STRINGSTRING
ftrC protein (Synechocystis sp. PCC6803) - STRING interaction network
"ftrC" - Ferredoxin-thioredoxin reductase catalytic chain in Synechocystis sp. PCC6803
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:
some 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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ftrCFerredoxin-thioredoxin reductase catalytic chain; Catalytic subunit of the ferredoxin-thioredoxin reductase (FTR), which catalyzes the two-electron reduction of thioredoxins by the electrons provided by reduced ferredoxin (118 aa)    
Predicted Functional Partners:
ftrV
Ferredoxin thioredoxin reductase variable chain; Variable subunit of the ferredoxin-thioredoxin reductase (FTR), which catalyzes the two-electron reduction of thioredoxins by the electrons provided by reduced ferredoxin (75 aa)
   
 
 
  0.998
fed
Ferredoxin; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions (97 aa)
     
      0.975
sll0662
Bacterial type ferredoxin family protein (133 aa)
     
      0.879
trxA
Thioredoxin; Component of the thioredoxin-thioredoxin reductase system. Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (107 aa)
     
 
  0.869
slr0565
Hypothetical protein (325 aa)
 
        0.836
sll0555
Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed (280 aa)
   
        0.799
psaF
Photosystem I subunit III; Probably participates in efficiency of electron transfer from plastocyanin to P700 (or cytochrome c553 in algae and cyanobacteria). This plastocyanin-docking protein contributes to the specific association of plastocyanin to PSI (165 aa)
   
   
  0.798
slr1702
Hypothetical protein (251 aa)
   
        0.796
slr1676
Hypothetical protein (163 aa)
   
        0.789
pcxA
Proton extrusion protein PcxA; Involved in light-induced Na(+)-dependent proton extrusion. Also seems to be involved in CO(2) transport (440 aa)
   
          0.777
Your Current Organism:
Synechocystis sp. PCC6803
NCBI taxonomy Id: 1148
Other names: Aphanocapsa sp. (strain N-1), Aphanocapsa sp. N-1, S. sp. PCC 6803, Synechocystis, Synechocystis PCC6803, Synechocystis sp. (ATCC 27184), Synechocystis sp. (PCC 6803), Synechocystis sp. (strain PCC 6803), Synechocystis sp. ATCC 27184, Synechocystis sp. PCC 6803, Synechocystis sp. PCC 6803 A, Synechocystis sp. PCC 6803 B, Synechocystis sp. PCC6803
Server load: low (14%) [HD]