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
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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
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experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
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[Homology]
Score
flaKPreflagellin peptidase; Cleaves the N-terminal leader peptide from preflagellins. (230 aa)    
Predicted Functional Partners:
flaJ
Flagella accessory protein J; Citation: J. Bac. 183: 7154-7164.
     
 0.923
flaB2
Flagellin B2; Flagellin is the subunit protein which polymerizes to form the filaments of archaeal flagella.
     
 0.848
MMP0281
Hypothetical nucleotide binding protein; Citation: Mol. Gen. Genet. 204 (1), 133-140 (1986).
     
 0.837
flaB1
Flagellin B1 percursor; Flagellin is the subunit protein which polymerizes to form the filaments of archaeal flagella.
     
 0.814
flaI
Flagella accessory protein I; Citation: J. Bac. 183: 7154-7164.
     
 0.759
flaH
Flagella accessory protein H; Citation: J. Bac. 183: 7154-7164.
     
 0.718
flaB3
Flagellin B3; Flagellin is the subunit protein which polymerizes to form the filaments of archaeal flagella.
     
 0.701
MMP1719
Conserved hypothetical protein.
       0.700
hisI
Phosphoribosyl-AMP cyclohydrolase; Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
       0.689
rce1
Conserved Hypothetical Protein; Endopeptidase which proteolytically removes the C-terminal three residues of farnesylated peptides containing the CAAX motif where C is cysteine, A is an aliphatic amino acid and X is any amino acid. Cleaves the CAAX motif C-terminal to both P1 and P1' positions. Hydrolysis depends on a farnesylated cysteine residue and no activity is shown towards geranylgeranylated peptides.
  
  
 0.675
Your Current Organism:
Methanococcus maripaludis S2
NCBI taxonomy Id: 267377
Other names: M. maripaludis S2, Methanococcus maripaludis LL, Methanococcus maripaludis str. S2, Methanococcus maripaludis strain S2
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