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
GU90_10905Cytochrome 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). (304 aa)    
Predicted Functional Partners:
GU90_10910
Cytochrome C oxidase subunit IV; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family.
 
 
 0.999
GU90_10935
Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
GU90_10945
Menaquinol-cytochrome C reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.999
GU90_10950
Menaquinol-cytochrome C reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
GU90_12315
Cytochrome C oxidase subunit 1; 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.
 
 0.999
GU90_12500
Menaquinol-cytochrome C reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
GU90_17575
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
   0.996
GU90_05665
NADH:ubiquinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.990
nuoH
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.
  
 
 0.989
ctaB
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.
 
 
 0.979
Your Current Organism:
Saccharopolyspora rectivirgula
NCBI taxonomy Id: 28042
Other names: ATCC 33515, DSM 43747, Faenia rectivirgula, IFO 12464, INMI 683, JCM 3057, Micropolyspora faeni, Micropolyspora rectivirgula, NBRC 12464, NRRL B-16280, S. rectivirgula, Thermopolyspora polyspora, Thermopolyspora rectivirgula, VKM Ac-810
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