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
xsaalpha-L-arabinofuranosidase. (498 aa)    
Predicted Functional Partners:
araA
L-arabinose isomerase; Catalyzes the conversion of L-arabinose to L-ribulose.
 
 
 0.947
abfA
alpha-L-arabinofuranosidase.
 
  
 
0.936
ABC3369
Beta-xylosidase; Belongs to the glycosyl hydrolase 43 family.
 
  
 0.880
uxaC
Uronate isomerase.
  
  
 0.846
ABC1212
Conserved hypothetical protein.
 
   
 0.792
ABC0555
Alpha-glucuronidase; Belongs to the glycosyl hydrolase 67 family.
 
   
 0.749
ABC1148
Xylosidase/arabinosidase; alpha-L-arabinofuranosidase; Belongs to the glycosyl hydrolase 43 family.
 
  
 0.713
ABC1138
Conserved hypothetical protein.
 
   
 0.634
araD
L-ribulose-5-phosphate 4-epimerase.
 
  
 0.611
ABC3370
Conserved hypothetical protein.
       0.608
Your Current Organism:
Bacillus clausii
NCBI taxonomy Id: 66692
Other names: B. clausii KSM-K16, Bacillus clausii KSM-K16, Bacillus sp. (strain KSM-K16), Bacillus sp. KSM-K16
Server load: low (36%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.