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
Xcel_2008PFAM: cytochrome c oxidase subunit III; KEGG: amc:MADE_03910 cytochrome o ubiquinol oxidase subunit III (ubiquinol oxidase chain C). (218 aa)    
Predicted Functional Partners:
Xcel_2009
PFAM: cytochrome c class I; KEGG: tbd:Tbd_2545 putative cytochrome c.
 
 
 0.999
Xcel_2010
PFAM: Rieske [2Fe-2S] domain protein; KEGG: vei:Veis_4950 Rieske (2Fe-2S) domain protein.
 
 
 0.999
Xcel_2011
PFAM: Cytochrome b/b6 domain; KEGG: sus:Acid_6208 cytochrome b/b6 domain- containing protein.
 
 
 0.999
Xcel_2014
Hypothetical protein; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family.
 
 
 0.999
Xcel_2015
Cytochrome 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.
 0.999
Xcel_2016
TIGRFAM: cytochrome c oxidase, subunit II; PFAM: cytochrome c oxidase subunit II; KEGG: pfl:PFL_0061 cytochrome c oxidase, subunit II.
 
 0.999
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
atpB
ATP synthase F0, A subunit; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
  
 
 0.987
Xcel_0481
KEGG: dds:Ddes_1656 proton-translocating NADH- quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I).
  
 
 0.983
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.
  
 
 0.982
Your Current Organism:
Xylanimonas cellulosilytica
NCBI taxonomy Id: 446471
Other names: X. cellulosilytica DSM 15894, Xylanimonas cellulosilytica DSM 15894, Xylanimonas cellulosilytica str. DSM 15894, Xylanimonas cellulosilytica strain DSM 15894
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