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
SHE96909.1Excalibur calcium-binding domain-containing protein. (207 aa)    
Predicted Functional Partners:
SHF82701.1
WD40-like Beta Propeller Repeat.
  
   0.677
guaA
GMP synthase (glutamine-hydrolysing); Catalyzes the synthesis of GMP from XMP.
  
 
  0.652
SHE96867.1
Two component transcriptional regulator, LuxR family.
       0.572
SHG95202.1
Hypothetical protein.
  
     0.430
rbfA
Ribosome-binding factor A; One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA.
  
  
 0.409
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.
   
 
 0.408
Your Current Organism:
Streptoalloteichus hindustanus
NCBI taxonomy Id: 2017
Other names: ATCC 31217, DSM 44523, IFO 15115, JCM 3268, NBRC 15115, NRRL B-11280, S. hindustanus, Streptalloteichus hindustanensis, Streptalloteichus hindustanus, Streptoalloteichus hindustanensis, VKM Ac-683, strain C677-91
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