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
Rmag_0040TIGRFAM: cytochrome c oxidase, cbb3-type, subunit II; PFAM: cytochrome C oxidase, mono-heme subunit/FixO; KEGG: tcx:Tcr_1964 cytochrome c oxidase, cbb3-type, subunit II. (243 aa)    
Predicted Functional Partners:
Rmag_0039
TIGRFAM: cytochrome c oxidase, cbb3-type, subunit I; PFAM: cytochrome c oxidase, subunit I; KEGG: tcx:Tcr_1965 cytochrome c oxidase, cbb3-type, subunit I; Belongs to the heme-copper respiratory oxidase family.
 0.999
Rmag_0041
Cytochrome c oxidase, cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex.
 
 0.999
Rmag_0034
Cytochrome-c oxidase; 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).
  
 0.988
Rmag_0075
PFAM: 4Fe-4S ferredoxin, iron-sulfur binding domain protein; KEGG: tcx:Tcr_1962 4Fe-4S ferredoxin, iron-sulfur binding.
 
  
 0.975
Rmag_0035
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.
    
 0.926
Rmag_0037
PFAM: cytochrome c oxidase, subunit III; KEGG: hch:HCH_00049 cytochrome-c oxidase, subnunit III.
    
  0.926
cyoE
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.
     
 0.902
Rmag_0808
Monoheme cytochrome SoxX (sulfur oxidation); KEGG: tbd:Tbd_0567 sulfur oxidation protein SoxX.
  
 
 0.746
Rmag_0974
KEGG: tcx:Tcr_0203 hypothetical protein.
 
     0.725
Rmag_0076
KEGG: tcx:Tcr_1961 hypothetical protein.
 
 
 0.698
Your Current Organism:
Ruthia magnifica
NCBI taxonomy Id: 413404
Other names: C. Ruthia magnifica str. Cm (Calyptogena magnifica), Candidatus Ruthia magnifica str. Cm (Calyptogena magnifica), Candidatus Ruthia magnifica strain Cm (Calyptogena magnifica), Ruthia magnifica str. Cm (Calyptogena magnifica)
Server load: low (36%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.