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 |
| CAZ95357.1 | CAZ98252.1 | ZOBELLIA_1301 | ZOBELLIA_4117 | Hypothetical protein that contains a N-terminal LuxE domain; Localized in the cytoplasm. | Conserved hypothetical protein; Localized in the cytoplasm. | 0.837 |
| CAZ95357.1 | speA | ZOBELLIA_1301 | ZOBELLIA_2014 | Hypothetical protein that contains a N-terminal LuxE domain; Localized in the cytoplasm. | Arginine decarboxylase catalyzes the biosynthesis of agmatine from arginine. It is involved in the putrescine biosynthesis pathway. Uses the pyridoxal- phosphate as prosthetic group linked to a conserved lysine residue; Binds a magnesium ion; Localized in the cytoplasm; High confidence in function and specificity. | 0.551 |
| CAZ96115.1 | CAZ96118.1 | ZOBELLIA_2016 | ZOBELLIA_2017 | Deoxyhypusine synthase-like protein; Deoxyhypusine synthase transfers alkyl or aryl groups on an acceptor molecule. It likely catalyzes the NAD(+)-dependent dehydrogenation of spermidine, resulting in the formation of an enzyme-imine intermediate by transfer of the 4-aminobutylidene group from dehydrospermidine to the active site lysine residue. The 4-aminobutylidene group is then transfered from the enzyme intermediate to an acceptor molecule; Localized in the cytoplasm; Specificity unclear. | Conserved hypothetical protein; Localized in the cytoplasm. | 0.843 |
| CAZ96115.1 | CAZ96120.1 | ZOBELLIA_2016 | ZOBELLIA_2018 | Deoxyhypusine synthase-like protein; Deoxyhypusine synthase transfers alkyl or aryl groups on an acceptor molecule. It likely catalyzes the NAD(+)-dependent dehydrogenation of spermidine, resulting in the formation of an enzyme-imine intermediate by transfer of the 4-aminobutylidene group from dehydrospermidine to the active site lysine residue. The 4-aminobutylidene group is then transfered from the enzyme intermediate to an acceptor molecule; Localized in the cytoplasm; Specificity unclear. | N-acetyltransferase / Carbon-Nitrogen hydrolase; Modular protein composed of a N-terminal N-acetyltransferase domain of the GNAT family (residues 2-224) and a C-terminal Carbon-Nitrogen hydrolase domain (225-508). The Gcn5-related N-acetyltransferases (GNAT) catalyze the transfer of the acetyl from the Coenzyme A donor to a primary amine of an acceptor. The carbon-nitrogen hydrolase domain is involved in the reduction of organic nitrogen compounds and ammonia production; Localized in the cytoplasm; Specificity unclear. | 0.557 |
| CAZ96115.1 | rimK2 | ZOBELLIA_2016 | ZOBELLIA_2019 | Deoxyhypusine synthase-like protein; Deoxyhypusine synthase transfers alkyl or aryl groups on an acceptor molecule. It likely catalyzes the NAD(+)-dependent dehydrogenation of spermidine, resulting in the formation of an enzyme-imine intermediate by transfer of the 4-aminobutylidene group from dehydrospermidine to the active site lysine residue. The 4-aminobutylidene group is then transfered from the enzyme intermediate to an acceptor molecule; Localized in the cytoplasm; Specificity unclear. | Ribosomal protein S6 modification protein; RimK is responsible for the addition of glutamate residues to the C-terminus of ribosomal protein S6. This protein forms a dimer; Binds one ATP and 2 manganese ions by subunit; Contains a N-terminal domain of unknown function (DUF785); Localized in the cytoplasm; High confidence in function and specificity. | 0.527 |
| CAZ96115.1 | speA | ZOBELLIA_2016 | ZOBELLIA_2014 | Deoxyhypusine synthase-like protein; Deoxyhypusine synthase transfers alkyl or aryl groups on an acceptor molecule. It likely catalyzes the NAD(+)-dependent dehydrogenation of spermidine, resulting in the formation of an enzyme-imine intermediate by transfer of the 4-aminobutylidene group from dehydrospermidine to the active site lysine residue. The 4-aminobutylidene group is then transfered from the enzyme intermediate to an acceptor molecule; Localized in the cytoplasm; Specificity unclear. | Arginine decarboxylase catalyzes the biosynthesis of agmatine from arginine. It is involved in the putrescine biosynthesis pathway. Uses the pyridoxal- phosphate as prosthetic group linked to a conserved lysine residue; Binds a magnesium ion; Localized in the cytoplasm; High confidence in function and specificity. | 0.928 |
| CAZ96115.1 | speB | ZOBELLIA_2016 | ZOBELLIA_2015 | Deoxyhypusine synthase-like protein; Deoxyhypusine synthase transfers alkyl or aryl groups on an acceptor molecule. It likely catalyzes the NAD(+)-dependent dehydrogenation of spermidine, resulting in the formation of an enzyme-imine intermediate by transfer of the 4-aminobutylidene group from dehydrospermidine to the active site lysine residue. The 4-aminobutylidene group is then transfered from the enzyme intermediate to an acceptor molecule; Localized in the cytoplasm; Specificity unclear. | Agmatinase hydrolyses agmatine to putrescine, the precursor for the biosynthesis of higher polyamines, spermidine and spermine; Adopts a 3-layer alpha-beta-alpha fold; Binds a manganese ion; Belongs to the arginase family; Localized in the cytoplasm; High confidence in function and specificity. | 0.902 |
| CAZ96118.1 | CAZ96115.1 | ZOBELLIA_2017 | ZOBELLIA_2016 | Conserved hypothetical protein; Localized in the cytoplasm. | Deoxyhypusine synthase-like protein; Deoxyhypusine synthase transfers alkyl or aryl groups on an acceptor molecule. It likely catalyzes the NAD(+)-dependent dehydrogenation of spermidine, resulting in the formation of an enzyme-imine intermediate by transfer of the 4-aminobutylidene group from dehydrospermidine to the active site lysine residue. The 4-aminobutylidene group is then transfered from the enzyme intermediate to an acceptor molecule; Localized in the cytoplasm; Specificity unclear. | 0.843 |
| CAZ96118.1 | CAZ96120.1 | ZOBELLIA_2017 | ZOBELLIA_2018 | Conserved hypothetical protein; Localized in the cytoplasm. | N-acetyltransferase / Carbon-Nitrogen hydrolase; Modular protein composed of a N-terminal N-acetyltransferase domain of the GNAT family (residues 2-224) and a C-terminal Carbon-Nitrogen hydrolase domain (225-508). The Gcn5-related N-acetyltransferases (GNAT) catalyze the transfer of the acetyl from the Coenzyme A donor to a primary amine of an acceptor. The carbon-nitrogen hydrolase domain is involved in the reduction of organic nitrogen compounds and ammonia production; Localized in the cytoplasm; Specificity unclear. | 0.528 |
| CAZ96118.1 | rimK2 | ZOBELLIA_2017 | ZOBELLIA_2019 | Conserved hypothetical protein; Localized in the cytoplasm. | Ribosomal protein S6 modification protein; RimK is responsible for the addition of glutamate residues to the C-terminus of ribosomal protein S6. This protein forms a dimer; Binds one ATP and 2 manganese ions by subunit; Contains a N-terminal domain of unknown function (DUF785); Localized in the cytoplasm; High confidence in function and specificity. | 0.508 |
| CAZ96118.1 | speA | ZOBELLIA_2017 | ZOBELLIA_2014 | Conserved hypothetical protein; Localized in the cytoplasm. | Arginine decarboxylase catalyzes the biosynthesis of agmatine from arginine. It is involved in the putrescine biosynthesis pathway. Uses the pyridoxal- phosphate as prosthetic group linked to a conserved lysine residue; Binds a magnesium ion; Localized in the cytoplasm; High confidence in function and specificity. | 0.861 |
| CAZ96118.1 | speB | ZOBELLIA_2017 | ZOBELLIA_2015 | Conserved hypothetical protein; Localized in the cytoplasm. | Agmatinase hydrolyses agmatine to putrescine, the precursor for the biosynthesis of higher polyamines, spermidine and spermine; Adopts a 3-layer alpha-beta-alpha fold; Binds a manganese ion; Belongs to the arginase family; Localized in the cytoplasm; High confidence in function and specificity. | 0.867 |
| CAZ96120.1 | CAZ96115.1 | ZOBELLIA_2018 | ZOBELLIA_2016 | N-acetyltransferase / Carbon-Nitrogen hydrolase; Modular protein composed of a N-terminal N-acetyltransferase domain of the GNAT family (residues 2-224) and a C-terminal Carbon-Nitrogen hydrolase domain (225-508). The Gcn5-related N-acetyltransferases (GNAT) catalyze the transfer of the acetyl from the Coenzyme A donor to a primary amine of an acceptor. The carbon-nitrogen hydrolase domain is involved in the reduction of organic nitrogen compounds and ammonia production; Localized in the cytoplasm; Specificity unclear. | Deoxyhypusine synthase-like protein; Deoxyhypusine synthase transfers alkyl or aryl groups on an acceptor molecule. It likely catalyzes the NAD(+)-dependent dehydrogenation of spermidine, resulting in the formation of an enzyme-imine intermediate by transfer of the 4-aminobutylidene group from dehydrospermidine to the active site lysine residue. The 4-aminobutylidene group is then transfered from the enzyme intermediate to an acceptor molecule; Localized in the cytoplasm; Specificity unclear. | 0.557 |
| CAZ96120.1 | CAZ96118.1 | ZOBELLIA_2018 | ZOBELLIA_2017 | N-acetyltransferase / Carbon-Nitrogen hydrolase; Modular protein composed of a N-terminal N-acetyltransferase domain of the GNAT family (residues 2-224) and a C-terminal Carbon-Nitrogen hydrolase domain (225-508). The Gcn5-related N-acetyltransferases (GNAT) catalyze the transfer of the acetyl from the Coenzyme A donor to a primary amine of an acceptor. The carbon-nitrogen hydrolase domain is involved in the reduction of organic nitrogen compounds and ammonia production; Localized in the cytoplasm; Specificity unclear. | Conserved hypothetical protein; Localized in the cytoplasm. | 0.528 |
| CAZ96120.1 | rimK2 | ZOBELLIA_2018 | ZOBELLIA_2019 | N-acetyltransferase / Carbon-Nitrogen hydrolase; Modular protein composed of a N-terminal N-acetyltransferase domain of the GNAT family (residues 2-224) and a C-terminal Carbon-Nitrogen hydrolase domain (225-508). The Gcn5-related N-acetyltransferases (GNAT) catalyze the transfer of the acetyl from the Coenzyme A donor to a primary amine of an acceptor. The carbon-nitrogen hydrolase domain is involved in the reduction of organic nitrogen compounds and ammonia production; Localized in the cytoplasm; Specificity unclear. | Ribosomal protein S6 modification protein; RimK is responsible for the addition of glutamate residues to the C-terminus of ribosomal protein S6. This protein forms a dimer; Binds one ATP and 2 manganese ions by subunit; Contains a N-terminal domain of unknown function (DUF785); Localized in the cytoplasm; High confidence in function and specificity. | 0.777 |
| CAZ96120.1 | speA | ZOBELLIA_2018 | ZOBELLIA_2014 | N-acetyltransferase / Carbon-Nitrogen hydrolase; Modular protein composed of a N-terminal N-acetyltransferase domain of the GNAT family (residues 2-224) and a C-terminal Carbon-Nitrogen hydrolase domain (225-508). The Gcn5-related N-acetyltransferases (GNAT) catalyze the transfer of the acetyl from the Coenzyme A donor to a primary amine of an acceptor. The carbon-nitrogen hydrolase domain is involved in the reduction of organic nitrogen compounds and ammonia production; Localized in the cytoplasm; Specificity unclear. | Arginine decarboxylase catalyzes the biosynthesis of agmatine from arginine. It is involved in the putrescine biosynthesis pathway. Uses the pyridoxal- phosphate as prosthetic group linked to a conserved lysine residue; Binds a magnesium ion; Localized in the cytoplasm; High confidence in function and specificity. | 0.569 |
| CAZ96120.1 | speB | ZOBELLIA_2018 | ZOBELLIA_2015 | N-acetyltransferase / Carbon-Nitrogen hydrolase; Modular protein composed of a N-terminal N-acetyltransferase domain of the GNAT family (residues 2-224) and a C-terminal Carbon-Nitrogen hydrolase domain (225-508). The Gcn5-related N-acetyltransferases (GNAT) catalyze the transfer of the acetyl from the Coenzyme A donor to a primary amine of an acceptor. The carbon-nitrogen hydrolase domain is involved in the reduction of organic nitrogen compounds and ammonia production; Localized in the cytoplasm; Specificity unclear. | Agmatinase hydrolyses agmatine to putrescine, the precursor for the biosynthesis of higher polyamines, spermidine and spermine; Adopts a 3-layer alpha-beta-alpha fold; Binds a manganese ion; Belongs to the arginase family; Localized in the cytoplasm; High confidence in function and specificity. | 0.645 |
| CAZ98252.1 | CAZ95357.1 | ZOBELLIA_4117 | ZOBELLIA_1301 | Conserved hypothetical protein; Localized in the cytoplasm. | Hypothetical protein that contains a N-terminal LuxE domain; Localized in the cytoplasm. | 0.837 |
| CAZ98252.1 | speA | ZOBELLIA_4117 | ZOBELLIA_2014 | Conserved hypothetical protein; Localized in the cytoplasm. | Arginine decarboxylase catalyzes the biosynthesis of agmatine from arginine. It is involved in the putrescine biosynthesis pathway. Uses the pyridoxal- phosphate as prosthetic group linked to a conserved lysine residue; Binds a magnesium ion; Localized in the cytoplasm; High confidence in function and specificity. | 0.688 |
| CAZ98672.1 | speA | ZOBELLIA_4537 | ZOBELLIA_2014 | Conserved hypothetical protein; Localized in the cytoplasm. | Arginine decarboxylase catalyzes the biosynthesis of agmatine from arginine. It is involved in the putrescine biosynthesis pathway. Uses the pyridoxal- phosphate as prosthetic group linked to a conserved lysine residue; Binds a magnesium ion; Localized in the cytoplasm; High confidence in function and specificity. | 0.437 |
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