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
ORV15414.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (218 aa)    
Predicted Functional Partners:
ORV15413.1
Haloacid dehalogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.777
ORV15412.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.736
ORV15449.1
Anti-anti-sigma factor; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the anti-sigma-factor antagonist family.
 
     0.688
ORV12726.1
Glycerol-3-phosphate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family.
  
  
  0.550
ORV14621.1
Glycerol-3-phosphate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family.
  
  
  0.545
nuoI
NADH dehydrogenase; 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 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.
    
 0.531
nuoN
NADH-quinone oxidoreductase subunit N; 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 2 family.
    
  0.530
ORV18042.1
NADH:ubiquinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.530
nuoK
NADH:ubiquinone oxidoreductase subunit K; 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 4L family.
    
  0.530
ORV18045.1
NADH:ubiquinone oxidoreductase subunit J; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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.
    
  0.530
Your Current Organism:
Mycobacterium celatum
NCBI taxonomy Id: 28045
Other names: ATCC 51131, CCUG 39185, CDC 90-0899, CIP 106109, DSM 44243, JCM 12373, M. celatum, NCTC 13729
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