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.
Knowledge-based Evidence
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
pepPCOG0006, Xaa-Pro aminopeptidase; Belongs to the peptidase M24B family. (353 aa)    
Predicted Functional Partners:
uvrA
Excinuclease ABC-subunit A; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate.
  
    0.875
pepT
Peptidase T; Cleaves the N-terminal amino acid of tripeptides. Belongs to the peptidase M20B family.
  
 
 0.842
pepN
Aminopeptidase N.
  
 
 0.838
pepF
Oligoendopeptidase F.
      
 0.792
comEB
dCMP deaminase.
  
  
 0.779
smi_1577
Peptidase M20 superfamily.
   
 
 0.745
smi_0639
Peptidase M13 superfamily; COG3590, metalloendopeptidase.
   
  
 0.730
smi_1927
Conserved hypothetical protein.
       0.725
pepX
Xaa-Pro dipeptidyl-peptidase; Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline; Belongs to the peptidase S15 family.
  
   
 0.682
map
Methionyl aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
  
  
 0.642
Your Current Organism:
Streptococcus mitis
NCBI taxonomy Id: 365659
Other names: S. mitis B6, Streptococcus mitis B6, Streptococcus mitis str. B6, Streptococcus mitis strain B6
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