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
ADU48496.1COGs: COG1290 Cytochrome b subunit of the bc complex; InterPro IPR005797; KEGG: kse:Ksed_16210 cytochrome b subunit of the bc complex; PFAM: Cytochrome b/b6 domain; SPTR: Cytochrome B subunit; PFAM: Cytochrome b(N-terminal)/b6/petB. (580 aa)    
Predicted Functional Partners:
ADU48493.1
Cytochrome-c oxidase; COGs: COG1845 Heme/copper-type cytochrome/quinol oxidase subunit 3; InterPro IPR000298; KEGG: kse:Ksed_16180 heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: cytochrome c oxidase subunit III; PRIAM: Cytochrome-c oxidase; SPTR: Heme/copper-type cytochrome/quinol oxidase, subunit 3; manually curated; PFAM: Cytochrome c oxidase subunit III.
 
 0.999
ADU48494.1
Menaquinol-cytochrome c reductase cytochrome c1 subunit precursor; InterPro IPR003088: IPR009152: IPR009056; KEGG: kse:Ksed_16190 cytochrome c, mono- and diheme variants family; PFAM: cytochrome c class I; SPTR: Cytochrome C heme-binding subunit; PFAM: Cytochrome c.
 
 0.999
ADU48495.1
Menaquinol-cytochrome c reductase iron-sulfur subunit precursor; COGs: COG0723 Rieske Fe-S protein; InterPro IPR017941; KEGG: kse:Ksed_16200 Rieske Fe-S protein; PFAM: Rieske [2Fe-2S] iron-sulphur domain; SPTR: Rieske iron-sulphur component of ubiQ-cytB reductase; PFAM: Rieske [2Fe-2S] domain.
 
 0.999
ADU48499.1
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.
 
 0.998
ADU48500.1
COGs: COG1622 Heme/copper-type cytochrome/quinol oxidase subunit 2; InterPro IPR002429: IPR014222: IPR001505; KEGG: cfl:Cfla_2082 cytochrome c oxidase, subunit II; PFAM: cytochrome c oxidase subunit II; SPTR: Cytochrome c oxidase subunit 2; TIGRFAM: cytochrome c oxidase, subunit II; PFAM: Cytochrome C oxidase subunit II, periplasmic domain; TIGRFAM: cytochrome c oxidase, subunit II.
 
 0.998
ADU48498.1
Hypothetical protein; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family.
 
 0.996
ADU46997.1
FAD dependent oxidoreductase; COGs: COG0665 Glycine/D-amino acid oxidase (deaminating); InterPro IPR017941: IPR006076; KEGG: nda:Ndas_1353 FAD dependent oxidoreductase; PFAM: FAD dependent oxidoreductase; Rieske [2Fe-2S] iron-sulphur domain; SPTR: FAD dependent oxidoreductase; PFAM: Rieske [2Fe-2S] domain; FAD dependent oxidoreductase.
  
 0.987
ADU47242.1
COGs: COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M); InterPro IPR003918: IPR001750: IPR010227; KEGG: cfl:Cfla_2704 proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I); SPTR: NADH dehydrogenase subunit 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.
   
 0.961
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.
   
 0.956
nuoH-2
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.
   
 0.956
Your Current Organism:
Intrasporangium calvum
NCBI taxonomy Id: 710696
Other names: I. calvum DSM 43043, Intrasporangium calvum DSM 43043, Intrasporangium calvum IFO 12989, Intrasporangium calvum NBRC 12989, Intrasporangium calvum str. DSM 43043, Intrasporangium calvum strain DSM 43043
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