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
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
OHY96852.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (1355 aa)    
Predicted Functional Partners:
nuoC
NADH-quinone oxidoreductase subunit C/D; 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; In the C-terminal section; belongs to the complex I 49 kDa subunit family.
   
   0.868
OHY95080.1
NADH-quinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 
 0.735
nuoH
NADH-quinone 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.
    
   0.693
OHY96973.1
Peptidase S8; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S8 family.
   
 0.692
OHY92056.1
Peptidase S8; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.692
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 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; Belongs to the complex I subunit 3 family.
    
   0.687
OHY88570.1
Peptidase M16; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
   0.684
OHY93136.1
Peptidylprolyl isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family.
    
  0.654
OHY93552.1
Peptidylprolyl isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family.
    
  0.654
OHY91881.1
Sulfate permease; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
   0.628
Your Current Organism:
Aeromonas sobria
NCBI taxonomy Id: 646
Other names: A. sobria, ATCC 43979, Aeromonas hybridization group 7 (HG7), Aeromonas sp. TH002, Aeromonas sp. TH004, Aeromonas sp. TH005, Aeromonas sp. TH018, Aeromonas sp. TH032, Aeromonas sp. TH035, Aeromonas sp. TH037, Aeromonas sp. TH040, Aeromonas sp. TH070, Aeromonas sp. TH082, Aeromonas sp. TH103, Aeromonas sp. TH112, Aeromonas sp. TH116, Aeromonas sp. TH119, CCUG 14830, CECT 4245, CIP 74.33, DSM 19176, JCM 2139, LMG 3783, LMG:3783, NCTC 12979, strain 208
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