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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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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
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Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
ACS18659.1PFAM: phospholipase D/Transphosphatidylase; SMART: phospholipase D/Transphosphatidylase; KEGG: rpi:Rpic_4172 phospholipase D/transphosphatidylase. (551 aa)    
Predicted Functional Partners:
ACS17147.1
Phosphatidylglycerophosphatase A; Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG).
     
 0.907
ACS17533.1
KEGG: bch:Bcen2424_5534 phospholipase C; TIGRFAM: phospholipase C, phosphocholine-specific; PFAM: phosphoesterase; protein of unknown function DUF756.
     
 0.904
ACS17719.1
Phospholipase C, phosphocholine-specific; KEGG: bmn:BMA10247_A0095 non-hemolytic phospholipase C; TIGRFAM: phospholipase C, phosphocholine-specific; PFAM: phosphoesterase; protein of unknown function DUF756.
     
 0.904
ACS18656.1
PFAM: FAD dependent oxidoreductase; KEGG: cti:RALTA_A1621 gamma-Glu-putrescine oxidase, FAD/NAD(P)-binding.
       0.554
ACS18657.1
PFAM: homospermidine synthase; KEGG: nmu:Nmul_A1700 homospermidine synthase.
       0.554
ACS18658.1
Hypothetical protein.
       0.554
Your Current Organism:
Variovorax paradoxus S110
NCBI taxonomy Id: 543728
Other names: V. paradoxus S110, Variovorax paradoxus str. S110, Variovorax paradoxus strain S110
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