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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
KRV48433.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (389 aa)    
Predicted Functional Partners:
KRV49899.1
Cystathionine beta-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
KRV49900.1
Ubiquinol-cytochrome C reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
KRV49898.1
Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.997
KRV49904.1
Cytochrome C oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.995
KRV49903.1
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.
 
 0.993
KRV49902.1
Cytochrome C oxidase subunit IV; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family.
 
 
 0.981
KRV50518.1
[Fe-S]-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.973
KRV50837.1
NADH:ubiquinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.891
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.
   
 
 0.891
KRV50814.1
NADH-quinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.891
Your Current Organism:
Streptomyces vitaminophilus
NCBI taxonomy Id: 76728
Other names: ATCC 31673, Actinosporangium vitaminiphilum, Actinosporangium vitaminophilum, DSM 41686, IFO 14294, JCM 6054, NBRC 14294, NRRL B-16933, S. vitaminophilus, Streptomyces vitaminiphilus, Streptomyces vitaminophileus, strain SF 2080
Server load: low (26%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.