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
atpDV-type ATPase, D subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. (234 aa)    
Predicted Functional Partners:
atpB
H+transporting two-sector ATPase alpha/beta subunit central region; Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type beta chain is a regulatory subunit.
 
 0.999
atpA
H+transporting two-sector ATPase alpha/beta subunit central region; Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type alpha chain is a catalytic subunit. Belongs to the ATPase alpha/beta chains family.
 
 0.999
Trad_2019
InterPro IPR008218; KEGG: dge:Dgeo_2048 vacuolar H+-transporting two-sector ATPase, F subunit; PFAM: Vacuolar H+transporting two-sector ATPase F subunit; SPTR: C1XVU9 Archaeal/vacuolar-type H+-ATPase subunit F; PFAM: ATP synthase (F/14-kDa) subunit.
  
 0.999
atpC
H+transporting two-sector ATPase C (AC39) subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane.
 
 0.999
Trad_2021
COGs: COG1390 H+-ATPase subunit E; InterPro IPR002842; KEGG: dge:Dgeo_2050 H+-transporting two-sector ATPase, E subunit; PFAM: H+transporting two-sector ATPase E subunit; SPTR: Q1IWP0 V-type ATP synthase subunit E; PFAM: ATP synthase (E/31 kDa) subunit.
  
 0.999
Trad_2022
H+transporting two-sector ATPase C subunit; InterPro IPR002379; KEGG: ttj:TTHA1277 V-type ATP synthase, subunit K; PFAM: H+transporting two-sector ATPase C subunit; SPTR: Q72J68 V-type sodium ATP synthase subunit K Homolog; PFAM: ATP synthase subunit C.
 
 0.999
Trad_2023
V-type ATPase 116 kDa subunit; COGs: COG1269 H+-ATPase subunit I; InterPro IPR002490; KEGG: ttj:TTHA1278 V-type ATP synthase subunit I; PFAM: V-type ATPase 116 kDa subunit; SPTR: Q72J67 V-type sodium ATP synthase subunit I; PFAM: V-type ATPase 116kDa subunit family; Belongs to the V-ATPase 116 kDa subunit family.
 
 0.999
Trad_2024
KEGG: ttj:TTHA1279 V-type ATP synthase, subunit (VapC-therm); SPTR: B7A885 V-type ATP synthase, subunit (VapC-therm).
    
  0.934
ppa
Inorganic diphosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
   
 
  0.931
Trad_2197
Chalcone and stilbene synthase domain protein; COGs: COG3424 naringenin-chalcone synthase; InterProIPR016039:IPR016038:IPR011141:IPR001099:IPR 012328; KEGG: ddr:Deide_21770 putative naringenin-chalcone synthase (flavonone synthase, 6-deoxychalcone synthase); PFAM: chalcone and stilbene synthase domain protein; SPTR: C1CZF5 Putative naringenin-chalcone synthase (Flavonone synthase, 6-deoxychalcone synthase); PFAM: Chalcone and stilbene synthases, N-terminal domain; Chalcone and stilbene synthases, C-terminal domain.
    
 0.545
Your Current Organism:
Truepera radiovictrix
NCBI taxonomy Id: 649638
Other names: T. radiovictrix DSM 17093, Truepera radiovictrix DSM 17093, Truepera radiovictrix RQ-24, Truepera radiovictrix str. DSM 17093, Truepera radiovictrix strain DSM 17093
Server load: low (24%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.