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
SDT79104.1Type VII secretion-associated serine protease mycosin; Belongs to the peptidase S8 family. (645 aa)    
Predicted Functional Partners:
SDS79963.1
Serine protease, subtilisin family.
  
  
 
0.721
SDT79106.1
Type VII secretion-associated serine protease mycosin; Belongs to the peptidase S8 family.
 
    
0.539
SDS73518.1
Serine protease, subtilisin family; Belongs to the peptidase S8 family.
  
  
 
0.530
SDS29738.1
Alpha-tubulin suppressor.
   
  0.518
SDS38834.1
Alpha-tubulin suppressor.
 
 
  0.518
SDT75650.1
Hypothetical protein.
  
 
  0.513
SDT74377.1
Hypothetical protein.
    
  0.442
SDT78522.1
Legume lectin domain-containing protein.
    
  0.442
SDT68413.1
Cytochrome oxidase assembly protein ShyY1.
    
   0.407
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.
    
   0.407
Your Current Organism:
Actinoplanes derwentensis
NCBI taxonomy Id: 113562
Other names: A. derwentensis, ATCC 49798, DSM 43941, IFO 14935, JCM 7556, NBRC 14935, NCIB 12875, NCIB:12875, NCIMB 12875, NRRL B-16692, strain LA 107
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.