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IL0188 protein (Idiomarina loihiensis) - STRING interaction network
"IL0188" - Anaerobic ribonucleoside triphosphate reductase in Idiomarina loihiensis
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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
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textmining
co-expression
protein homology
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Score
IL0188Anaerobic ribonucleoside triphosphate reductase (612 aa)    
Predicted Functional Partners:
IL0187
Radical enzyme activating protein (157 aa)
 
          0.973
dut
Deoxyuridine 5’-triphosphate nucleotidohydrolase; This enzyme is involved in nucleotide metabolism- it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA (151 aa)
       
  0.967
dcd
Deoxycytidine triphosphate deaminase (195 aa)
       
    0.955
mazG
Pyrophosphatase MazG (257 aa)
       
    0.955
atpB
ATP synthase F0F1 subunit A; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane (265 aa)
         
    0.954
atpE
ATP synthase F0F1 subunit C; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (85 aa)
         
    0.954
atpF
ATP synthase F0F1 subunit B; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (156 aa)
         
    0.954
atpH
ATP synthase F0F1 subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (177 aa)
         
    0.954
atpA
ATP synthase F0F1 subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit (513 aa)
         
    0.954
atpG
ATP synthase F0F1 subunit gamma; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex (287 aa)
         
    0.954
Your Current Organism:
Idiomarina loihiensis
NCBI taxonomy Id: 283942
Other names: I. loihiensis, I. loihiensis L2TR, Idiomarina loihiensis, Idiomarina loihiensis Donachie et al. 2003, Idiomarina loihiensis L2TR, Idiomarina loihiensis str. L2TR, Idiomarina loihiensis strain L2TR
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