STRINGSTRING
STRING protein interaction network
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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ACO46820.1Putative Cytochrome-c oxidase (Cytochrome-c oxidase polypeptide I+III, Complex IV); putative membrane protein; Belongs to the heme-copper respiratory oxidase family. (817 aa)    
Predicted Functional Partners:
nuoH
Putative NADH dehydrogenase (quinone), subunit H (NADH-quinone 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.
   
 
 0.999
ACO45357.1
Putative NADH dehydrogenase (quinone), subunit M (NADH-quinone oxidoreductase, subunit M).
  
 
 0.999
nuoN
Putative NADH dehydrogenase (quinone), subunit N (NADH-quinone oxidoreductase, subunit N); 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 a menaquinone. 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; Belongs to the complex I subunit 2 family.
   
 
 0.999
ACO45980.1
Putative FAD dependent oxidoreductase.
  
 
 0.999
ctaB
Putative protoheme IX farnesyltransferase (Heme O synthase); 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.
 
 0.999
ctaC
Putative cytochrome-c oxidase, subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
 
 0.999
ACO47087.1
Putative cytochrome b/b6; putative membrane protein.
 
 
 0.999
ACO47088.1
Putative Rieske 2Fe-2S protein.
 
 
 0.999
ACO45694.1
Putative arsenite oxidase (ArOx) small subunit containing a Rieske (2Fe-S) cluster.
  
 
 0.998
ACO45345.1
Putative NADH dehydrogenase (quinone), subunit A (NADH-quinone oxidoreductase, subunit A); NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain.
   
 
 0.994
Your Current Organism:
Deinococcus deserti
NCBI taxonomy Id: 546414
Other names: D. deserti VCD115, Deinococcus deserti VCD115, Deinococcus deserti str. VCD115, Deinococcus deserti strain VCD115
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