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
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
Tpau_2942Cytochrome c oxidase, subunit I; 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. (581 aa)    
Predicted Functional Partners:
Tpau_1537
PFAM: cytochrome c oxidase subunit II; KEGG: nfa:nfa17080 putative cytochrome c oxidase subunit II.
 
 0.999
Tpau_2692
KEGG: mjl:Mjls_3302 cytochrome c oxidase, subunit III; PFAM: cytochrome c oxidase subunit III.
 0.999
Tpau_1538
Cytochrome-c oxidase; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family.
 
 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.
 
 0.998
Tpau_2695
PFAM: Cytochrome b/b6 domain; KEGG: rer:RER_35980 menaquinol-cytochrome c reductase cytochrome b subunit.
 
 
 0.998
Tpau_2694
Rieske (2Fe-2S) iron-sulfur domain protein; PFAM: Rieske [2Fe-2S] iron-sulphur domain; KEGG: mab:MAB_1967c ubiquinol-cytochrome c reductase iron-sulfur subunit (Rieske iron-sulfur protein).
 
 0.993
Tpau_2693
PFAM: cytochrome c class I; KEGG: rop:ROP_08590 menaquinol-cytochrome c reductase cytochrome c subunit.
 
 
 0.989
Tpau_3180
KEGG: nfa:nfa26560 NADH dehydrogenase subunit M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I).
  
 
 0.973
nuoH
NADH dehydrogenase (quinone); 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.
  
 
 0.972
nuoA
NADH-ubiquinone/plastoquinone oxidoreductase chain 3; 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 a menaquinone. 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 subunit 3 family.
   
 
 0.967
Your Current Organism:
Tsukamurella paurometabola
NCBI taxonomy Id: 521096
Other names: T. paurometabola DSM 20162, Tsukamurella paurometabola ATCC 8368, Tsukamurella paurometabola DSM 20162, Tsukamurella paurometabola str. DSM 20162, Tsukamurella paurometabola strain DSM 20162
Server load: low (28%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.