STRINGSTRING
STRING protein interaction network
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
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
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Textmining
[Homology]
Score
AMF_814Called by Glimmer 2; Conserved hypothetical protein called by Glimmer 2; psort: bacterial inner membrane --- Certainty= 0.259(Affirmative); COG0612 Predicted Zn-dependent peptidases. (444 aa)    
Predicted Functional Partners:
AMF_815
Called by Glimmer 2; Conserved hypothetical protein called by Glimmer 2; psort: bacterial inner membrane --- Certainty= 0.100(Affirmative); COG0612 Predicted Zn-dependent peptidases; Belongs to the peptidase M16 family.
  
 0.979
petC
Cytochrome c1, heme protein precursor; Psort: bacterial inner membrane --- Certainty= 0.317(Affirmative); COG2857 CYT1 cytochrome c1.
   
 0.914
nuoF
NADH dehydrogenase I chain F (nuoF); NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family.
   
  0.895
nuoG
NADH dehydrogenase I chain G (nuoG); NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. Belongs to the complex I 75 kDa subunit family.
   
  0.871
atpA
F1-ATP synthase alpha subunit (atpA); Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. Belongs to the ATPase alpha/beta chains family.
   
 0.859
petA
Cytochrome B6-F complex iron-sulfur subunit (petA); Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
   
  0.829
petA-2
Cytochrome B6-F complex iron-sulfur subunit (petA); Psort: bacterial cytoplasm --- Certainty= 0.295(Affirmative); split domain; COG0723 QcrA Rieske Fe-S protein.
   
  0.829
lspA
Lipoprotein signal peptidase (lspA); This protein specifically catalyzes the removal of signal peptides from prolipoproteins; Belongs to the peptidase A8 family.
  
    0.824
atpH
ATP synthase delta chain (atpH); F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family.
   
  0.811
nuoI
NADH dehydrogenase I chain I (nuoI); NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
  
   0.798
Your Current Organism:
Anaplasma marginale
NCBI taxonomy Id: 320483
Other names: A. marginale str. Florida, Anaplasma marginale str. Florida, Anaplasma marginale strain Florida
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