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
ELR96311.1Putative Zn-dependent peptidase; PFAM: Peptidase M16 inactive domain; Insulinase (Peptidase family M16); Belongs to the peptidase M16 family. (427 aa)    
Predicted Functional Partners:
ELR97752.1
Putative Zn-dependent peptidase; PFAM: Peptidase M16 inactive domain; Insulinase (Peptidase family M16); overlaps another CDS with the same product name.
 
    
0.915
petB
Cytochrome b subunit of the bc complex; 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.
    
 0.849
ELR98119.1
glycine/D-amino acid oxidase, deaminating; PFAM: Rieske [2Fe-2S] domain; FAD dependent oxidoreductase.
   
 0.844
petC
Rieske Fe-S 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.
   
 0.839
ndhH
NADH dehydrogenase I, D 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.
   
 
 0.819
ndhJ
NADH:ubiquinone oxidoreductase 27 kD 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.
   
 
 0.808
ELR96359.1
Acyl carrier protein; PFAM: Phosphopantetheine attachment site.
  
 0.804
ELR96361.1
PFAM: Acyl-CoA dehydrogenase, C-terminal domain; Acyl-CoA dehydrogenase, middle domain; Acyl-CoA dehydrogenase, N-terminal domain.
   
 0.794
ELR99536.1
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; PFAM: Phosphopantetheine attachment site; Acyl-CoA dehydrogenase, C-terminal domain; Acyl-CoA dehydrogenase, middle domain; AMP-binding enzyme; Acyl-CoA dehydrogenase, N-terminal domain.
   
 0.794
ndhK
NADH-quinone oxidoreductase, B 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; Belongs to the complex I 20 kDa subunit family.
   
 
 0.760
Your Current Organism:
Gloeocapsa sp. PCC73106
NCBI taxonomy Id: 102232
Other names: Chroococcus sp. SAG 6.82, G. sp. PCC 73106, Gloeocapsa sp. ATCC 27928, Gloeocapsa sp. PCC 73106
Server load: low (12%) [HD]