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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
coxCCytochrome C oxidase, subunit III (coxC); Psort: bacterial inner membrane --- Certainty= 0.370(Affirmative); COG1845 CyoC heme/copper-type cytochrome/quinol oxidase, subunit 3. (272 aa)    
Predicted Functional Partners:
petB
Cytochrome B (petB); 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.
 
 
 0.999
coxB
Cytochrome c oxidase subunit II (coxB); 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).
 
 0.999
coxA
Cytochrome c oxidase subunit I (coxA); Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.
 
 0.999
atpB
ATP synthase A chain (atpB); Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
  
 
 0.998
nuoH
NADH dehydrogenase I chain H (nuoH); 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. This subunit may bind ubiquinone.
  
 
 0.997
ctaB
Cytochrome c oxidase assembly factor (ctaB); Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
 
 
 0.997
nuoM
NADH dehydrogenase I chain M (nuoM); Psort: bacterial inner membrane --- Certainty= 0.711(Affirmative); COG1008 NuoM NADH:ubiquinone oxidoreductase subunit 4 (chain M).
  
 
 0.996
AMF_834
Called by Glimmer 2; Conserved hypothetical protein called by Glimmer 2; psort: bacterial inner membrane --- Certainty= 0.592(Affirmative); COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1.
  
 0.995
petC
Cytochrome c1, heme protein precursor; Psort: bacterial inner membrane --- Certainty= 0.317(Affirmative); COG2857 CYT1 cytochrome c1.
  
 
 0.994
cycM
Cytochrome C (cycM); Psort: bacterial inner membrane --- Certainty= 0.412(Affirmative); COG3303 NrfA formate-dependent nitrite reductase, periplasmic cytochrome c552 subunit.
 
 0.972
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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