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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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Co-expression
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[Homology]
Score
Isop_1950Cytochrome b/b6 domain protein; COGs: COG1290 Cytochrome b subunit of the bc complex; InterPro IPR005797: IPR009056; KEGG: gau:GAU_0696 putative menaquinol-cytochrome c reductase cytochrome b/c subunit; PFAM: Cytochrome b/b6 domain; SPTR: Putative menaquinol-cytochrome c reductase cytochrome b/c subunit; PFAM: Cytochrome c; Cytochrome b(C-terminal)/b6/petD. (638 aa)    
Predicted Functional Partners:
Isop_1951
InterPro IPR017941; KEGG: plm:Plim_0423 Rieske (2Fe-2S) domain protein; PFAM: Rieske [2Fe-2S] iron-sulphur domain; SPTR: Menaquinol-cytochrome c reductase, iron-sulfur subunit; PFAM: Rieske [2Fe-2S] domain.
 
 0.999
Isop_0869
COGs: COG0843 Heme/copper-type cytochrome/quinol oxidase subunit 1; InterPro IPR000883; KEGG: psl:Psta_2929 cytochrome-c oxidase; PFAM: cytochrome c oxidase subunit I; SPTR: Cytochrome c oxidase subunit I; PFAM: Cytochrome C and Quinol oxidase polypeptide I; TIGRFAM: cytochrome c oxidase, subunit I; Belongs to the heme-copper respiratory oxidase family.
 
 
 0.985
Isop_0868
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).
 
 
 0.983
Isop_0872
Cytochrome-c oxidase; COGs: COG1845 Heme/copper-type cytochrome/quinol oxidase subunit 3; InterPro IPR000298: IPR020606; KEGG: hwa:HQ2352A cytochrome-C-like terminal oxidase, subunit III; PFAM: cytochrome c oxidase subunit III; PRIAM: Cytochrome-c oxidase; SPTR: Cytochrome-c-like terminal oxidase, subunit III; PFAM: Cytochrome c oxidase subunit III.
 
 
 0.983
Isop_3640
Proton-translocating NADH-quinone oxidoreductase, chain M; COGs: COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M); InterPro IPR010227: IPR001750: IPR003918; KEGG: psl:Psta_0731 proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I); SPTR: Proton-translocating NADH-quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH-Ubiquinone/plastoquinone (complex I), various chains; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M.
  
 
 0.967
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.
  
 
 0.967
nuoN
Proton-translocating NADH-quinone oxidoreductase, chain N; 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; Belongs to the complex I subunit 2 family.
  
 
 0.938
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 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; Belongs to the complex I subunit 3 family.
  
 
 0.933
nuoK
NADH-ubiquinone oxidoreductase chain 4L; 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; Belongs to the complex I subunit 4L family.
  
 
 0.912
Isop_0635
4Fe-4S ferredoxin iron-sulfur binding domain protein; COGs: COG0348 Polyferredoxin; InterPro IPR017896: IPR017900; KEGG: hoh:Hoch_0561 4Fe-4S ferredoxin iron-sulfur binding domain protein; SPTR: 4Fe-4S ferredoxin iron-sulfur binding domain protein; PFAM: 4Fe-4S binding domain.
 
 
 0.900
Your Current Organism:
Isosphaera pallida
NCBI taxonomy Id: 575540
Other names: I. pallida ATCC 43644, Isosphaera pallida ATCC 43644, Isosphaera pallida DSM 9630, Isosphaera pallida IS1B, Isosphaera pallida str. ATCC 43644, Isosphaera pallida strain ATCC 43644
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