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
Noca_1622PFAM: cytochrome c oxidase, subunit II; KEGG: tdn:Tmden_0103 putative cytochrome c oxidase subunit II. (196 aa)    
Predicted Functional Partners:
Noca_1623
PFAM: cytochrome c oxidase, subunit I; KEGG: tdn:Tmden_0104 cytochrome c oxidase, subunit I.
 
 0.999
Noca_3134
PFAM: cytochrome c oxidase, subunit III; KEGG: sco:SCO2151 cytochrome c oxidase subunit III.
  
 0.998
Noca_3140
Cytochrome-c oxidase; 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.
  
 0.995
ctaB
Protoheme IX farnesyltransferase; 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.
  
 
 0.975
Noca_3137
PFAM: Cytochrome b/b6, N-terminal domain; KEGG: pac:PPA0710 cytochrome b subunit.
  
 0.950
Noca_2944
PFAM: Cytochrome b/b6, N-terminal domain; KEGG: oih:OB1775 menaquinol-cytochrome-c reductase cytochrome b subunit.
 
 
 0.919
Noca_3141
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).
     
  0.900
nuoH
NADH dehydrogenase subunit H; 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.
   
 
 0.894
Noca_0532
KEGG: rha:RHA1_ro05921 probable NADH dehydrogenase subunit M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I).
   
 
 0.894
Noca_3135
Menaquinol-cytochrome c reductase cytochrome c1 subunit precursor; PFAM: cytochrome c, class I; KEGG: sco:SCO2150 cytochrome C heme-binding subunit.
  
 
 0.881
Your Current Organism:
Nocardioides sp. JS614
NCBI taxonomy Id: 196162
Other names: N. sp. JS614
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