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 |
| 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 | CAZ94370.1 | ZOBELLIA_294 | ZOBELLIA_297 | Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | Conserved protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. contains various metallo-hydrolases including beta-lactamases, but also glyoxylases and arylsulfatases. The active site is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | 0.469 |
| 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 | CAZ94370.1 | ZOBELLIA_295 | ZOBELLIA_297 | 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 protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. contains various metallo-hydrolases including beta-lactamases, but also glyoxylases and arylsulfatases. The active site is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | 0.515 |
| 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 |
| CAZ94370.1 | CAZ94367.1 | ZOBELLIA_297 | ZOBELLIA_294 | Conserved protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. contains various metallo-hydrolases including beta-lactamases, but also glyoxylases and arylsulfatases. The active site is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 0.469 |
| CAZ94370.1 | CAZ94368.1 | ZOBELLIA_297 | ZOBELLIA_295 | Conserved protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. contains various metallo-hydrolases including beta-lactamases, but also glyoxylases and arylsulfatases. The active site is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | 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. | 0.515 |
| CAZ94370.1 | CAZ94457.1 | ZOBELLIA_297 | ZOBELLIA_384 | Conserved protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. contains various metallo-hydrolases including beta-lactamases, but also glyoxylases and arylsulfatases. The active site is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | Type I polyketide synthases are modular enzymes involved in the synthesis of various polyketides. This enzyme encompasses five modules: beta-ketoacyl synthase (KS), acyltransferase (AC), dehydratase (DH), enoyl reductase (ER) and acyl carrier protein (ACP). This modular enzyme is homologous to mycocerosic acid synthase (EC 2.3.1.111). Binds 1 phosphopantetheine group covalently. Localized in the cytoplasmic membrane; Specificity unclear. | 0.911 |
| CAZ94370.1 | CAZ96747.1 | ZOBELLIA_297 | ZOBELLIA_2597 | Conserved protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. contains various metallo-hydrolases including beta-lactamases, but also glyoxylases and arylsulfatases. The active site is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | Metallo-beta-lactamase superfamily protein; Protein with a N-terminal metallo beta-lactamase domain and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site Cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue; binds two zinc ions per molecule as cofactor; Localized in the cytoplasm; Function unclear. | 0.953 |
| CAZ94370.1 | CAZ98563.1 | ZOBELLIA_297 | ZOBELLIA_4428 | Conserved protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. contains various metallo-hydrolases including beta-lactamases, but also glyoxylases and arylsulfatases. The active site is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | Protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. The active site of the metallo-beta-lactamase domain is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | 0.960 |
| CAZ94370.1 | glpE2 | ZOBELLIA_297 | ZOBELLIA_296 | Conserved protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. contains various metallo-hydrolases including beta-lactamases, but also glyoxylases and arylsulfatases. The active site is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function 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. | 0.761 |
| CAZ94457.1 | CAZ94370.1 | ZOBELLIA_384 | ZOBELLIA_297 | Type I polyketide synthases are modular enzymes involved in the synthesis of various polyketides. This enzyme encompasses five modules: beta-ketoacyl synthase (KS), acyltransferase (AC), dehydratase (DH), enoyl reductase (ER) and acyl carrier protein (ACP). This modular enzyme is homologous to mycocerosic acid synthase (EC 2.3.1.111). Binds 1 phosphopantetheine group covalently. Localized in the cytoplasmic membrane; Specificity unclear. | Conserved protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. contains various metallo-hydrolases including beta-lactamases, but also glyoxylases and arylsulfatases. The active site is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | 0.911 |
| CAZ94457.1 | CAZ96747.1 | ZOBELLIA_384 | ZOBELLIA_2597 | Type I polyketide synthases are modular enzymes involved in the synthesis of various polyketides. This enzyme encompasses five modules: beta-ketoacyl synthase (KS), acyltransferase (AC), dehydratase (DH), enoyl reductase (ER) and acyl carrier protein (ACP). This modular enzyme is homologous to mycocerosic acid synthase (EC 2.3.1.111). Binds 1 phosphopantetheine group covalently. Localized in the cytoplasmic membrane; Specificity unclear. | Metallo-beta-lactamase superfamily protein; Protein with a N-terminal metallo beta-lactamase domain and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site Cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue; binds two zinc ions per molecule as cofactor; Localized in the cytoplasm; Function unclear. | 0.911 |
| CAZ94457.1 | CAZ98563.1 | ZOBELLIA_384 | ZOBELLIA_4428 | Type I polyketide synthases are modular enzymes involved in the synthesis of various polyketides. This enzyme encompasses five modules: beta-ketoacyl synthase (KS), acyltransferase (AC), dehydratase (DH), enoyl reductase (ER) and acyl carrier protein (ACP). This modular enzyme is homologous to mycocerosic acid synthase (EC 2.3.1.111). Binds 1 phosphopantetheine group covalently. Localized in the cytoplasmic membrane; Specificity unclear. | Protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. The active site of the metallo-beta-lactamase domain is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | 0.911 |
| CAZ94457.1 | glpE2 | ZOBELLIA_384 | ZOBELLIA_296 | Type I polyketide synthases are modular enzymes involved in the synthesis of various polyketides. This enzyme encompasses five modules: beta-ketoacyl synthase (KS), acyltransferase (AC), dehydratase (DH), enoyl reductase (ER) and acyl carrier protein (ACP). This modular enzyme is homologous to mycocerosic acid synthase (EC 2.3.1.111). Binds 1 phosphopantetheine group covalently. Localized in the cytoplasmic membrane; 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. | 0.426 |
| CAZ94457.1 | glpE4 | ZOBELLIA_384 | ZOBELLIA_1202 | Type I polyketide synthases are modular enzymes involved in the synthesis of various polyketides. This enzyme encompasses five modules: beta-ketoacyl synthase (KS), acyltransferase (AC), dehydratase (DH), enoyl reductase (ER) and acyl carrier protein (ACP). This modular enzyme is homologous to mycocerosic acid synthase (EC 2.3.1.111). Binds 1 phosphopantetheine group covalently. Localized in the cytoplasmic membrane; 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; Signal peptide cleaved between the residues 19 and 20; Localized in the periplasmic space; High confidence in function and specificity. | 0.426 |
| CAZ96747.1 | CAZ94370.1 | ZOBELLIA_2597 | ZOBELLIA_297 | Metallo-beta-lactamase superfamily protein; Protein with a N-terminal metallo beta-lactamase domain and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site Cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue; binds two zinc ions per molecule as cofactor; Localized in the cytoplasm; Function unclear. | Conserved protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. contains various metallo-hydrolases including beta-lactamases, but also glyoxylases and arylsulfatases. The active site is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | 0.953 |
| CAZ96747.1 | CAZ94457.1 | ZOBELLIA_2597 | ZOBELLIA_384 | Metallo-beta-lactamase superfamily protein; Protein with a N-terminal metallo beta-lactamase domain and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site Cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue; binds two zinc ions per molecule as cofactor; Localized in the cytoplasm; Function unclear. | Type I polyketide synthases are modular enzymes involved in the synthesis of various polyketides. This enzyme encompasses five modules: beta-ketoacyl synthase (KS), acyltransferase (AC), dehydratase (DH), enoyl reductase (ER) and acyl carrier protein (ACP). This modular enzyme is homologous to mycocerosic acid synthase (EC 2.3.1.111). Binds 1 phosphopantetheine group covalently. Localized in the cytoplasmic membrane; Specificity unclear. | 0.911 |
| CAZ96747.1 | CAZ98563.1 | ZOBELLIA_2597 | ZOBELLIA_4428 | Metallo-beta-lactamase superfamily protein; Protein with a N-terminal metallo beta-lactamase domain and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site Cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue; binds two zinc ions per molecule as cofactor; Localized in the cytoplasm; Function unclear. | Protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. The active site of the metallo-beta-lactamase domain is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear. | 0.959 |
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