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
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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
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
AGA89007.1Thioredoxin domain-containing protein; PFAM: Thioredoxin; TIGRFAM: thioredoxin; Belongs to the thioredoxin family. (130 aa)    
Predicted Functional Partners:
AGA89846.1
Glutathione-disulfide reductase, animal/bacterial; PFAM: Pyridine nucleotide-disulphide oxidoreductase; Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain; TIGRFAM: glutathione-disulfide reductase, animal/bacterial.
   
 
 0.851
groL
Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 
 0.832
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. [...]
 
  
 0.824
hslV
ATP-dependent protease HslVU, peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
  
  
 0.801
AGA91180.1
PFAM: Pyridine nucleotide-disulphide oxidoreductase; TIGRFAM: thioredoxin-disulfide reductase.
 
 
 0.790
hslU
ATP-dependent protease HslVU, ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
   
   0.790
AGA90011.1
Ribonucleoside-diphosphate reductase, alpha subunit; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
  
 
 0.709
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 [...]
 
 
 0.688
AGA89050.1
Protein affecting phage T7 exclusion by the F plasmid; PFAM: FxsA cytoplasmic membrane protein.
   
    0.656
htpG
Molecular chaperone of HSP90 family; Molecular chaperone. Has ATPase activity.
   
 
 0.622
Your Current Organism:
Thioflavicoccus mobilis
NCBI taxonomy Id: 765912
Other names: T. mobilis 8321, Thioflavicoccus mobilis 8321, Thioflavicoccus mobilis ATCC 700959, Thioflavicoccus mobilis str. 8321, Thioflavicoccus mobilis strain 8321
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