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
Databases
Textmining
[Homology]
Score
KRV48968.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (310 aa)    
Predicted Functional Partners:
KRV48967.1
CopY family transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
  0.979
KRV48920.1
CopY family transcriptional repressor; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
  0.907
KRV48254.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.700
ftsH
Cell division protein FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family.
   
 0.662
secY
Preprotein translocase subunit SecY; 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.
   
 
 0.567
KRV50992.1
DNA primase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.512
KRV47405.1
Aminoglycoside phosphotransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.498
KRV49454.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.495
KRV50728.1
DNA primase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
   
 0.489
KRV49826.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.488
Your Current Organism:
Streptomyces vitaminophilus
NCBI taxonomy Id: 76728
Other names: ATCC 31673, Actinosporangium vitaminiphilum, Actinosporangium vitaminophilum, DSM 41686, IFO 14294, JCM 6054, NBRC 14294, NRRL B-16933, S. vitaminophilus, Streptomyces vitaminiphilus, Streptomyces vitaminophileus, strain SF 2080
Server load: medium (44%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.