Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
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from curated databases
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experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
AGB15592.1Zn-dependent protease with chaperone function; PFAM: Peptidase family M48. (441 aa)    
Predicted Functional Partners:
grpE
Molecular chaperone GrpE (heat shock protein); Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. [...]
  
  
 0.692
dnaK
Chaperone protein DnaK; Acts as a chaperone.
  
 
 0.539
AGB16033.1
DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain.
 
 
 0.517
AGB17577.1
Putative low-complexity protein; PFAM: Pentapeptide repeats (8 copies); Ion channel.
     
 0.489
AGB15593.1
Putative nucleic acid-binding protein, contains PIN domain; PFAM: PIN domain.
       0.488
AGB15594.1
PFAM: SpoVT / AbrB like domain; TIGRFAM: looped-hinge helix DNA binding domain, AbrB family.
       0.488
AGB17507.1
K+ transport system, NAD-binding component; PFAM: TrkA-N domain; TrkA-C domain.
 
   
 0.459
AGB15950.1
DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain.
  
 
 0.448
AGB16309.1
DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain.
  
 
 0.448
dnaJ
Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...]
  
 
 0.448
Your Current Organism:
Halovivax ruber
NCBI taxonomy Id: 797302
Other names: H. ruber XH-70, Halovivax ruber JCM 13892, Halovivax ruber XH-70, Halovivax ruber str. XH-70, Halovivax ruber strain XH-70
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