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
A0A443I7R7Uncharacterized protein. (415 aa)    
Predicted Functional Partners:
A0A443HM52
Putative alpha-1,2-mannosyltransferase.
     
 0.735
A0A443HRF5
Anp1-domain-containing protein.
    
 0.707
A0A443HHQ7
Polyketide synthase.
  
 
 0.658
A0A443HJF8
Putative polyketide synthase.
  
 
 0.658
VdtX
Highly reducing polyketide synthase VdtX; Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of viriditoxin, one of the 'classical' secondary metabolites produced by fungi and that has antibacterial activity. The first step is performed by the polyketide synthase VdtA which condenses one acetyl-CoA and 6 malonyl- CoA units to form the heptaketide monomer backbone of viriditoxin. The product of VdtA is then O-methylated on C7 by the O-methyltransferase VdtC. The O-methyl group is important for the stereoselective coupling of the monomers at the [...]
  
 
 0.658
VdtA
Non-reducing polyketide synthase VdtA; Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of viriditoxin, one of the 'classical' secondary metabolites produced by fungi and that has antibacterial activity. The first step is performed by the polyketide synthase VdtA which condenses one acetyl-CoA and 6 malonyl- CoA units to form the heptaketide monomer backbone of viriditoxin. The product of VdtA is then O-methylated on C7 by the O-methyltransferase VdtC. The O-methyl group is important for the stereoselective coupling of the monomers at the final [...]
  
 
 0.658
A0A443HKV5
Alpha/Beta hydrolase protein.
  
 
 0.658
A0A443HKW4
Polyketide synthase.
  
 
 0.658
A0A443HMP7
Uncharacterized protein.
  
 
 0.658
A0A443HMX5
Thioesterase-like superfamily-domain-containing protein.
  
 
 0.658
Your Current Organism:
Byssochlamys spectabilis
NCBI taxonomy Id: 264951
Other names: ATCC 90900, B. spectabilis, Byssochlamys spectabilis (Udagawa & Shoji Suzuki) Houbraken & Samson 2008, CBS 101075, FRR 5219, JCM 12815, Pacilomyces variotii, Paecilomyces spectabilis, Paecilomyces variotii, Paecilomyces variotti, Paecilomyces vatiotii, Talaromyces spectabilis
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