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
AGA26195.1Cytochrome b subunit of the bc complex; PFAM: Cytochrome b(N-terminal)/b6/petB. (261 aa)    
Predicted Functional Partners:
nuoB-2
NADH-quinone oxidoreductase, B subunit; 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 49 kDa subunit family.
   
 
 0.999
AGA26194.1
Rieske Fe-S protein; PFAM: Rieske [2Fe-2S] domain.
 
 0.998
AGA30752.1
Rieske Fe-S protein; PFAM: Rieske [2Fe-2S] domain.
 
 0.996
AGA29915.1
Cytochrome c1; PFAM: PA14 domain.
 
 0.993
AGA27906.1
PFAM: Cytochrome c; Cytochrome C oxidase subunit II, periplasmic domain; TIGRFAM: cytochrome c oxidase, subunit II.
  
 0.980
AGA30946.1
Heme/copper-type cytochrome/quinol oxidase, subunit 1; PFAM: Cytochrome C and Quinol oxidase polypeptide I; TIGRFAM: cytochrome c oxidase, subunit I; Belongs to the heme-copper respiratory oxidase family.
 
 
 0.977
AGA30949.1
Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III.
 
 
 0.976
AGA30945.1
Heme/copper-type cytochrome/quinol oxidases, 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).
 
 
 0.975
AGA27905.1
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.
 
 
 0.968
AGA27904.1
Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III.
 
 
 0.967
Your Current Organism:
Singulisphaera acidiphila
NCBI taxonomy Id: 886293
Other names: S. acidiphila DSM 18658, Singulisphaera acidiphila DSM 18658, Singulisphaera acidiphila MOB10, Singulisphaera acidiphila str. DSM 18658, Singulisphaera acidiphila strain DSM 18658
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