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.
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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
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[Homology]
Score
AIM00465.1Cytochrome C oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. (314 aa)    
Predicted Functional Partners:
ctaD-2
Cytochrome C oxidase; 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.
 0.999
AIM00467.1
Cytochrome C oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
AIM00468.1
Bb3-type cytochrome oxidase subunit IV; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
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.
 
 0.997
AIL98735.1
Cytochrome B562; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.995
AIM00469.1
Cytochrome C oxidase subunit IV; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.991
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.
 
 
 0.988
AIL99688.1
Cytochrome B; 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.
 
 
 0.956
nuoH
NADH:ubiquinone oxidoreductase subunit H; 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 ubiquinone. 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. This subunit may bind ubiquinone.
   
 0.925
coxB
Cytochrome B561; 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).
  
  
 
0.923
Your Current Organism:
Sinorhizobium meliloti
NCBI taxonomy Id: 382
Other names: ATCC 9930, CCUG 27879, CFBP 5561, DSM 30135, Ensifer meliloti, Ensifer sp. AC50a, Ensifer sp. AC50e, HAMBI 2148, IAM 12611, ICMP 12623, IFO 14782, JCM 20682, LMG 6133, LMG:6133, NBRC 14782, NCAIM B.01520, NRRL L-45, NZP 4027, Rhizobium meliloti, Rhizobium meliloti (megaplasmid pRME41B SYM), Rhizobium meliloti (plasmid pRmeGR4b), Rhizobium meliloti plasmid pRmeGR4b, Rhizobium sp. AC50e, S. meliloti
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