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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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Textmining
[Homology]
Score
AFY36113.1Protein of unknown function DUF185; PFAM: Uncharacterized ACR, COG1565; COGs: COG1565 conserved hypothetical protein; InterPro IPR003788; KEGG: npu:Npun_F4975 hypothetical protein; PFAM: Protein of unknown function DUF185; SPTR: Putative uncharacterized protein. (412 aa)    
Predicted Functional Partners:
ndhH
NADH dehydrogenase subunit D; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
 
 
 0.931
ndhK
NAD(P)H-quinone oxidoreductase subunit K; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration; Belongs to the complex I 20 kDa subunit family.
 
 
 0.881
ndhJ
NADH dehydrogenase subunit C; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
 
 
 0.862
ndhA
NADH dehydrogenase subunit H; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
  
  
 0.789
ndhC
NADH dehydrogenase subunit A; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
 
  
  0.746
ndhI
NAD(P)H-quinone oxidoreductase subunit I; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient; Belongs to the complex I 23 kDa subunit family.
  
  
 0.716
AFY30918.1
4Fe-4S ferredoxin iron-sulfur binding domain-containing protein; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
     
 0.654
AFY32349.1
NIL domain-containing protein; PFAM: NIL domain; InterPro IPR018449:IPR001450; KEGG: npu:Npun_F4770 4Fe-4S ferredoxin iron-sulfur binding domain-containing protein; PFAM: NIL domain; 4Fe-4S binding domain; SMART: NIL domain; SPTR: 4Fe-4S ferredoxin, iron-sulfur binding domain protein.
     
 0.654
AFY34026.1
PFAM: Squalene/phytoene synthase; COGs: COG1562 Phytoene/squalene synthetase; InterPro IPR002060; KEGG: ava:Ava_4794 phytoene synthase; PFAM: Squalene/phytoene synthase; PRIAM: Phytoene synthase; SPTR: Phytoene synthase; manually curated.
     
 0.644
AFY34554.1
Farnesyl-diphosphate farnesyltransferase; PFAM: Squalene/phytoene synthase; COGs: COG1562 Phytoene/squalene synthetase; InterPro IPR002060; KEGG: npu:Npun_R2917 squalene/phytoene synthase; PFAM: Squalene/phytoene synthase; SPTR: Squalene/phytoene synthase.
     
 0.644
Your Current Organism:
Calothrix sp. PCC7507
NCBI taxonomy Id: 99598
Other names: C. sp. PCC 7507, Calothrix sp. PCC 7507
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