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
Node Content
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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Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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dnaJChaperone 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 [...] (364 aa)    
Predicted Functional Partners:
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 0.997
htpG
Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity.
  
 0.996
grpE
GrpE 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. Several rounds of ATP-dependent i [...]
 
 
 0.991
hscA
Fe-S protein assembly chaperone HscA; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB.
 0.990
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 0.970
Rmag_1033
Hypothetical protein.
    
 0.930
lon
ATP-dependent proteinase, Serine peptidase, MEROPS family S16; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
  
 
 0.929
Rmag_0310
PFAM: peptidylprolyl isomerase, FKBP-type; peptidyl-prolyl cis-trans isomerase, cyclophilin type; KEGG: tde:TDE2391 peptidyl-prolyl cis-trans isomerase.
   
 
 0.897
groS
Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.837
Rmag_0686
PFAM: protein kinase; protein phosphatase 2C domain protein; SMART: tyrosine protein kinase; serine/threonine protein kinase; KEGG: hch:HCH_05817 serine/threonine protein kinase.
  
 
 0.836
Your Current Organism:
Ruthia magnifica
NCBI taxonomy Id: 413404
Other names: C. Ruthia magnifica str. Cm (Calyptogena magnifica), Candidatus Ruthia magnifica str. Cm (Calyptogena magnifica), Candidatus Ruthia magnifica strain Cm (Calyptogena magnifica), Ruthia magnifica str. Cm (Calyptogena magnifica)
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