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ABK75868.1 ABK75868.1 ABK73463.1 ABK73463.1 nuoC nuoC nuoI nuoI nuoB nuoB nuoD nuoD nuoG nuoG ABK69760.1 ABK69760.1 pks pks ABK74901.1 ABK74901.1 ABK74760.1 ABK74760.1
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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
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
ABK75868.1Conserved hypothetical protein. (161 aa)    
Predicted Functional Partners:
ABK73463.1
Iron-sulfur binding oxidoreductase; Identified by match to protein family HMM PF00355; match to protein family HMM PF01266.
  
 
 0.891
nuoC
NADH-quinone oxidoreductase chain 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 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 30 kDa subunit family.
  
 0.838
nuoI
NADH-quinone oxidoreductase, I 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 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.
  
 0.828
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 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.
  
 0.819
nuoD
NADH-quinone oxidoreducatase, 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 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.
  
 0.817
nuoG
NADH-quinone oxidoreductase, G subunit; 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. Belongs to the complex I 75 kDa subunit family.
  
 0.812
ABK69760.1
Conserved hypothetical protein.
 
 
 0.801
pks
Type I modular polyketide synthase; Identified by match to protein family HMM PF00106; match to protein family HMM PF00107; match to protein family HMM PF00109; match to protein family HMM PF00550; match to protein family HMM PF00698; match to protein family HMM PF01370; match to protein family HMM PF02801.
  
 0.783
ABK74901.1
Conserved hypothetical protein.
 
    0.778
ABK74760.1
AMP-dependent synthetase and ligase; Identified by match to protein family HMM PF00501; match to protein family HMM PF00550.
  
 0.777
Your Current Organism:
Mycolicibacterium smegmatis
NCBI taxonomy Id: 246196
Other names: M. smegmatis MC2 155, Mycobacterium smegmatis MC2 155, Mycolicibacterium smegmatis MC2 155
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