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.
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
msrPOxidoreductase, molybdopterin binding protein; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to [...] (331 aa)    
Predicted Functional Partners:
msrQ
Ferric reductase domain protein protein transmembrane component, N-terminal domain protein; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides elec [...]
 
  
 0.993
Aave_1504
PFAM: cytochrome c, class I; KEGG: pol:Bpro_2050 cytochrome c, class I.
   
 
 0.720
Aave_3038
PFAM: cytochrome c, class I; KEGG: bpm:BURPS1710b_0038 cytochrome c family protein.
   
 
 0.720
Aave_1526
Cytochrome c oxidase, cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex.
   
 
 0.666
Aave_0986
PFAM: cytochrome c assembly protein; KEGG: pol:Bpro_0774 cytochrome c assembly protein.
       0.660
Aave_0985
PFAM: ResB family protein; KEGG: pol:Bpro_0773 ResB-like.
       0.656
Aave_2800
PFAM: OmpA/MotB domain protein; KEGG: pol:Bpro_3552 OmpA/MotB.
  
 
 0.613
Aave_3907
Cytochrome c oxidase, subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
   
 
 0.606
Aave_3925
PFAM: cytochrome c, class I; KEGG: bbr:BB1776 putative cytochrome.
   
 
 0.605
Aave_1116
PFAM: Transthyretin; KEGG: pol:Bpro_1426 transthyretin; Belongs to the transthyretin family. 5-hydroxyisourate hydrolase subfamily.
   
   0.523
Your Current Organism:
Acidovorax citrulli
NCBI taxonomy Id: 397945
Other names: A. citrulli AAC00-1, Acidovorax avenae subsp. citrulli AAC00-1, Acidovorax citrulli AAC00-1, Acidovorax citrulli str. AAC00-1, Acidovorax citrulli strain AAC00-1
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