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 |
| CAZ94322.1 | CAZ96783.1 | ZOBELLIA_249 | ZOBELLIA_2633 | Conserved hypothetical protein; Possibly localized in the cytoplasm. | Family M28 contains aminopeptidases and carboxypeptidases with two co-catalytic zinc ions (I and II). Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The zinc ligands occur in the sequence in the order His (II), Asp (I and II), Glu (I), Asp or Glu (II) and His (I). In addition, two other residues, an Asp and a Glu, are believed to be important for catalysis. Four of these residues occur in the motifs His-Xaa-Asp and Glu-Glu. Localized in the cytoplasm; Specificity unclear. | 0.415 |
| CAZ94793.1 | CAZ96783.1 | ZOBELLIA_727 | ZOBELLIA_2633 | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Features a signal p [...] | Family M28 contains aminopeptidases and carboxypeptidases with two co-catalytic zinc ions (I and II). Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The zinc ligands occur in the sequence in the order His (II), Asp (I and II), Glu (I), Asp or Glu (II) and His (I). In addition, two other residues, an Asp and a Glu, are believed to be important for catalysis. Four of these residues occur in the motifs His-Xaa-Asp and Glu-Glu. Localized in the cytoplasm; Specificity unclear. | 0.425 |
| CAZ94793.1 | CAZ96979.1 | ZOBELLIA_727 | ZOBELLIA_2832 | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Features a signal p [...] | Family M28 contains aminopeptidases and carboxypeptidases with two co-catalytic zinc ions (I and II). Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The zinc ligands occur in the sequence in the order His (II), Asp (I and II), Glu (I), Asp or Glu (II) and His (I). In addition, two other residues, an Asp and a Glu, are believed to be important for catalysis. Four of these residues occur in the motifs His-Xaa-Asp and Glu-Glu. Features a signal peptide cleaved between the residues 20 and 21. Loc [...] | 0.543 |
| CAZ94793.1 | dppA1 | ZOBELLIA_727 | ZOBELLIA_1190 | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Features a signal p [...] | Dipeptidyl-peptidase IV, family S9; Dipeptidyl-peptidase IV releases an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline. Belongs to the family S9 of the serine peptidases. The active site residues are in the order Ser, Asp, His in the sequence. The motif around the active site serine is G W S (Y/F) G G. DppA displays a two domain architecture, with a N-terminal eight-bladed beta-propeller and a C-terminal S9 peptidase domain. Features a signal peptide cleaved between the residues 20 and 21. Localiz [...] | 0.476 |
| CAZ95352.1 | CAZ96783.1 | ZOBELLIA_1296 | ZOBELLIA_2633 | Conserved hypothetical lipoprotein; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 26 and 27; Localized in the outer membrane; Conserved hypothetical protein. | Family M28 contains aminopeptidases and carboxypeptidases with two co-catalytic zinc ions (I and II). Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The zinc ligands occur in the sequence in the order His (II), Asp (I and II), Glu (I), Asp or Glu (II) and His (I). In addition, two other residues, an Asp and a Glu, are believed to be important for catalysis. Four of these residues occur in the motifs His-Xaa-Asp and Glu-Glu. Localized in the cytoplasm; Specificity unclear. | 0.420 |
| CAZ95578.1 | CAZ96783.1 | ZOBELLIA_1522 | ZOBELLIA_2633 | Prolyl oligopeptidase, family S9; Prolyl oligopeptidase cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long. Has an absolute requirement for an X-Pro bond in the trans configuration immediately preceding the Pro-Y scissible bond; Belongs to the family S9 of the peptidases; Contains a putative lipoprotein signal peptide cleaved between the residues 16 and 17; Possibly localized in the outer membrane; High confidence in function and specificity. | Family M28 contains aminopeptidases and carboxypeptidases with two co-catalytic zinc ions (I and II). Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The zinc ligands occur in the sequence in the order His (II), Asp (I and II), Glu (I), Asp or Glu (II) and His (I). In addition, two other residues, an Asp and a Glu, are believed to be important for catalysis. Four of these residues occur in the motifs His-Xaa-Asp and Glu-Glu. Localized in the cytoplasm; Specificity unclear. | 0.424 |
| CAZ95578.1 | dppA1 | ZOBELLIA_1522 | ZOBELLIA_1190 | Prolyl oligopeptidase, family S9; Prolyl oligopeptidase cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long. Has an absolute requirement for an X-Pro bond in the trans configuration immediately preceding the Pro-Y scissible bond; Belongs to the family S9 of the peptidases; Contains a putative lipoprotein signal peptide cleaved between the residues 16 and 17; Possibly localized in the outer membrane; High confidence in function and specificity. | Dipeptidyl-peptidase IV, family S9; Dipeptidyl-peptidase IV releases an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline. Belongs to the family S9 of the serine peptidases. The active site residues are in the order Ser, Asp, His in the sequence. The motif around the active site serine is G W S (Y/F) G G. DppA displays a two domain architecture, with a N-terminal eight-bladed beta-propeller and a C-terminal S9 peptidase domain. Features a signal peptide cleaved between the residues 20 and 21. Localiz [...] | 0.420 |
| CAZ96780.1 | CAZ96781.1 | ZOBELLIA_2630 | ZOBELLIA_2631 | 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. Localized in the cytoplasmic membrane; Specificity unclear. | The 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 winged-helix DNA-binding domain) that acts as transcriptional regulator; Family membership. | 0.968 |
| CAZ96780.1 | CAZ96782.1 | ZOBELLIA_2630 | ZOBELLIA_2632 | 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. Localized in the cytoplasmic membrane; Specificity unclear. | Amidohydrolase; This protein would catalyse the hydrolysis of amide or amine bonds in various substrates. It adopts a classical alpha-beta TIM-barrel fold. The active site is located in the mouth of the enzyme barrel and contains a bound iron ion that coordinates a hydroxyl nucleophile; Belongs to the Amidohydrolase family; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 24 and 25; Localized in the outer membrane; Specificity unclear. | 0.527 |
| CAZ96780.1 | CAZ96783.1 | ZOBELLIA_2630 | ZOBELLIA_2633 | 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. Localized in the cytoplasmic membrane; Specificity unclear. | Family M28 contains aminopeptidases and carboxypeptidases with two co-catalytic zinc ions (I and II). Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The zinc ligands occur in the sequence in the order His (II), Asp (I and II), Glu (I), Asp or Glu (II) and His (I). In addition, two other residues, an Asp and a Glu, are believed to be important for catalysis. Four of these residues occur in the motifs His-Xaa-Asp and Glu-Glu. Localized in the cytoplasm; Specificity unclear. | 0.483 |
| CAZ96781.1 | CAZ96780.1 | ZOBELLIA_2631 | ZOBELLIA_2630 | The 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 winged-helix DNA-binding domain) that acts as transcriptional regulator; 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. Localized in the cytoplasmic membrane; Specificity unclear. | 0.968 |
| CAZ96781.1 | CAZ96782.1 | ZOBELLIA_2631 | ZOBELLIA_2632 | The 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 winged-helix DNA-binding domain) that acts as transcriptional regulator; Family membership. | Amidohydrolase; This protein would catalyse the hydrolysis of amide or amine bonds in various substrates. It adopts a classical alpha-beta TIM-barrel fold. The active site is located in the mouth of the enzyme barrel and contains a bound iron ion that coordinates a hydroxyl nucleophile; Belongs to the Amidohydrolase family; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 24 and 25; Localized in the outer membrane; Specificity unclear. | 0.527 |
| CAZ96781.1 | CAZ96783.1 | ZOBELLIA_2631 | ZOBELLIA_2633 | The 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 winged-helix DNA-binding domain) that acts as transcriptional regulator; Family membership. | Family M28 contains aminopeptidases and carboxypeptidases with two co-catalytic zinc ions (I and II). Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The zinc ligands occur in the sequence in the order His (II), Asp (I and II), Glu (I), Asp or Glu (II) and His (I). In addition, two other residues, an Asp and a Glu, are believed to be important for catalysis. Four of these residues occur in the motifs His-Xaa-Asp and Glu-Glu. Localized in the cytoplasm; Specificity unclear. | 0.482 |
| CAZ96782.1 | CAZ96780.1 | ZOBELLIA_2632 | ZOBELLIA_2630 | Amidohydrolase; This protein would catalyse the hydrolysis of amide or amine bonds in various substrates. It adopts a classical alpha-beta TIM-barrel fold. The active site is located in the mouth of the enzyme barrel and contains a bound iron ion that coordinates a hydroxyl nucleophile; Belongs to the Amidohydrolase family; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 24 and 25; Localized in the outer membrane; Specificity unclear. | 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. Localized in the cytoplasmic membrane; Specificity unclear. | 0.527 |
| CAZ96782.1 | CAZ96781.1 | ZOBELLIA_2632 | ZOBELLIA_2631 | Amidohydrolase; This protein would catalyse the hydrolysis of amide or amine bonds in various substrates. It adopts a classical alpha-beta TIM-barrel fold. The active site is located in the mouth of the enzyme barrel and contains a bound iron ion that coordinates a hydroxyl nucleophile; Belongs to the Amidohydrolase family; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 24 and 25; Localized in the outer membrane; Specificity unclear. | The 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 winged-helix DNA-binding domain) that acts as transcriptional regulator; Family membership. | 0.527 |
| CAZ96782.1 | CAZ96783.1 | ZOBELLIA_2632 | ZOBELLIA_2633 | Amidohydrolase; This protein would catalyse the hydrolysis of amide or amine bonds in various substrates. It adopts a classical alpha-beta TIM-barrel fold. The active site is located in the mouth of the enzyme barrel and contains a bound iron ion that coordinates a hydroxyl nucleophile; Belongs to the Amidohydrolase family; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 24 and 25; Localized in the outer membrane; Specificity unclear. | Family M28 contains aminopeptidases and carboxypeptidases with two co-catalytic zinc ions (I and II). Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The zinc ligands occur in the sequence in the order His (II), Asp (I and II), Glu (I), Asp or Glu (II) and His (I). In addition, two other residues, an Asp and a Glu, are believed to be important for catalysis. Four of these residues occur in the motifs His-Xaa-Asp and Glu-Glu. Localized in the cytoplasm; Specificity unclear. | 0.798 |
| CAZ96783.1 | CAZ94322.1 | ZOBELLIA_2633 | ZOBELLIA_249 | Family M28 contains aminopeptidases and carboxypeptidases with two co-catalytic zinc ions (I and II). Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The zinc ligands occur in the sequence in the order His (II), Asp (I and II), Glu (I), Asp or Glu (II) and His (I). In addition, two other residues, an Asp and a Glu, are believed to be important for catalysis. Four of these residues occur in the motifs His-Xaa-Asp and Glu-Glu. Localized in the cytoplasm; Specificity unclear. | Conserved hypothetical protein; Possibly localized in the cytoplasm. | 0.415 |
| CAZ96783.1 | CAZ94793.1 | ZOBELLIA_2633 | ZOBELLIA_727 | Family M28 contains aminopeptidases and carboxypeptidases with two co-catalytic zinc ions (I and II). Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The zinc ligands occur in the sequence in the order His (II), Asp (I and II), Glu (I), Asp or Glu (II) and His (I). In addition, two other residues, an Asp and a Glu, are believed to be important for catalysis. Four of these residues occur in the motifs His-Xaa-Asp and Glu-Glu. Localized in the cytoplasm; Specificity unclear. | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Features a signal p [...] | 0.425 |
| CAZ96783.1 | CAZ95352.1 | ZOBELLIA_2633 | ZOBELLIA_1296 | Family M28 contains aminopeptidases and carboxypeptidases with two co-catalytic zinc ions (I and II). Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The zinc ligands occur in the sequence in the order His (II), Asp (I and II), Glu (I), Asp or Glu (II) and His (I). In addition, two other residues, an Asp and a Glu, are believed to be important for catalysis. Four of these residues occur in the motifs His-Xaa-Asp and Glu-Glu. Localized in the cytoplasm; Specificity unclear. | Conserved hypothetical lipoprotein; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 26 and 27; Localized in the outer membrane; Conserved hypothetical protein. | 0.420 |
| CAZ96783.1 | CAZ95578.1 | ZOBELLIA_2633 | ZOBELLIA_1522 | Family M28 contains aminopeptidases and carboxypeptidases with two co-catalytic zinc ions (I and II). Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The zinc ligands occur in the sequence in the order His (II), Asp (I and II), Glu (I), Asp or Glu (II) and His (I). In addition, two other residues, an Asp and a Glu, are believed to be important for catalysis. Four of these residues occur in the motifs His-Xaa-Asp and Glu-Glu. Localized in the cytoplasm; Specificity unclear. | Prolyl oligopeptidase, family S9; Prolyl oligopeptidase cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long. Has an absolute requirement for an X-Pro bond in the trans configuration immediately preceding the Pro-Y scissible bond; Belongs to the family S9 of the peptidases; Contains a putative lipoprotein signal peptide cleaved between the residues 16 and 17; Possibly localized in the outer membrane; High confidence in function and specificity. | 0.424 |
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