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
AGA25661.1Beta-propeller domain-containing protein, methanol dehydrogenase; PFAM: Domain of unknown function (DUF477). (233 aa)    
Predicted Functional Partners:
AGA30753.1
Cytochrome b subunit of the bc complex; PFAM: Cytochrome c; Cytochrome b(C-terminal)/b6/petD.
    
   0.875
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.
  
 
   0.805
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.
  
 
   0.799
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).
  
 
   0.795
AGA27906.1
PFAM: Cytochrome c; Cytochrome C oxidase subunit II, periplasmic domain; TIGRFAM: cytochrome c oxidase, subunit II.
    
   0.761
AGA30949.1
Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III.
  
 
   0.727
AGA26194.1
Rieske Fe-S protein; PFAM: Rieske [2Fe-2S] domain.
  
   0.680
AGA30752.1
Rieske Fe-S protein; PFAM: Rieske [2Fe-2S] domain.
  
   0.680
AGA27904.1
Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III.
    
   0.667
AGA26195.1
Cytochrome b subunit of the bc complex; PFAM: Cytochrome b(N-terminal)/b6/petB.
    
   0.646
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
Server load: medium (44%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.