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
AEB86145.1PFAM: Cytochrome c, class I; KEGG: dia:Dtpsy_2961 cytochrome c class I. (137 aa)    
Predicted Functional Partners:
AEB83272.1
Ubiquinol-cytochrome c reductase, iron-sulfur subunit; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
 
 0.976
AEB83274.1
Cytochrome c1; KEGG: ajs:Ajs_0791 cytochrome c1; manually curated; PFAM: Cytochrome c1.
  
 0.960
AEB86629.1
KEGG: azc:AZC_0960 cytochrome c; manually curated; PFAM: Cytochrome c, class I.
  
  
 
0.924
AEB86273.1
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).
   
 0.915
AEB83510.1
PFAM: Cytochrome c, class I; KEGG: dia:Dtpsy_0985 cytochrome c class I.
    
 0.913
AEB86144.1
KEGG: ajs:Ajs_3652 hypothetical protein.
 
    0.877
AEB86223.1
KEGG: app:CAP2UW1_1324 oxidoreductase FAD-binding domain protein; PFAM: Oxidoreductase, FAD-binding domain; Ferredoxin; Cytochrome b/b6, N-terminal; Oxidoreductase FAD/NAD(P)-binding.
  
 0.860
AEB83460.1
PFAM: 4Fe-4S binding domain; KEGG: dia:Dtpsy_2790 4Fe-4S ferredoxin iron-sulfur binding domain protein.
  
 
 0.831
AEB86226.1
PFAM: Methyl-viologen-reducing hydrogenase, delta subunit; 4Fe-4S binding domain; KEGG: app:CAP2UW1_1327 methyl-viologen-reducing hydrogenase delta subunit.
  
 0.808
AEB83452.1
KEGG: dia:Dtpsy_2798 respiratory-chain NADH dehydrogenase domain 51 kDa subunit; PFAM: NADH:ubiquinone oxidoreductase, 51kDa subunit; NADH:ubiquinone oxidoreductase, 24kDa subunit; Soluble ligand binding domain; NADH ubiquinone oxidoreductase, F subunit, iron sulphur binding; SMART: NADH ubiquinone oxidoreductase, F subunit, iron sulphur binding.
   
 
 0.805
Your Current Organism:
Alicycliphilus denitrificans
NCBI taxonomy Id: 596154
Other names: A. denitrificans K601, Alicycliphilus denitrificans DSM 14773, Alicycliphilus denitrificans K601, Alicycliphilus denitrificans str. K601, Alicycliphilus denitrificans strain K601, Pseudomonas sp. K601, beta proteobacterium K601
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