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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
SFJ98307.1Ubiquinol-cytochrome c reductase cytochrome b subunit; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. (437 aa)    
Predicted Functional Partners:
SFJ04480.1
NADH dehydrogenase subunit M.
 
 
 0.999
SFJ98294.1
Ubiquinol-cytochrome c reductase cytochrome c1 subunit.
 0.999
SFJ98324.1
Ubiquinol-cytochrome c reductase iron-sulfur subunit; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
 0.999
nuoH
NADH dehydrogenase 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.
  
 
 0.998
SFI97207.1
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).
 
 0.998
SFI97329.1
Cytochrome c oxidase subunit 3.
 
 0.998
SFK00688.1
Cytochrome c oxidase subunit 1; Belongs to the heme-copper respiratory oxidase family.
 
 0.998
SFJ94523.1
Cytochrome c oxidase cbb3-type subunit 3; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex.
  
 0.994
SFJ24556.1
Cytochrome o ubiquinol oxidase subunit 1; Belongs to the heme-copper respiratory oxidase family.
 
 0.993
nuoN
NADH dehydrogenase 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 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; Belongs to the complex I subunit 2 family.
  
 
 0.992
Your Current Organism:
Celeribacter halophilus
NCBI taxonomy Id: 576117
Other names: C. halophilus, CGMCC 1.8891, Celeribacter halophilus (Wang et al. 2012) Lai et al. 2014, DSM 26270, Huaishuia halophila, Huaishuia halophila Wang et al. 2012, LMG 24854, LMG:24854, MCCC 1A06432, Pseudoruegeria sp. ZXM137, strain ZXM137
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