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
Databases
Textmining
[Homology]
Score
AMF_067Called by Glimmer 2; Conserved hypothetical protein called by Glimmer 2; psort: bacterial cytoplasm --- Certainty= 0.386(Affirmative). (106 aa)    
Predicted Functional Partners:
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.
  
   0.892
AMF_054
Called by Glimmer 2; Conserved hypothetical protein called by Glimmer 2; psort: bacterial cytoplasm --- Certainty= 0.013(Affirmative).
  
   0.857
nuoC1
NADH-ubiquinone oxidoreductase subunit (nuoC1); 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; Belongs to the complex I 30 kDa subunit family.
  
   0.823
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.
  
   0.782
AMF_370
Called by Glimmer 2; Conserved hypothetical protein called by Glimmer 2; psort: bacterial inner membrane --- Certainty= 0.130(Affirmative); COG0500 SAM-dependent methyltransferases.
  
  
 0.762
AMF_1013
NADH-ubiquinone oxidoreductase, putative; Psort: bacterial inner membrane --- Certainty= 0.102(Affirmative); COG0702 Predicted nucleoside-diphosphate-sugar epimerases.
   
   0.753
nuoE
NADH dehydrogenase I chain E (nuoE); Psort: bacterial cytoplasm --- Certainty= 0.446(Affirmative); COG1905 NuoE NADH:ubiquinone oxidoreductase 24 kD subunit.
    
   0.749
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.
    
   0.749
cycM
Cytochrome C (cycM); Psort: bacterial inner membrane --- Certainty= 0.412(Affirmative); COG3303 NrfA formate-dependent nitrite reductase, periplasmic cytochrome c552 subunit.
  
 
   0.737
coxC
Cytochrome C oxidase, subunit III (coxC); Psort: bacterial inner membrane --- Certainty= 0.370(Affirmative); COG1845 CyoC heme/copper-type cytochrome/quinol oxidase, subunit 3.
  
   0.633
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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