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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
ORB42523.1Cytochrome C oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. (201 aa)    
Predicted Functional Partners:
ORB33686.1
Cytochrome C oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.998
ORB43523.1
Cytochrome ubiquinol 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.
 
 0.996
ORB40178.1
Cytochrome ubiquinol 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.
 
 0.996
ORB38674.1
Menaquinol-cytochrome C reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.996
ORB38675.1
Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.995
ORB38716.1
Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.993
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.
 
 
 0.985
ORB40151.1
NADH-quinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.976
nuoA
NADH-quinone oxidoreductase subunit A; 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 a menaquinone. 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 subunit 3 family.
   
 0.974
ORB33685.1
Cytochrome C oxidase subunit IV; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family.
  
 0.974
Your Current Organism:
Mycolicibacterium porcinum
NCBI taxonomy Id: 39693
Other names: ATCC 33776, CCUG 37674, CIP 105392, DSM 44242, JCM 6378, M. porcinum, Mycobacterium porcinum, strain E10241-1
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