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.
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
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[Homology]
Score
psaIPhotosystem I reaction center; May help in the organization of the PsaL subunit. Belongs to the PsaI family. (46 aa)    
Predicted Functional Partners:
psaL
Photosystem I reaction center; KEGG: car:cauri_1558 0.84 cdsA; phosphatidate cytidylyltransferase K00981.
   
 
 0.902
EKF05001.1
Photosystem I reaction center; KEGG: mar:MAE_11850 0.53 gmk; guanylate kinase; K00942 guanylate kinase.
    
 
 0.887
psaM
Photosystem I reaction center subunit XII; Psort location: CytoplasmicMembrane, score: 9.82.
    
 
 0.887
psaA
Photosystem I P700 apoprotein A1; PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6; Belongs to the PsaA/PsaB family.
    
 
 0.887
psaB
Photosystem I P700 apoprotein A2; PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6; Belongs to the PsaA/PsaB family.
    
 
 0.886
EKF06019.1
Photosystem I reaction center; KEGG: rsa:RSal33209_0709 0.91 3-oxoacyl-[acyl-carrier protein] reductase; Psort location: CytoplasmicMembrane, score: 9.82.
    
 
 0.884
EKE97054.1
Putative PsaC; Photosystem I iron-sulfur protein; KEGG: drm:Dred_3277 0.0024 glycyl-radical activating family protein; K04069 pyruvate formate lyase activating enzyme; Psort location: CytoplasmicMembrane, score: 10.00.
    
 
 0.884
EKF00444.1
Photosystem I reaction center; KEGG: fre:Franean1_1984 0.91 ATP-dependent metalloprotease FtsH; K03798 cell division protease FtsH; Psort location: CytoplasmicMembrane, score: 9.82.
    
 
 0.869
EKF05640.1
Photosystem I reaction center; KEGG: sdn:Sden_1559 0.998 phosphatidate cytidylyltransferase; K00981 phosphatidate cytidylyltransferase; Psort location: CytoplasmicMembrane, score: 9.82.
    
 
 0.834
psaJ
Photosystem I reaction center; May help in the organization of the PsaE and PsaF subunits. Belongs to the PsaJ family.
    
 
 0.834
Your Current Organism:
Tolypothrix sp. PCC7601
NCBI taxonomy Id: 1188
Other names: Calothrix sp. PCC 7601, Fremyella diplosiphon ACMM 396, Fremyella diplosiphon IAM M-100, Fremyella diplosiphon UTEX B 481, Microchaete diplosiphon UTEX B 481, T. sp. PCC 7601, Tolypothrix (Calothrix) sp. PCC 7601, Tolypothrix sp. PCC 7601, Tolypothrix sp. PCC 7601 = UTEX B 481
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.