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
SEB04347.1PRC-barrel domain-containing protein. (171 aa)    
Predicted Functional Partners:
SEA15758.1
FKBP-type peptidyl-prolyl cis-trans isomerase.
    
   0.477
SEA15874.1
FKBP-type peptidyl-prolyl cis-trans isomerase FklB.
    
   0.477
SEA87708.1
FKBP-type peptidyl-prolyl cis-trans isomerase FkpA.
    
   0.477
SEA87732.1
FKBP-type peptidyl-prolyl cis-trans isomerase.
    
   0.477
SEB10469.1
FKBP-type peptidyl-prolyl cis-trans isomerase FkpA.
    
   0.477
SEB21647.1
Domain amino terminal to FKBP-type peptidyl-prolyl isomerase.
    
   0.477
SEB04322.1
Hypothetical protein.
       0.444
secY
Protein translocase subunit secY/sec61 alpha; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
   
 
 0.400
Your Current Organism:
Pedobacter hartonius
NCBI taxonomy Id: 425514
Other names: CIP 109468, DSM 19033, P. hartonius, Pedobacter hartonius Muurholm et al. 2007, WB 3.3-3
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