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 |
| CAZ94840.1 | CAZ94841.1 | ZOBELLIA_774 | ZOBELLIA_775 | The pyridine nucleotide-disulphide reductases (PNDR) are thioredoxin reductase-like protein with a active site that is a redox-active disulfide bond. It uses the FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate; Localized in the cytoplasm; Family membership. | Hypothetical protein. Putatively localized in the cytoplasm. | 0.524 |
| CAZ94840.1 | CAZ94842.1 | ZOBELLIA_774 | ZOBELLIA_776 | The pyridine nucleotide-disulphide reductases (PNDR) are thioredoxin reductase-like protein with a active site that is a redox-active disulfide bond. It uses the FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate; Localized in the cytoplasm; Family membership. | The sensor histidine kinase belongs to two-component signal transduction systems. It catalyzes the ATP dependent autophosphorylation of a conserved histidine in its phosphoacceptor domain and the signal dependent phosphorylation of a conserved aspartic acid present in the response regulator receiver domain; Contains two transmembrane segments and one N-terminal tetratrico peptide motif (TPR); Localized in the cytoplasmic membrane; Family membership. | 0.514 |
| CAZ94840.1 | CAZ94843.1 | ZOBELLIA_774 | ZOBELLIA_777 | The pyridine nucleotide-disulphide reductases (PNDR) are thioredoxin reductase-like protein with a active site that is a redox-active disulfide bond. It uses the FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate; Localized in the cytoplasm; Family membership. | Response regulator proteins are involved in the two-component signal transduction systems to detect and respond to environmental changes. These proteins consist of two domains, an N-terminal response regulator receiver domain that is substrate for a histidine protein kinase sensor, and a variable C-terminal effector domain with DNA- binding activity (here, a LuxR-type HTH domain) that acts as transcriptional regulator; Family membership. | 0.514 |
| CAZ94840.1 | CAZ95937.1 | ZOBELLIA_774 | ZOBELLIA_1884 | The pyridine nucleotide-disulphide reductases (PNDR) are thioredoxin reductase-like protein with a active site that is a redox-active disulfide bond. It uses the FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate; Localized in the cytoplasm; Family membership. | Conserved hypothetical protein belonging to the DUF1094 family; Localized in the cytoplasm; Belongs to the UPF0403 family. | 0.694 |
| CAZ94840.1 | CAZ97884.1 | ZOBELLIA_774 | ZOBELLIA_3746 | The pyridine nucleotide-disulphide reductases (PNDR) are thioredoxin reductase-like protein with a active site that is a redox-active disulfide bond. It uses the FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate; Localized in the cytoplasm; Family membership. | Glycosyltransferase, family GT4; Glycosyltransferase catalyses the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; Belongs to the family 4 of the glycosyltransferases (GT4); Localized in the cytoplasm; Specificity unclear. | 0.557 |
| CAZ94840.1 | add | ZOBELLIA_774 | ZOBELLIA_772 | The pyridine nucleotide-disulphide reductases (PNDR) are thioredoxin reductase-like protein with a active site that is a redox-active disulfide bond. It uses the FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate; Localized in the cytoplasm; Family membership. | Adenosine deaminase; Catalyzes the hydrolytic deamination of adenine to hypoxanthine. Plays an important role in the purine salvage pathway and in nitrogen catabolism. | 0.529 |
| CAZ94840.1 | metB | ZOBELLIA_774 | ZOBELLIA_1454 | The pyridine nucleotide-disulphide reductases (PNDR) are thioredoxin reductase-like protein with a active site that is a redox-active disulfide bond. It uses the FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate; Localized in the cytoplasm; Family membership. | The Cystathionine gamma-synthase is found in the Selenoamino acid metabolism pathway and involved in the second step of the methionine biosynthesis; Uses a pyridoxal phosphate group as cofactor, attached to a lysine residue located in the central section of the enzyme; Localized in the cytoplasm; High confidence in function and specificity. | 0.905 |
| CAZ94840.1 | moeB | ZOBELLIA_774 | ZOBELLIA_3684 | The pyridine nucleotide-disulphide reductases (PNDR) are thioredoxin reductase-like protein with a active site that is a redox-active disulfide bond. It uses the FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate; Localized in the cytoplasm; Family membership. | Molybdopterin synthase activating protein; Enzyme involved in the biosynthesis of molybdopterin cofactor, necessary for molybdoenzymes. Plays a role in the activation of the small subunit of the molybdopterin converting factor (moaD); Contains a N- terminal transmembrane segment and a C-terminal rhodanese domain; Belongs to the hesA/moeB/thiF family; Localized in the cytoplasmic membrane; High confidence in function and specificity. | 0.547 |
| CAZ94840.1 | rpeA | ZOBELLIA_774 | ZOBELLIA_773 | The pyridine nucleotide-disulphide reductases (PNDR) are thioredoxin reductase-like protein with a active site that is a redox-active disulfide bond. It uses the FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate; Localized in the cytoplasm; Family membership. | Ribulose-phosphate 3-epimerase converts D-ribulose 5-phosphate into D-xylulose 5-phosphate in Pentose phosphate pathway; Adopts a a TIM barrel fold; Localized in the cytoplasm; High confidence in function and specificity. | 0.817 |
| CAZ94840.1 | sufS | ZOBELLIA_774 | ZOBELLIA_1842 | The pyridine nucleotide-disulphide reductases (PNDR) are thioredoxin reductase-like protein with a active site that is a redox-active disulfide bond. It uses the FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate; Localized in the cytoplasm; Family membership. | Cysteine desulfurase; Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine. | 0.905 |
| CAZ94841.1 | CAZ94840.1 | ZOBELLIA_775 | ZOBELLIA_774 | Hypothetical protein. Putatively localized in the cytoplasm. | The pyridine nucleotide-disulphide reductases (PNDR) are thioredoxin reductase-like protein with a active site that is a redox-active disulfide bond. It uses the FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate; Localized in the cytoplasm; Family membership. | 0.524 |
| CAZ94841.1 | CAZ94842.1 | ZOBELLIA_775 | ZOBELLIA_776 | Hypothetical protein. Putatively localized in the cytoplasm. | The sensor histidine kinase belongs to two-component signal transduction systems. It catalyzes the ATP dependent autophosphorylation of a conserved histidine in its phosphoacceptor domain and the signal dependent phosphorylation of a conserved aspartic acid present in the response regulator receiver domain; Contains two transmembrane segments and one N-terminal tetratrico peptide motif (TPR); Localized in the cytoplasmic membrane; Family membership. | 0.757 |
| CAZ94841.1 | CAZ94843.1 | ZOBELLIA_775 | ZOBELLIA_777 | Hypothetical protein. Putatively localized in the cytoplasm. | Response regulator proteins are involved in the two-component signal transduction systems to detect and respond to environmental changes. These proteins consist of two domains, an N-terminal response regulator receiver domain that is substrate for a histidine protein kinase sensor, and a variable C-terminal effector domain with DNA- binding activity (here, a LuxR-type HTH domain) that acts as transcriptional regulator; Family membership. | 0.757 |
| CAZ94841.1 | rpeA | ZOBELLIA_775 | ZOBELLIA_773 | Hypothetical protein. Putatively localized in the cytoplasm. | Ribulose-phosphate 3-epimerase converts D-ribulose 5-phosphate into D-xylulose 5-phosphate in Pentose phosphate pathway; Adopts a a TIM barrel fold; Localized in the cytoplasm; High confidence in function and specificity. | 0.524 |
| CAZ94842.1 | CAZ94840.1 | ZOBELLIA_776 | ZOBELLIA_774 | The sensor histidine kinase belongs to two-component signal transduction systems. It catalyzes the ATP dependent autophosphorylation of a conserved histidine in its phosphoacceptor domain and the signal dependent phosphorylation of a conserved aspartic acid present in the response regulator receiver domain; Contains two transmembrane segments and one N-terminal tetratrico peptide motif (TPR); Localized in the cytoplasmic membrane; Family membership. | The pyridine nucleotide-disulphide reductases (PNDR) are thioredoxin reductase-like protein with a active site that is a redox-active disulfide bond. It uses the FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate; Localized in the cytoplasm; Family membership. | 0.514 |
| CAZ94842.1 | CAZ94841.1 | ZOBELLIA_776 | ZOBELLIA_775 | The sensor histidine kinase belongs to two-component signal transduction systems. It catalyzes the ATP dependent autophosphorylation of a conserved histidine in its phosphoacceptor domain and the signal dependent phosphorylation of a conserved aspartic acid present in the response regulator receiver domain; Contains two transmembrane segments and one N-terminal tetratrico peptide motif (TPR); Localized in the cytoplasmic membrane; Family membership. | Hypothetical protein. Putatively localized in the cytoplasm. | 0.757 |
| CAZ94842.1 | CAZ94843.1 | ZOBELLIA_776 | ZOBELLIA_777 | The sensor histidine kinase belongs to two-component signal transduction systems. It catalyzes the ATP dependent autophosphorylation of a conserved histidine in its phosphoacceptor domain and the signal dependent phosphorylation of a conserved aspartic acid present in the response regulator receiver domain; Contains two transmembrane segments and one N-terminal tetratrico peptide motif (TPR); Localized in the cytoplasmic membrane; Family membership. | Response regulator proteins are involved in the two-component signal transduction systems to detect and respond to environmental changes. These proteins consist of two domains, an N-terminal response regulator receiver domain that is substrate for a histidine protein kinase sensor, and a variable C-terminal effector domain with DNA- binding activity (here, a LuxR-type HTH domain) that acts as transcriptional regulator; Family membership. | 0.966 |
| CAZ94842.1 | rpeA | ZOBELLIA_776 | ZOBELLIA_773 | The sensor histidine kinase belongs to two-component signal transduction systems. It catalyzes the ATP dependent autophosphorylation of a conserved histidine in its phosphoacceptor domain and the signal dependent phosphorylation of a conserved aspartic acid present in the response regulator receiver domain; Contains two transmembrane segments and one N-terminal tetratrico peptide motif (TPR); Localized in the cytoplasmic membrane; Family membership. | Ribulose-phosphate 3-epimerase converts D-ribulose 5-phosphate into D-xylulose 5-phosphate in Pentose phosphate pathway; Adopts a a TIM barrel fold; Localized in the cytoplasm; High confidence in function and specificity. | 0.525 |
| CAZ94843.1 | CAZ94840.1 | ZOBELLIA_777 | ZOBELLIA_774 | Response regulator proteins are involved in the two-component signal transduction systems to detect and respond to environmental changes. These proteins consist of two domains, an N-terminal response regulator receiver domain that is substrate for a histidine protein kinase sensor, and a variable C-terminal effector domain with DNA- binding activity (here, a LuxR-type HTH domain) that acts as transcriptional regulator; Family membership. | The pyridine nucleotide-disulphide reductases (PNDR) are thioredoxin reductase-like protein with a active site that is a redox-active disulfide bond. It uses the FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate; Localized in the cytoplasm; Family membership. | 0.514 |
| CAZ94843.1 | CAZ94841.1 | ZOBELLIA_777 | ZOBELLIA_775 | Response regulator proteins are involved in the two-component signal transduction systems to detect and respond to environmental changes. These proteins consist of two domains, an N-terminal response regulator receiver domain that is substrate for a histidine protein kinase sensor, and a variable C-terminal effector domain with DNA- binding activity (here, a LuxR-type HTH domain) that acts as transcriptional regulator; Family membership. | Hypothetical protein. Putatively localized in the cytoplasm. | 0.757 |
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