STRINGSTRING
rtcB protein (Methanococcus voltae) - STRING interaction network
"rtcB" - Hypothetical protein in Methanococcus voltae
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
rtcBHypothetical protein (480 aa)    
Predicted Functional Partners:
Mvol_0779
Hypothetical protein (156 aa)
 
  0.902
Mvol_1473
Purine or other phosphorylase family 1 (253 aa)
         
  0.807
Mvol_1664
Adenylosuccinate lyase (448 aa)
   
   
  0.743
map
Methionine aminopeptidase, type II; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val) (297 aa)
   
   
  0.727
dys
Deoxyhypusine synthase; Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue (340 aa)
   
   
  0.716
Mvol_1495
DEAD/DEAH box helicase domain-containing protein (584 aa)
   
  0.639
Mvol_0962
Nuclease (229 aa)
              0.573
cheB
Response regulator receiver modulated CheB methylesterase; Involved in the modulation of the chemotaxis system; catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR (382 aa)
         
  0.553
Mvol_0903
APHP domain-containing protein (1087 aa)
           
  0.527
secY
Preprotein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently (446 aa)
         
  0.524
Your Current Organism:
Methanococcus voltae
NCBI taxonomy Id: 456320
Other names: M. voltae, M. voltae A3, Methanococcus voltae, Methanococcus voltae A3, Methanococcus voltae str. A3, Methanococcus voltae strain A3, Methanococcus voltaei
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