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
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.
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from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
prmCSAM-dependent methyltransferase; HemK; PrmC; transfers a methyl group from S-adenosylmethionine to amide nitrogen of specific glutamine residues in protein chain release factors PrfA and PrfB; Derived by automated computational analysis using gene prediction method: Protein Homology. (282 aa)    
Predicted Functional Partners:
prfA
Peptide chain release factor 1; Recognizes the termination signals UAG and UAA during protein translation a specificity which is dependent on amino acid residues residing in loops of the L-shaped tRNA-like molecule of RF1; this protein is similar to release factor 2; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.990
KOY60778.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.794
hemA
glutamyl-tRNA reductase; Catalyzes the formation of glutamate-1-semialdehyde from glutamyl-tRNA(Glu) and NADPH; the second step of the pathway is catalyzed by glutamate-1-semialdehyde aminomutase which results in the formation of 5-aminolevulinic acid; functions in porphyrin (tetrapyrroles) biosynthesis; the crystal structure showed a C-terminal dimerization domain that appears to be absent in Chlamydial proteins; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.707
kdsA
2-dehydro-3-deoxyphosphooctonate aldolase; Catalyzes the formation of 2-dehydro-3-deoxy-D-octonate 8-phosphate from phosphoenolpyruvate and D-arabinose 5-phosphate in LPS biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the KdsA family.
       0.668
trmB
tRNA (guanine-N(7)-)-methyltransferase; catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA by transferring the methyl residue from S-adenosyl-L-methionine; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 
 0.591
ybeY
Metal-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
   
 0.531
KOY60772.1
Ribose-phosphate pyrophosphokinase; Catalyzes the formation of 5-phospho-alpha-D-ribose 1-phosphate from D-ribose 5-phosphate and ATP; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
   0.520
atpE
ATP F0F1 synthase subunit C; Produces ATP from ADP in the presence of a proton gradient across the membrane. Subunit C is part of the membrane proton channel F0; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
   0.466
gcvP
Glycine dehydrogenase; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family.
     
  0.454
ispE
Kinase; Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol; Belongs to the GHMP kinase family. IspE subfamily.
       0.452
Your Current Organism:
Photorhabdus heterorhabditis
NCBI taxonomy Id: 880156
Other names: ATCC BAA-2479, DSM 25263, P. heterorhabditis, Photorhabdus heterorhabditis Ferreira et al. 2014, Photorhabdus sp. Q614, Photorhabdus sp. Q614(2009), Photorhabdus sp. SF41, Photorhabdus sp. SF783, strain SF41
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