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
STH3147Putative menaquinol-cytochrome C reductase. (253 aa)    
Predicted Functional Partners:
STH3146
Plastoquinol--plastocyanin reductase.
 
 0.999
STH3148
Menaquinol-cytochrome C reductase.
  
 0.998
STH2096
Cytochrome c oxidase subunit II; 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).
  
 0.996
STH3144
Hypothetical protein.
  
 
 0.990
STH2098
Cytochrome C oxidase subunit III.
 
 
 0.985
STH2097
Cytochrome C oxidase subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.
 
 
 0.984
nuoM2
NADH dehydrogenase I subunit M.
  
 
 0.982
nuoH1
NADH dehydrogenase I 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.
   
 
 0.964
nuoH2
NADH dehydrogenase I 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.
   
 
 0.964
STH929
Conserved hypothetical protein.
  
 
 0.953
Your Current Organism:
Symbiobacterium thermophilum
NCBI taxonomy Id: 292459
Other names: S. thermophilum IAM 14863, Symbiobacterium thermophilum IAM 14863, Symbiobacterium thermophilum str. IAM 14863, Symbiobacterium thermophilum strain IAM 14863
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.