STRINGSTRING
AGE27338.1 AGE27338.1 cyoD cyoD cyoB cyoB cyoA cyoA cyoE cyoE AGE25885.1 AGE25885.1 AGE25886.1 AGE25886.1 nuoC nuoC AGE25888.1 AGE25888.1 nuoH nuoH AGE26332.1 AGE26332.1
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.
Node Color
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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
AGE27338.1COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3. (207 aa)    
Predicted Functional Partners:
cyoD
COG3125 Heme/copper-type cytochrome/quinol oxidase, subunit 4.
 
 0.999
cyoB
COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1; Belongs to the heme-copper respiratory oxidase family.
 0.999
cyoA
COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2.
 
 0.999
cyoE
Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
 
  
 0.985
AGE25885.1
COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2.
 
 0.981
AGE25886.1
COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1.
 0.981
nuoC
Bifunctional NADH:ubiquinone oxidoreductase subunit C/D; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the C-terminal section; belongs to the complex I 49 kDa subunit family.
   
 0.973
AGE25888.1
COG3125 Heme/copper-type cytochrome/quinol oxidase, subunit 4.
 
 
 0.967
nuoH
NADH:ubiquinone oxidoreductase subunit H; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone.
   
 0.940
AGE26332.1
COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M).
   
 0.940
Your Current Organism:
Pseudomonas poae
NCBI taxonomy Id: 1282356
Other names: P. poae RE*1-1-14, Pseudomonas poae RE*1-1-14
Server load: low (30%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.