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
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easEFAD-linked oxidoreductase easE; FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid. DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4- dimethylallyl-L-tryptophan. The second step is catalyzed by the methyltransferase easF that methylates 4- dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine. The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethy [...] (500 aa)    
Predicted Functional Partners:
easF
4-dimethylallyltryptophan N-methyltransferase easF; 4-dimethylallyltryptophan N-methyltransferase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid. DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan. The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L- methionine, resulting in the formation of 4-dimethylallyl-L-abrine. The catalase easC and the FAD-dependent oxido [...]
      
 0.560
Your Current Organism:
Trichophyton benhamiae
NCBI taxonomy Id: 663331
Other names: Arthroderma benhamiae CBS 112371, T. benhamiae CBS 112371, Trichophyton benhamiae CBS 112371
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