLIA_296 | Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | Thiosulfate sulfurtransferase catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide; The relatively low affinity of GlpE for both thiosulfate and cyanide suggests that these compounds are not the physiological substrates. Thioredoxin 1 or related dithiol proteins could instead be the physiological sulfur-acceptor substrate; Contains one only rhodanese domain; Localized in the cytoplasm; High confidence in function and specificity. | 0.464 |
| CAZ94368.1 | CAZ94367.1 | ZOBELLIA_295 | ZOBELLIA_294 | This protein belongs to the Heavy metal transport protein family. The Heavy-Metal-Associated (HMA) domain contains two conserved cysteines that are probably involved in metal binding. Its structure comprises our- stranded antiparallel beta-sheet and two alpha helices packed in an alpha-beta sandwich fold. Somes of these HMA proteins are involved in bacterial resistance to toxic metals, such as lead and cadmium. Localized in the cytoplasm; Specificity unclear. | Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 0.554 |
| CAZ94368.1 | CAZ95745.1 | ZOBELLIA_295 | ZOBELLIA_1691 | This protein belongs to the Heavy metal transport protein family. The Heavy-Metal-Associated (HMA) domain contains two conserved cysteines that are probably involved in metal binding. Its structure comprises our- stranded antiparallel beta-sheet and two alpha helices packed in an alpha-beta sandwich fold. Somes of these HMA proteins are involved in bacterial resistance to toxic metals, such as lead and cadmium. Localized in the cytoplasm; Specificity unclear. | Conserved hypothetical lipoprotein; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 19 and 20; Localized in the outer membrane; Conserved hypothetical protein. | 0.756 |
| CAZ94368.1 | CAZ96425.1 | ZOBELLIA_295 | ZOBELLIA_2269 | This protein belongs to the Heavy metal transport protein family. The Heavy-Metal-Associated (HMA) domain contains two conserved cysteines that are probably involved in metal binding. Its structure comprises our- stranded antiparallel beta-sheet and two alpha helices packed in an alpha-beta sandwich fold. Somes of these HMA proteins are involved in bacterial resistance to toxic metals, such as lead and cadmium. Localized in the cytoplasm; Specificity unclear. | Transcriptional repressor. The BlaI like repressors form homodimers that specifically bind DNA operator/promoter sequences. Followed by a blaR1-like regulator protein; High confidence in function and specificity. | 0.537 |
| CAZ94368.1 | CAZ96442.1 | ZOBELLIA_295 | ZOBELLIA_2286 | This protein belongs to the Heavy metal transport protein family. The Heavy-Metal-Associated (HMA) domain contains two conserved cysteines that are probably involved in metal binding. Its structure comprises our- stranded antiparallel beta-sheet and two alpha helices packed in an alpha-beta sandwich fold. Somes of these HMA proteins are involved in bacterial resistance to toxic metals, such as lead and cadmium. Localized in the cytoplasm; Specificity unclear. | BlaI-type transcriptional regulator are repressors usually involved in regulation of resistance to beta-lactams; The N-terminal region of these proteins is involved in DNA operator sequence recognition, while the C-terminal is responsible for dimerisation of the protein; Localized in the cytoplasm; High confidence in function and specificity. | 0.537 |
| CAZ94368.1 | CAZ97624.1 | ZOBELLIA_295 | ZOBELLIA_3486 | This protein belongs to the Heavy metal transport protein family. The Heavy-Metal-Associated (HMA) domain contains two conserved cysteines that are probably involved in metal binding. Its structure comprises our- stranded antiparallel beta-sheet and two alpha helices packed in an alpha-beta sandwich fold. Somes of these HMA proteins are involved in bacterial resistance to toxic metals, such as lead and cadmium. Localized in the cytoplasm; Specificity unclear. | Conserved hypothetical protein; Localized in the cytoplasm. | 0.664 |
| CAZ94368.1 | actP | ZOBELLIA_295 | ZOBELLIA_1166 | This protein belongs to the Heavy metal transport protein family. The Heavy-Metal-Associated (HMA) domain contains two conserved cysteines that are probably involved in metal binding. Its structure comprises our- stranded antiparallel beta-sheet and two alpha helices packed in an alpha-beta sandwich fold. Somes of these HMA proteins are involved in bacterial resistance to toxic metals, such as lead and cadmium. Localized in the cytoplasm; Specificity unclear. | ActP is a P-type ATPase responsible for copper efflux using ATP hydrolysis for energy. ActP controls copper homeostasis. Belongs to the cation transport P-type ATPase family. Features eight transmembrane helices. Localized in the cytoplasmic membrane; High confidence in function and specificity. | 0.603 |
| CAZ94368.1 | ccoI | ZOBELLIA_295 | ZOBELLIA_2260 | This protein belongs to the Heavy metal transport protein family. The Heavy-Metal-Associated (HMA) domain contains two conserved cysteines that are probably involved in metal binding. Its structure comprises our- stranded antiparallel beta-sheet and two alpha helices packed in an alpha-beta sandwich fold. Somes of these HMA proteins are involved in bacterial resistance to toxic metals, such as lead and cadmium. Localized in the cytoplasm; Specificity unclear. | Belongs to the cation transport P-type ATPase family. Involved in the ccoGHIS operon. Features eight transmembrane helices. Localized in the cytoplasmic membrane; Hypothetical protein. | 0.603 |
| CAZ94368.1 | glpE2 | ZOBELLIA_295 | ZOBELLIA_296 | This protein belongs to the Heavy metal transport protein family. The Heavy-Metal-Associated (HMA) domain contains two conserved cysteines that are probably involved in metal binding. Its structure comprises our- stranded antiparallel beta-sheet and two alpha helices packed in an alpha-beta sandwich fold. Somes of these HMA proteins are involved in bacterial resistance to toxic metals, such as lead and cadmium. Localized in the cytoplasm; Specificity unclear. | Thiosulfate sulfurtransferase catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide; The relatively low affinity of GlpE for both thiosulfate and cyanide suggests that these compounds are not the physiological substrates. Thioredoxin 1 or related dithiol proteins could instead be the physiological sulfur-acceptor substrate; Contains one only rhodanese domain; Localized in the cytoplasm; High confidence in function and specificity. | 0.651 |
| CAZ94368.1 | sodC | ZOBELLIA_295 | ZOBELLIA_114 | This protein belongs to the Heavy metal transport protein family. The Heavy-Metal-Associated (HMA) domain contains two conserved cysteines that are probably involved in metal binding. Its structure comprises our- stranded antiparallel beta-sheet and two alpha helices packed in an alpha-beta sandwich fold. Somes of these HMA proteins are involved in bacterial resistance to toxic metals, such as lead and cadmium. Localized in the cytoplasm; Specificity unclear. | Superoxide dismutase [Cu-Zn]; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the Cu-Zn superoxide dismutase family. | 0.756 |
| CAZ94368.1 | ziaA | ZOBELLIA_295 | ZOBELLIA_780 | This protein belongs to the Heavy metal transport protein family. The Heavy-Metal-Associated (HMA) domain contains two conserved cysteines that are probably involved in metal binding. Its structure comprises our- stranded antiparallel beta-sheet and two alpha helices packed in an alpha-beta sandwich fold. Somes of these HMA proteins are involved in bacterial resistance to toxic metals, such as lead and cadmium. Localized in the cytoplasm; Specificity unclear. | ZiaA is a P-type ATPase responsible for zinc efflux using ATP hydrolysis for energy. ZiaA controls zinc homeostasis. Belongs to the cation transport P-type ATPase family. Features six transmembrane helices. Localized in the cytoplasmic membrane; High confidence in function and specificity. | 0.603 |
| CAZ95745.1 | CAZ94368.1 | ZOBELLIA_1691 | ZOBELLIA_295 | Conserved hypothetical lipoprotein; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 19 and 20; Localized in the outer membrane; Conserved hypothetical protein. | This protein belongs to the Heavy metal transport protein family. The Heavy-Metal-Associated (HMA) domain contains two conserved cysteines that are probably involved in metal binding. Its structure comprises our- stranded antiparallel beta-sheet and two alpha helices packed in an alpha-beta sandwich fold. Somes of these HMA proteins are involved in bacterial resistance to toxic metals, such as lead and cadmium. Localized in the cytoplasm; Specificity unclear. | 0.756 |
| CAZ95745.1 | actP | ZOBELLIA_1691 | ZOBELLIA_1166 | Conserved hypothetical lipoprotein; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 19 and 20; Localized in the outer membrane; Conserved hypothetical protein. | ActP is a P-type ATPase responsible for copper efflux using ATP hydrolysis for energy. ActP controls copper homeostasis. Belongs to the cation transport P-type ATPase family. Features eight transmembrane helices. Localized in the cytoplasmic membrane; High confidence in function and specificity. | 0.939 |
| CAZ96425.1 | CAZ94368.1 | ZOBELLIA_2269 | ZOBELLIA_295 | Transcriptional repressor. The BlaI like repressors form homodimers that specifically bind DNA operator/promoter sequences. Followed by a blaR1-like regulator protein; High confidence in function and specificity. | This protein belongs to the Heavy metal transport protein family. The Heavy-Metal-Associated (HMA) domain contains two conserved cysteines that are probably involved in metal binding. Its structure comprises our- stranded antiparallel beta-sheet and two alpha helices packed in an alpha-beta sandwich fold. Somes of these HMA proteins are involved in bacterial resistance to toxic metals, such as lead and cadmium. Localized in the cytoplasm; Specificity unclear. | 0.537 |
| CAZ96425.1 | actP | ZOBELLIA_2269 | ZOBELLIA_1166 | Transcriptional repressor. The BlaI like repressors form homodimers that specifically bind DNA operator/promoter sequences. Followed by a blaR1-like regulator protein; High confidence in function and specificity. | ActP is a P-type ATPase responsible for copper efflux using ATP hydrolysis for energy. ActP controls copper homeostasis. Belongs to the cation transport P-type ATPase family. Features eight transmembrane helices. Localized in the cytoplasmic membrane; High confidence in function and specificity. | 0.682 |
| CAZ96442.1 | CAZ94368.1 | ZOBELLIA_2286 | ZOBELLIA_295 | BlaI-type transcriptional regulator are repressors usually involved in regulation of resistance to beta-lactams; The N-terminal region of these proteins is involved in DNA operator sequence recognition, while the C-terminal is responsible for dimerisation of the protein; Localized in the cytoplasm; High confidence in function and specificity. | This protein belongs to the Heavy metal transport protein family. The Heavy-Metal-Associated (HMA) domain contains two conserved cysteines that are probably involved in metal binding. Its structure comprises our- stranded antiparallel beta-sheet and two alpha helices packed in an alpha-beta sandwich fold. Somes of these HMA proteins are involved in bacterial resistance to toxic metals, such as lead and cadmium. Localized in the cytoplasm; Specificity unclear. | 0.537 |
| CAZ96442.1 | actP | ZOBELLIA_2286 | ZOBELLIA_1166 | BlaI-type transcriptional regulator are repressors usually involved in regulation of resistance to beta-lactams; The N-terminal region of these proteins is involved in DNA operator sequence recognition, while the C-terminal is responsible for dimerisation of the protein; Localized in the cytoplasm; High confidence in function and specificity. | ActP is a P-type ATPase responsible for copper efflux using ATP hydrolysis for energy. ActP controls copper homeostasis. Belongs to the cation transport P-type ATPase family. Features eight transmembrane helices. Localized in the cytoplasmic membrane; High confidence in function and specificity. | 0.682 |
| CAZ97624.1 | CAZ94368.1 | ZOBELLIA_3486 | ZOBELLIA_295 | Conserved hypothetical protein; Localized in the cytoplasm. | This protein belongs to the Heavy metal transport protein family. The Heavy-Metal-Associated (HMA) domain contains two conserved cysteines that are probably involved in metal binding. Its structure comprises our- stranded antiparallel beta-sheet and two alpha helices packed in an alpha-beta sandwich fold. Somes of these HMA proteins are involved in bacterial resistance to toxic metals, such as lead and cadmium. Localized in the cytoplasm; Specificity unclear. | 0.664 |
| actP | CAZ94368.1 | ZOBELLIA_1166 | ZOBELLIA_295 | ActP is a P-type ATPase responsible for copper efflux using ATP hydrolysis for energy. ActP controls copper homeostasis. Belongs to the cation transport P-type ATPase family. Features eight transmembrane helices. Localized in the cytoplasmic membrane; High confidence in function and specificity. | This protein belongs to the Heavy metal transport protein family. The Heavy-Metal-Associated (HMA) domain contains two conserved cysteines that are probably involved in metal binding. Its structure comprises our- stranded antiparallel beta-sheet and two alpha helices packed in an alpha-beta sandwich fold. Somes of these HMA proteins are involved in bacterial resistance to toxic metals, such as lead and cadmium. Localized in the cytoplasm; Specificity unclear. | 0.603 |
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