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
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Textmining
[Homology]
Score
petCRieske (2Fe-2S) domain protein; Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. Belongs to the Rieske iron-sulfur protein family. (179 aa)    
Predicted Functional Partners:
petB
Cytochrome b/b6, N-terminal domain protein; Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
 
 0.999
petA
Cytochrome f; Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
 
 
 0.999
petD
Cytochrome b/b6, C-terminal domain protein; Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
 
 
 0.998
petN
PetN family protein; Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
    
 0.978
petM
PetM of cytochrome b6f complex subunit 7; Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
    
 0.978
ACC81318.1
PFAM: Cytochrome b/b6, N-terminal domain; KEGG: ana:all0253 similar to cytochrome b6.
 
 0.970
ndhH
NADH-ubiquinone oxidoreductase, chain 49kDa; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
   
 
 0.925
ACC80218.1
PFAM: Rieske [2Fe-2S] domain protein; KEGG: ana:all0606 cytochrome b6/f-complex iron-sulfur protein.
  
  
0.923
ACC83583.1
PFAM: Rieske [2Fe-2S] domain protein; KEGG: pmi:PMT9312_0462 twin-arginine translocation pathway signal.
  
  
 
0.919
ndhJ
NADH dehydrogenase (ubiquinone), 30 kDa subunit; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
   
 
 0.913
Your Current Organism:
Nostoc punctiforme
NCBI taxonomy Id: 63737
Other names: N. punctiforme PCC 73102, Nostoc punctiforme ATCC 29133, Nostoc punctiforme PCC 73102, Nostoc sp. (strain ATCC 29133 / PCC 73102), Nostoc sp. ATCC 29133, Nostoc sp. PCC 73102
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