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 |
| CAZ95731.1 | CAZ95732.1 | ZOBELLIA_1677 | ZOBELLIA_1678 | Metal-dependent hydrolase; Conserved protein belonging to the metallo beta-lactamase superfamily. The histidine residues which coordinate the zinc ions are strictly conserved in this protein, suggesting that it is a metal-dependent hydrolase. But its exact function is still unknown; Localized in the cytoplasm; Function unclear. | Serine endopeptidase, family S8; The Serine endopeptidases use a catalytic serine residue as a nucleophile and form an acyl intermediate. These peptidases can also readily act as transferases; Belongs to the families S8 of peptidases, clan SB; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 20 and 21; Localized in the cytoplasmic and/or outer membrane; Family membership. | 0.449 |
| CAZ95731.1 | CAZ95733.1 | ZOBELLIA_1677 | ZOBELLIA_1679 | Metal-dependent hydrolase; Conserved protein belonging to the metallo beta-lactamase superfamily. The histidine residues which coordinate the zinc ions are strictly conserved in this protein, suggesting that it is a metal-dependent hydrolase. But its exact function is still unknown; Localized in the cytoplasm; Function 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 [...] | 0.516 |
| CAZ95731.1 | rnpA | ZOBELLIA_1677 | ZOBELLIA_1680 | Metal-dependent hydrolase; Conserved protein belonging to the metallo beta-lactamase superfamily. The histidine residues which coordinate the zinc ions are strictly conserved in this protein, suggesting that it is a metal-dependent hydrolase. But its exact function is still unknown; Localized in the cytoplasm; Function unclear. | Ribonuclease P protein component; RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. | 0.441 |
| CAZ95732.1 | CAZ95731.1 | ZOBELLIA_1678 | ZOBELLIA_1677 | Serine endopeptidase, family S8; The Serine endopeptidases use a catalytic serine residue as a nucleophile and form an acyl intermediate. These peptidases can also readily act as transferases; Belongs to the families S8 of peptidases, clan SB; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 20 and 21; Localized in the cytoplasmic and/or outer membrane; Family membership. | Metal-dependent hydrolase; Conserved protein belonging to the metallo beta-lactamase superfamily. The histidine residues which coordinate the zinc ions are strictly conserved in this protein, suggesting that it is a metal-dependent hydrolase. But its exact function is still unknown; Localized in the cytoplasm; Function unclear. | 0.449 |
| CAZ95732.1 | CAZ95733.1 | ZOBELLIA_1678 | ZOBELLIA_1679 | Serine endopeptidase, family S8; The Serine endopeptidases use a catalytic serine residue as a nucleophile and form an acyl intermediate. These peptidases can also readily act as transferases; Belongs to the families S8 of peptidases, clan SB; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 20 and 21; Localized in the cytoplasmic and/or outer membrane; Family membership. | 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 [...] | 0.854 |
| CAZ95732.1 | CAZ95735.1 | ZOBELLIA_1678 | ZOBELLIA_1681 | Serine endopeptidase, family S8; The Serine endopeptidases use a catalytic serine residue as a nucleophile and form an acyl intermediate. These peptidases can also readily act as transferases; Belongs to the families S8 of peptidases, clan SB; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 20 and 21; Localized in the cytoplasmic and/or outer membrane; Family membership. | Carboxy-terminal processing peptidase, family S41; This enzyme is a modular protein with a N-terminal PDZ domain, a central carboxy-terminal processing peptidase and a C-terminal domain of unknown function. The catalytic module belongs to the family S41 of the peptidase. It shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C- terminus. PDZ domains are multifunctional protein-protein interaction modules. In many cases, PDZ dom [...] | 0.458 |
| CAZ95732.1 | CAZ95736.1 | ZOBELLIA_1678 | ZOBELLIA_1682 | Serine endopeptidase, family S8; The Serine endopeptidases use a catalytic serine residue as a nucleophile and form an acyl intermediate. These peptidases can also readily act as transferases; Belongs to the families S8 of peptidases, clan SB; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 20 and 21; Localized in the cytoplasmic and/or outer membrane; Family membership. | Glyoxalase superfamily protein; Family membership. | 0.404 |
| CAZ95732.1 | CAZ97882.1 | ZOBELLIA_1678 | ZOBELLIA_3744 | Serine endopeptidase, family S8; The Serine endopeptidases use a catalytic serine residue as a nucleophile and form an acyl intermediate. These peptidases can also readily act as transferases; Belongs to the families S8 of peptidases, clan SB; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 20 and 21; Localized in the cytoplasmic and/or outer membrane; Family membership. | Possible ABC importer, ATPase component; Conserved hypothetical protein that could be an ATP-binding protein; Localized in the cytoplasm; Conserved hypothetical protein. | 0.432 |
| CAZ95732.1 | ftsK | ZOBELLIA_1678 | ZOBELLIA_4615 | Serine endopeptidase, family S8; The Serine endopeptidases use a catalytic serine residue as a nucleophile and form an acyl intermediate. These peptidases can also readily act as transferases; Belongs to the families S8 of peptidases, clan SB; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 20 and 21; Localized in the cytoplasmic and/or outer membrane; Family membership. | FtsK is a DNA motor protein, which is both required to move DNA out of the region of the septum during cell division and for the septum formation. Tracks DNA in an ATP-dependent manner by generating positive supercoils in front of it and negative supercoils behind it. It forms a hexamer. Features four transmembrane helices. Localized in the cytoplasmic membrane; High confidence in function and specificity. | 0.424 |
| CAZ95732.1 | pmr1 | ZOBELLIA_1678 | ZOBELLIA_3488 | Serine endopeptidase, family S8; The Serine endopeptidases use a catalytic serine residue as a nucleophile and form an acyl intermediate. These peptidases can also readily act as transferases; Belongs to the families S8 of peptidases, clan SB; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 20 and 21; Localized in the cytoplasmic and/or outer membrane; Family membership. | Pmr1 is Aa P-type ATPase responsible for calcium efflux using ATP hydrolysis for energy. Pmr1 controls calcium homeostasis. Belongs to the cation transport P-type ATPase family. Features nine transmembrane helices. Localized in the cytoplasmic membrane; High confidence in function and specificity. | 0.421 |
| CAZ95732.1 | rnpA | ZOBELLIA_1678 | ZOBELLIA_1680 | Serine endopeptidase, family S8; The Serine endopeptidases use a catalytic serine residue as a nucleophile and form an acyl intermediate. These peptidases can also readily act as transferases; Belongs to the families S8 of peptidases, clan SB; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 20 and 21; Localized in the cytoplasmic and/or outer membrane; Family membership. | Ribonuclease P protein component; RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. | 0.564 |
| CAZ95733.1 | CAZ95731.1 | ZOBELLIA_1679 | ZOBELLIA_1677 | 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 [...] | Metal-dependent hydrolase; Conserved protein belonging to the metallo beta-lactamase superfamily. The histidine residues which coordinate the zinc ions are strictly conserved in this protein, suggesting that it is a metal-dependent hydrolase. But its exact function is still unknown; Localized in the cytoplasm; Function unclear. | 0.516 |
| CAZ95733.1 | CAZ95732.1 | ZOBELLIA_1679 | ZOBELLIA_1678 | 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 [...] | Serine endopeptidase, family S8; The Serine endopeptidases use a catalytic serine residue as a nucleophile and form an acyl intermediate. These peptidases can also readily act as transferases; Belongs to the families S8 of peptidases, clan SB; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 20 and 21; Localized in the cytoplasmic and/or outer membrane; Family membership. | 0.854 |
| CAZ95733.1 | CAZ95735.1 | ZOBELLIA_1679 | ZOBELLIA_1681 | 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 [...] | Carboxy-terminal processing peptidase, family S41; This enzyme is a modular protein with a N-terminal PDZ domain, a central carboxy-terminal processing peptidase and a C-terminal domain of unknown function. The catalytic module belongs to the family S41 of the peptidase. It shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C- terminus. PDZ domains are multifunctional protein-protein interaction modules. In many cases, PDZ dom [...] | 0.484 |
| CAZ95733.1 | CAZ95736.1 | ZOBELLIA_1679 | ZOBELLIA_1682 | 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 [...] | Glyoxalase superfamily protein; Family membership. | 0.417 |
| CAZ95733.1 | rnpA | ZOBELLIA_1679 | ZOBELLIA_1680 | 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 [...] | Ribonuclease P protein component; RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. | 0.599 |
| CAZ95735.1 | CAZ95732.1 | ZOBELLIA_1681 | ZOBELLIA_1678 | Carboxy-terminal processing peptidase, family S41; This enzyme is a modular protein with a N-terminal PDZ domain, a central carboxy-terminal processing peptidase and a C-terminal domain of unknown function. The catalytic module belongs to the family S41 of the peptidase. It shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C- terminus. PDZ domains are multifunctional protein-protein interaction modules. In many cases, PDZ dom [...] | Serine endopeptidase, family S8; The Serine endopeptidases use a catalytic serine residue as a nucleophile and form an acyl intermediate. These peptidases can also readily act as transferases; Belongs to the families S8 of peptidases, clan SB; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 20 and 21; Localized in the cytoplasmic and/or outer membrane; Family membership. | 0.458 |
| CAZ95735.1 | CAZ95733.1 | ZOBELLIA_1681 | ZOBELLIA_1679 | Carboxy-terminal processing peptidase, family S41; This enzyme is a modular protein with a N-terminal PDZ domain, a central carboxy-terminal processing peptidase and a C-terminal domain of unknown function. The catalytic module belongs to the family S41 of the peptidase. It shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C- terminus. PDZ domains are multifunctional protein-protein interaction modules. In many cases, PDZ dom [...] | 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 [...] | 0.484 |
| CAZ95735.1 | CAZ95736.1 | ZOBELLIA_1681 | ZOBELLIA_1682 | Carboxy-terminal processing peptidase, family S41; This enzyme is a modular protein with a N-terminal PDZ domain, a central carboxy-terminal processing peptidase and a C-terminal domain of unknown function. The catalytic module belongs to the family S41 of the peptidase. It shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C- terminus. PDZ domains are multifunctional protein-protein interaction modules. In many cases, PDZ dom [...] | Glyoxalase superfamily protein; Family membership. | 0.701 |
| CAZ95735.1 | rnpA | ZOBELLIA_1681 | ZOBELLIA_1680 | Carboxy-terminal processing peptidase, family S41; This enzyme is a modular protein with a N-terminal PDZ domain, a central carboxy-terminal processing peptidase and a C-terminal domain of unknown function. The catalytic module belongs to the family S41 of the peptidase. It shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C- terminus. PDZ domains are multifunctional protein-protein interaction modules. In many cases, PDZ dom [...] | Ribonuclease P protein component; RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. | 0.672 |
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