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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
AHY45998.1DHHA2 domain; COG:COG1227: Inorganic pyrophosphatase/exopolyphosphatase [Energy production and conversion]; Pfam:PF02833:DHHA2; ProSiteProfiles:PS51371:Cystathionine beta-synthase, core; SMART:SM00116:Cystathionine beta-synthase, core; SUPERFAMILY:SSF64182:No Description. (540 aa)    
Predicted Functional Partners:
atpB
ATP synthase F0, A subunit; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Belongs to the ATPase A chain family.
  
 
 0.947
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.
  
 
 0.932
atpC
ATP synthase F1, epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane.
    
 0.911
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.
    
 0.910
atpD
atpD: ATP synthase F1, beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
    
 0.909
atpA
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.
  
 
  0.904
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.
  
 
  0.904
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.
    
 0.904
AHY45785.1
COG:COG0546: Predicted phosphatases [General function prediction only]; Pfam:PF13419:HAD-like domain; Pfam:PF13419:HAD-like domain; PRINTS:PR00413:Haloacid dehalogenase/epoxide hydrolase; SUPERFAMILY:SSF56784:HAD-like domain.
    
  0.902
ppk
Polyphosphate kinase 1; Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP). Belongs to the polyphosphate kinase 1 (PPK1) family.
    
  0.901
Your Current Organism:
Rubrobacter radiotolerans
NCBI taxonomy Id: 42256
Other names: ATCC 51242, Arthrobacter radiotolerans, CIP 106991, DSM 46359, DSM 5868, IAM 12072, IFO 14777, JCM 2153, NBRC 14777, R. radiotolerans, strain P-1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.