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
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Cooccurrence
Coexpression
Experiments
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[Homology]
Score
Slit_0167PFAM: protein of unknown function DUF185; KEGG: app:CAP2UW1_0267 protein of unknown function DUF185. (384 aa)    
Predicted Functional Partners:
nuoC
NADH (or F420H2) dehydrogenase, 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.
 
 
 0.811
nuoD
NADH dehydrogenase I, D subunit; 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.
 
 
 0.800
Slit_0166
KEGG: dar:Daro_3867 hypothetical protein.
       0.757
Slit_2099
PFAM: Zinc finger, CHCC-type; KEGG: dar:Daro_3295 hypothetical protein.
  
     0.735
Slit_2398
PFAM: Domain of unknown function DUF1841; KEGG: nmu:Nmul_A2703 hypothetical protein.
  
     0.700
bioC
Biotin biosynthesis protein BioC; Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L- methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
  
     0.697
Slit_1403
PFAM: 2,3-bisphosphoglycerate-independent phosphoglycerate mutase; KEGG: nmu:Nmul_A2416 hypothetical protein.
  
     0.696
nuoB
NADH-quinone oxidoreductase, B subunit; 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.
  
 
 0.692
Slit_1608
PFAM: Respiratory-chain NADH dehydrogenase domain 51 kDa subunit; NADH ubiquinone oxidoreductase, F subunit, iron sulphur binding; NADH dehydrogenase (ubiquinone) 24 kDa subunit; Soluble ligand binding domain; KEGG: dar:Daro_0979 NADH dehydrogenase.
    
 0.686
Slit_0168
PFAM: short-chain dehydrogenase/reductase SDR; KEGG: nmu:Nmul_A0336 pteridine reductase.
       0.643
Your Current Organism:
Sideroxydans lithotrophicus
NCBI taxonomy Id: 580332
Other names: S. lithotrophicus ES-1, Sideroxydans lithotrophicus ES-1, Sideroxydans lithotrophicus str. ES-1, Sideroxydans lithotrophicus strain ES-1, iron-oxidizing lithotroph ES-1
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