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
KPM46662.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (424 aa)    
Predicted Functional Partners:
KPM50095.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.995
KPM47505.1
Peptidase M16; Derived by automated computational analysis using gene prediction method: Protein Homology.
     0.978
KPM46876.1
NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.962
KPM46878.1
NADH dehydrogenase; 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.
   
 0.962
KPM46879.1
NADH-quinone oxidoreductase subunit E; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
  0.959
KPM46634.1
Cytochrome c oxidase subunit II; 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).
  
 
 0.947
KPM46633.1
Cytochrome C oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family.
    
 0.937
KPM49401.1
Deoxynucleoside kinase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  0.929
nuoD
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 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 49 kDa subunit family.
   
 0.928
nuoD-2
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 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 49 kDa subunit family.
   
 0.928
Your Current Organism:
Jiulongibacter sediminis
NCBI taxonomy Id: 1605367
Other names: J. sediminis, Jiulongibacter sediminis Liu et al. 2016, KCTC 42153, Lacihabitans sp. MCCC 1A00733, Leadbetterella sp. JN14-9, MCCC 1A00733, strain JN14-9
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