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
Tbis_1069PFAM: peptidase M16 domain protein; KEGG: dal:Dalk_4744 peptidase M16 domain protein; Belongs to the peptidase M16 family. (435 aa)    
Predicted Functional Partners:
Tbis_1294
PFAM: Rieske [2Fe-2S] domain protein; KEGG: vei:Veis_4950 Rieske (2Fe-2S) domain protein.
   
 0.988
Tbis_1998
PFAM: Rieske [2Fe-2S] domain protein; KEGG: gme:Gmet_0538 Rieske (2Fe-2S) region.
   
 0.988
Tbis_0286
NADH-quinone oxidoreductase, F subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family.
   
 
 0.977
Tbis_1293
PFAM: Cytochrome b/b6 domain; KEGG: sus:Acid_6208 cytochrome b/b6 domain- containing protein.
    
 0.975
Tbis_0287
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.
   
 
 0.970
Tbis_0285
TIGRFAM: NADH-quinone oxidoreductase, E subunit; PFAM: NADH dehydrogenase (ubiquinone) 24 kDa subunit; KEGG: aba:Acid345_1312 NADH-quinone oxidoreductase, E subunit.
   
 
 0.960
nuoI
NADH-quinone oxidoreductase, chain 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.
  
 
 0.948
nuoI-2
4Fe-4S ferredoxin iron-sulfur binding domain protein; 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.
  
 
 0.948
Tbis_2930
PFAM: NmrA family protein; KEGG: aav:Aave_1295 NmrA family protein.
   
 
 0.945
nuoD
NADH dehydrogenase I, D subunit; 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 49 kDa subunit family.
   
 
 0.927
Your Current Organism:
Thermobispora bispora
NCBI taxonomy Id: 469371
Other names: T. bispora DSM 43833, Thermobispora bispora ATCC 19993, Thermobispora bispora DSM 43833, Thermobispora bispora str. DSM 43833, Thermobispora bispora strain DSM 43833
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