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
Acry_1122PFAM: sodium/calcium exchanger membrane region. (338 aa)    
Predicted Functional Partners:
Acry_1121
TIGRFAM: ATPase, P-type (transporting), HAD superfamily, subfamily IC; PFAM: cation transporting ATPase domain protein; Haloacid dehalogenase domain protein hydrolase; cation transporting ATPase domain protein; E1-E2 ATPase-associated domain protein.
 
 
 0.859
nuoC-2
NADH dehydrogenase subunit C / NADH dehydrogenase subunit D; 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; In the N-terminal section; belongs to the complex I 30 kDa subunit family.
     
 0.482
Acry_1123
Oxidoreductase domain protein; PFAM: Semialdehyde dehydrogenase, NAD - binding; oxidoreductase domain protein; Oxidoreductase, C-terminal domain; homoserine dehydrogenase, NAD-binding.
  
    0.457
Acry_1117
TIGRFAM: NADH-quinone oxidoreductase, E subunit; PFAM: NADH dehydrogenase (ubiquinone), 24 kDa subunit.
       0.455
Acry_1116
PFAM: Respiratory-chain NADH dehydrogenase domain, 51 kDa subunit.
       0.453
nuoB2
NADH dehydrogenase subunit B; 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.
       0.453
nuoA-2
NADH dehydrogenase subunit A; 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; Belongs to the complex I subunit 3 family.
       0.453
nuoH-2
NADH dehydrogenase subunit H; 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. This subunit may bind ubiquinone.
       0.450
Acry_1115
TIGRFAM: NADH-quinone oxidoreductase, chain G; PFAM: ferredoxin; molybdopterin oxidoreductase Fe4S4 region; Belongs to the complex I 75 kDa subunit family.
       0.450
nuoI-2
NADH dehydrogenase 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.
       0.439
Your Current Organism:
Acidiphilium cryptum
NCBI taxonomy Id: 349163
Other names: A. cryptum JF-5, Acidiphilium cryptum JF-5, Acidiphilium cryptum str. JF-5, Acidiphilium cryptum strain JF-5, Acidiphilum cryptum JF-5
Server load: low (14%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.