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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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query proteins and first shell of interactors
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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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Score
Psed_1111PFAM: Peptidase M16, C-terminal; Peptidase M16, N-terminal; KEGG: svi:Svir_06880 predicted Zn-dependent peptidase. (457 aa)    
Predicted Functional Partners:
Psed_1110
PFAM: Peptidase M16, C-terminal; Peptidase M16, N-terminal; KEGG: svi:Svir_06870 predicted Zn-dependent peptidase.
     0.996
Psed_3297
KEGG: scb:SCAB_16891 respiratory chain oxidoreductase; PFAM: NADH:ubiquinone oxidoreductase, 51kDa subunit; NADH:ubiquinone oxidoreductase, 24kDa subunit; Soluble ligand binding domain; NADH ubiquinone oxidoreductase, F subunit, iron sulphur binding; SMART: NADH ubiquinone oxidoreductase, F subunit, iron sulphur binding.
   
 0.971
atpA
ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. Belongs to the ATPase alpha/beta chains family.
   
 0.863
Psed_1112
NAD(+) diphosphatase; KEGG: fal:FRAAL0398 NADH pyrophosphatase; PFAM: NUDIX hydrolase domain; Zinc ribbon, NADH pyrophosphatase; NADH pyrophosphatase-like, N-terminal.
  
  
 0.855
atpH
ATP synthase subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family.
   
 0.850
Psed_5563
NADH-quinone oxidoreductase, chain G; 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.
   
 0.848
Psed_2755
Rieske (2Fe-2S) iron-sulfur domain protein; PFAM: Rieske [2Fe-2S] iron-sulphur domain; KEGG: sen:SACE_1686 ubiquinol-cytochrome c reductase iron-sulfur subunit.
   
 0.837
Psed_4723
PFAM: Rieske [2Fe-2S] iron-sulphur domain; KEGG: tcu:Tcur_2193 Rieske (2Fe-2S) domain-containing protein.
   
 0.837
nuoC
NAD(P)H-quinone oxidoreductase subunit J; 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.
  
 
 0.814
nuoI
NAD(P)H-quinone oxidoreductase subunit I; 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.
  
 
 0.807
Your Current Organism:
Pseudonocardia dioxanivorans
NCBI taxonomy Id: 675635
Other names: P. dioxanivorans CB1190, Pseudonocardia dioxanivorans CB1190, Pseudonocardia dioxanivorans DSM 44775, Pseudonocardia dioxanivorans str. CB1190, Pseudonocardia dioxanivorans strain CB1190
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