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
cyoE-2Protoheme 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. (295 aa)    
Predicted Functional Partners:
cyoA
Cytochrome ubiquinol oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.981
cyoB
Cytochrome ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family.
 
 
 0.981
cyoD
Cytochrome o ubiquinol oxidase subunit IV; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.981
ARQ73505.1
Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.980
ctaD
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.
 
 
 0.910
ARQ72808.1
Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.899
coxB
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).
 
  
 0.847
ARQ72811.1
Cytochrome c oxidase subunit 3; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.831
ARQ73502.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.752
ARQ72812.1
Cytochrome c oxidase assembly protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.743
Your Current Organism:
Pseudomonas fragi
NCBI taxonomy Id: 296
Other names: ATCC 4973, Bacterium fragi, CCUG 556, CFBP 4556, CIP 55.4, DSM 3456, HAMBI 28, IFO 3458, LMG 2191, LMG:2191, NBRC 3458, NCCB 69033, NCIB 8542, NCIB:8542, NCTC 10689, NRRL B-25, NRRL B-727, NRRL:B:25, P. fragi, Pseudomonas fragariae, VKM B-898, VKM:B:898
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