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TON_1776 protein (Thermococcus onnurineus) - STRING interaction network
"TON_1776" - Permease in Thermococcus onnurineus
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second shell of interactors
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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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Score
TON_1776Permease (283 aa)    
Predicted Functional Partners:
priL
DNA primase large subunit; Regulatory subunit of DNA primase, an RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Stabilizes and modulates the activity of the small subunit, increasing the rate of DNA synthesis, and conferring RNA synthesis capability. The DNA polymerase activity may enable DNA primase to also catalyze primer extension after primer synthesis. May also play a role in DNA repair (401 aa)
   
        0.865
priS
DNA primase small subunit; Catalytic subunit of DNA primase, an RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. The small subunit contains the primase catalytic core and has DNA synthesis activity on its own. Binding to the large subunit stabilizes and modulates the activity, increasing the rate of DNA synthesis while decreasing the length of the DNA fragments, and conferring RNA synthesis capability. The DNA polymerase activity may enable DNA primase to also catalyze primer extension after primer synthesis. [...] (346 aa)
   
   
  0.864
carS
Hypothetical protein; Catalyzes the formation of CDP-2,3-bis-(O- geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O- geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids (170 aa)
   
 
  0.801
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 (481 aa)
     
 
  0.582
truA
tRNA pseudouridine synthase A; Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs (267 aa)
   
        0.533
tgtA
7-cyano-7-deazaguanine tRNA-ribosyltransferase; Exchanges the guanine residue with 7-cyano-7- deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D- loop) of archaeal tRNAs (580 aa)
   
        0.515
TON_1503
Hypothetical protein (280 aa)
              0.480
TON_0383
Endopeptidase IV (335 aa)
              0.480
Your Current Organism:
Thermococcus onnurineus
NCBI taxonomy Id: 523850
Other names: T. onnurineus, T. onnurineus NA1, Thermococcus onnurineus, Thermococcus onnurineus NA1, Thermococcus onnurineus str. NA1, Thermococcus onnurineus strain NA1, Thermococcus sp. NA1
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