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
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Co-expression
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[Homology]
Score
petAUbiquinol-cytochrome c reductase, iron-sulfur subunit; 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. (189 aa)    
Predicted Functional Partners:
petB
Ubiquinol-cytochrome c reductase, cytochrome b; 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
petC
Ubiquinol-cytochrome c reductase, cytochrome c1; Identified by similarity to SP:P23135; match to protein family HMM PF02167.
 
 0.999
cycM
Cytochrome C, membrane-bound; Identified by similarity to SP:P30323; match to protein family HMM PF00034.
 
 0.991
nuoD
NADH dehydrogenase I, D subunit; 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 49 kDa subunit family.
   
 0.987
nuoI
NADH dehydrogenase I, I subunit; 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.
  
 0.987
nuoE
NADH dehydrogenase I, E subunit; Identified by similarity to GB:CAA71011.1; match to protein family HMM PF01257; match to protein family HMM TIGR01958.
   
 0.986
APH_0101
Peptidase, M16 family; Identified by match to protein family HMM PF00675; match to protein family HMM PF05193; Belongs to the peptidase M16 family.
 
 
 0.985
APH_0019
Cytochrome c oxidase, subunit III; Identified by match to protein family HMM PF00510.
  
 0.983
APH_1084
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).
  
 0.977
APH_1295
Conserved domain protein.
  
 
 0.968
Your Current Organism:
Anaplasma phagocytophilum
NCBI taxonomy Id: 212042
Other names: A. phagocytophilum str. HZ, Anaplasma phagocytophilum HZ, Anaplasma phagocytophilum str. HZ
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