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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
AEB86224.1KEGG: app:CAP2UW1_3424 putative cytochrome c oxidase, subunit I. (482 aa)    
Predicted Functional Partners:
AEB86230.1
PFAM: Cytochrome c oxidase subunit II C-terminal; KEGG: app:CAP2UW1_1791 cytochrome c oxidase subunit II.
 
 0.998
AEB86226.1
PFAM: Methyl-viologen-reducing hydrogenase, delta subunit; 4Fe-4S binding domain; KEGG: app:CAP2UW1_1327 methyl-viologen-reducing hydrogenase delta subunit.
 
 
 0.989
AEB86229.1
Cytochrome-c oxidase; KEGG: app:CAP2UW1_1790 cytochrome c oxidase subunit I; PFAM: Cytochrome c oxidase, subunit I.
 
  
 
0.975
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).
 
 0.975
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.
  
 
 0.966
AEB84617.1
KEGG: ajs:Ajs_2775 ubiquinol oxidase, subunit II; TIGRFAM: Cytochrome o ubiquinol oxidase subunit II; PFAM: COX aromatic rich; Cytochrome c oxidase subunit II C-terminal.
  
 0.949
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.
 
 
 0.949
AEB84614.1
KEGG: ajs:Ajs_2778 cytochrome c oxidase subunit IV; TIGRFAM: Cytochrome o ubiquinol oxidase subunit IV; PFAM: Cytochrome C oxidase subunit IV prokaryotic.
  
 
 0.931
AEB86227.1
PFAM: Copper chaperone SCO1/SenC; KEGG: app:CAP2UW1_1788 electron transport protein SCO1/SenC.
 
  
 0.931
AEB86278.1
PFAM: Cytochrome c oxidase, subunit III; KEGG: dia:Dtpsy_2855 cytochrome c oxidase subunit III.
 
 0.931
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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