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
Node Content
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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from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
ANW19585.1Ribosomal methyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. (479 aa)    
Predicted Functional Partners:
rpsE
30S ribosomal protein S5; Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. Belongs to the universal ribosomal protein uS5 family.
    
 0.851
BB341_27660
Polyketide synthase; Frameshifted; incomplete; partial on complete genome; missing stop; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.814
ANW17161.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.723
nuoB2
NADH-quinone oxidoreductase subunit B; 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.
    
 0.703
nuoB1
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.
    
 0.703
ANW17142.1
Non-ribosomal peptide synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.672
nuoD1
NADH dehydrogenase 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 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.
    
 0.657
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 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.
    
 0.657
rpsO
30S ribosomal protein S15; Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
   
  0.643
ANW19118.1
Benzoate transporter; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.634
Your Current Organism:
Streptomyces clavuligerus
NCBI taxonomy Id: 1901
Other names: ATCC 27064, BCRC 11518, CBS 226.75, CCRC 11518, CCRC:11518, CECT 3125, DSM 40751, DSM 738, IFO 13307, IMET 43657, JCM 4710, KCTC 9095, NBRC 13307, NCIMB 12785, NCIMB 14335, NRRL 3585, S. clavuligerus, Streptomyces clavuligerus ATCC 27064, Streptomyces clavuligerus NRRL 3585, VKM Ac-602
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