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
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
NIDE0963Protein of unknown function, contains acyl transferase and methyltransferase regions; No homology to any previously reported sequences; 2071574, 7893120. (910 aa)    
Predicted Functional Partners:
nuoCD
NADH-quinone oxidoreductase, subunits C and D; Function of homologous gene experimentally demonstrated in an other organism; enzyme; In the N-terminal section; belongs to the complex I 30 kDa subunit family.
  
 
 0.949
nuoE
NADH-quinone oxidoreductase, subunit E; Function of homologous gene experimentally demonstrated in an other organism; enzyme.
   
   0.805
fdsG
Formate dehydrogenase, gamma subunit; Function of strongly homologous gene; enzyme.
   
   0.805
NIDE0964
Putative Histidine kinase, contains GAF domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
 
    0.772
nuoD
NADH-quinone oxidoreductase, subunit 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; Belongs to the complex I 49 kDa subunit family.
   
 
 0.768
nuoF
NADH-quinone oxidoreductase, subunit F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family.
  
 
 0.755
fdsB
Formate dehydrogenase, beta subunit; Function of strongly homologous gene; enzyme.
  
 
 0.755
nuoF-2
NADH-quinone oxidoreductase, subunit F; Function of homologous gene experimentally demonstrated in an other organism; carrier.
  
 
 0.755
nuoH
NADH-quinone oxidoreductase, membrane 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.
   
 
 0.746
nuoC
NADH-quinone oxidoreductase, subunit C; 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 30 kDa subunit family.
   
 
 0.741
Your Current Organism:
Nitrospira defluvii
NCBI taxonomy Id: 330214
Other names: Candidatus Nitrospira defluvii, LMG 27402, LMG:27402, N. defluvii, NCIMB 14950, strain A17
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