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 | crpA1 | ZOBELLIA_294 | ZOBELLIA_293 | Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | Catabolite gene activator; This protein complexes with cyclic AMP and binds to specific DNA sites near the promoter to regulate the transcription of several catabolite-sensitive operons. It displays a N-terminal cyclic nucleotide-binding domain and a C-terminal helix-turn-helix DNA-binding domain. The cyclic nucleotide-binding domain is composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure. There are six invariant amino acids in this domain, three of which are glycine residues that are thought to be essential for maintenance of the structu [...] | 0.690 |
| 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 | crpA1 | ZOBELLIA_295 | ZOBELLIA_293 | 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. | Catabolite gene activator; This protein complexes with cyclic AMP and binds to specific DNA sites near the promoter to regulate the transcription of several catabolite-sensitive operons. It displays a N-terminal cyclic nucleotide-binding domain and a C-terminal helix-turn-helix DNA-binding domain. The cyclic nucleotide-binding domain is composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure. There are six invariant amino acids in this domain, three of which are glycine residues that are thought to be essential for maintenance of the structu [...] | 0.434 |
| 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 | crpA1 | ZOBELLIA_297 | ZOBELLIA_293 | 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. | Catabolite gene activator; This protein complexes with cyclic AMP and binds to specific DNA sites near the promoter to regulate the transcription of several catabolite-sensitive operons. It displays a N-terminal cyclic nucleotide-binding domain and a C-terminal helix-turn-helix DNA-binding domain. The cyclic nucleotide-binding domain is composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure. There are six invariant amino acids in this domain, three of which are glycine residues that are thought to be essential for maintenance of the structu [...] | 0.422 |
| CAZ96491.1 | crpA1 | ZOBELLIA_2337 | ZOBELLIA_293 | Hypothetical membrane protein; Contains seven transmembrane segments; Localized in the cytoplasmic membrane; Hypothetical protein. | Catabolite gene activator; This protein complexes with cyclic AMP and binds to specific DNA sites near the promoter to regulate the transcription of several catabolite-sensitive operons. It displays a N-terminal cyclic nucleotide-binding domain and a C-terminal helix-turn-helix DNA-binding domain. The cyclic nucleotide-binding domain is composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure. There are six invariant amino acids in this domain, three of which are glycine residues that are thought to be essential for maintenance of the structu [...] | 0.422 |
| crpA1 | CAZ94367.1 | ZOBELLIA_293 | ZOBELLIA_294 | Catabolite gene activator; This protein complexes with cyclic AMP and binds to specific DNA sites near the promoter to regulate the transcription of several catabolite-sensitive operons. It displays a N-terminal cyclic nucleotide-binding domain and a C-terminal helix-turn-helix DNA-binding domain. The cyclic nucleotide-binding domain is composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure. There are six invariant amino acids in this domain, three of which are glycine residues that are thought to be essential for maintenance of the structu [...] | Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 0.690 |
| crpA1 | CAZ94368.1 | ZOBELLIA_293 | ZOBELLIA_295 | Catabolite gene activator; This protein complexes with cyclic AMP and binds to specific DNA sites near the promoter to regulate the transcription of several catabolite-sensitive operons. It displays a N-terminal cyclic nucleotide-binding domain and a C-terminal helix-turn-helix DNA-binding domain. The cyclic nucleotide-binding domain is composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure. There are six invariant amino acids in this domain, three of which are glycine residues that are thought to be essential for maintenance of the structu [...] | 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. | 0.434 |
| crpA1 | CAZ94370.1 | ZOBELLIA_293 | ZOBELLIA_297 | Catabolite gene activator; This protein complexes with cyclic AMP and binds to specific DNA sites near the promoter to regulate the transcription of several catabolite-sensitive operons. It displays a N-terminal cyclic nucleotide-binding domain and a C-terminal helix-turn-helix DNA-binding domain. The cyclic nucleotide-binding domain is composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure. There are six invariant amino acids in this domain, three of which are glycine residues that are thought to be essential for maintenance of the structu [...] | 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. | 0.422 |
| crpA1 | CAZ96491.1 | ZOBELLIA_293 | ZOBELLIA_2337 | Catabolite gene activator; This protein complexes with cyclic AMP and binds to specific DNA sites near the promoter to regulate the transcription of several catabolite-sensitive operons. It displays a N-terminal cyclic nucleotide-binding domain and a C-terminal helix-turn-helix DNA-binding domain. The cyclic nucleotide-binding domain is composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure. There are six invariant amino acids in this domain, three of which are glycine residues that are thought to be essential for maintenance of the structu [...] | Hypothetical membrane protein; Contains seven transmembrane segments; Localized in the cytoplasmic membrane; Hypothetical protein. | 0.422 |