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
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
NPD11_673[C] COG0221 Inorganic pyrophosphatase. (116 aa)    
Predicted Functional Partners:
AQM60010.1
HAD-SF-IA-v1: HAD hydrolase, IA, variant 1 family protein; [R] COG0546 Predicted phosphatases.
   
 
 0.917
AQM61136.1
[C] COG1227 Inorganic pyrophosphatase/exopolyphosphatase.
     
 0.911
atpF
ATP synthase F0, B subunit; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0); Belongs to the ATPase B chain family.
   
 
 0.852
atpG
ATP synthase F1, gamma subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
  
 
 0.833
atpH
ATP synthase F1, delta subunit; 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.
   
 
 0.828
atpA
ATP synthase F1, alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
   
 
 0.795
ntpD
V-type ATPase, D subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane.
   
 
  0.793
ntpB
V-type sodium ATPase subunit B; Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type beta chain is a regulatory subunit.
   
 
 0.758
ntpK
V-type sodium ATPase subunit K; [C] COG0636 F0F1-type ATP synthase, subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K; Belongs to the V-ATPase proteolipid subunit family.
   
 
 0.745
atpE
ATP synthase F0, C subunit; 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.
   
 
 0.745
Your Current Organism:
Clostridium baratii
NCBI taxonomy Id: 1561
Other names: ATCC 27638, Acuformis perennis, BCRC 14541, C. baratii, CCRC 14541, CCRC:14541, CCUG 24033, CIP 104306, Clostridium barati, Clostridium paraperfringens, Clostridium perenne, DSM 601, Inflabilis barati
Server load: low (12%) [HD]