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_3141Cytochrome 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). (324 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.
 
 0.999
Noca_3139
Conserved hypothetical protein; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family.
 
 0.999
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.
 
 0.999
Noca_3137
PFAM: Cytochrome b/b6, N-terminal domain; KEGG: pac:PPA0710 cytochrome b subunit.
 
 0.998
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.
 
 
 0.997
Noca_2944
PFAM: Cytochrome b/b6, N-terminal domain; KEGG: oih:OB1775 menaquinol-cytochrome-c reductase cytochrome b subunit.
 
 
 0.997
Noca_3135
Menaquinol-cytochrome c reductase cytochrome c1 subunit precursor; PFAM: cytochrome c, class I; KEGG: sco:SCO2150 cytochrome C heme-binding subunit.
 
 
 0.996
Noca_3136
PFAM: Rieske [2Fe-2S] domain protein; KEGG: pac:PPA0711 ubiquinol-cytochrome c reductase iron-sulfur subunit.
 
 
 0.996
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).
  
 
 0.911
Your Current Organism:
Nocardioides sp. JS614
NCBI taxonomy Id: 196162
Other names: N. sp. JS614
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