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
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
thsThermosome (ths); Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity; Belongs to the TCP-1 chaperonin family. (542 aa)    
Predicted Functional Partners:
MJ_1417
ATP-dependent protease LA, putative (lon); ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Degrades polypeptides processively (By similarity).
  
 0.970
mdh
L-lactate dehydrogenase EGAD|7256|705; Catalyzes the reversible oxidation of (S)-malate and (S)- sulfolactate to oxaloacetate and sulfopyruvate, respectively. Can use both NADH and NADPH, although activity is higher with NADPH. Oxidation of (S)-sulfolactate is observed only in the presence of NADP(+). Can also oxidize tartrate. Cannot reduce pyruvate, nor alpha-ketoglutarate. Belongs to the LDH/MDH superfamily.
  
 0.951
rps2
SSU ribosomal protein S2P; Similar to GP:1707827 percent identity: 54.69; identified by sequence similarity; putative; Belongs to the universal ribosomal protein uS2 family.
 
 0.921
pfdB
erpK protein isolog; Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding (By similarity).
  
 0.917
fusA
Translation elongation factor EF-2; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity); Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase [...]
 
 
 0.896
MJ_1411
Glyceraldehyde-3-phosphate dehydrogenase, NADP-dependent (gapN); Involved in F420 biosynthesis through the oxidation of lactaldehyde to lactate. The substrate preference order is propionaldehyde > DL-lactaldehyde, DL-glyceraldehyde > crotonaldehyde > glycolaldehyde > acetaldehyde, acrolein > formaldehyde. No activity was observed towards methylglyoxal or glyceraldehyde-3-phosphate. Has a preference for NAD over NADP.
  
 0.888
MJ_0285
Small heat shock protein (hsp20); Chaperone that confers thermal protection to other proteins; Belongs to the small heat shock protein (HSP20) family.
  
  
 0.842
tbp
Transcription initiation factor IID, TATA-box binding protein; General factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Binds specifically to the TATA box promoter element which lies close to the position of transcription initiation (By similarity).
 
 
 0.842
rps3
SSU ribosomal protein S3P (rpsC); Binds the lower part of the 30S subunit head. Belongs to the universal ribosomal protein uS3 family.
 
 0.833
infB
Translation initiation factor aIF-2 (infB); Function in general translation initiation by promoting the binding of the formylmethionine-tRNA to ribosomes. Seems to function along with eIF-2 (By similarity).
 
 
 0.820
Your Current Organism:
Methanocaldococcus jannaschii
NCBI taxonomy Id: 243232
Other names: M. jannaschii DSM 2661, Methanocaldococcus jannaschii DSM 2661, Methanocaldococcus jannaschii str. DSM 2661, Methanococcus jannaschii DSM 2661
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