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
AFZ15393.1PFAM: Complex I intermediate-associated protein 30 (CIA30); NmrA-like family; COGs: COG0702 nucleoside-diphosphate-sugar epimerase; InterPro IPR001509:IPR013857; KEGG: npu:Npun_F6553 NADH:ubiquinone oxidoreductase complex I intermediate-associated protein 30; PFAM: NADH:ubiquinone oxidoreductase intermediate-associated protein 30; NAD-dependent epimerase/dehydratase; SPTR: Putative uncharacterized protein. (493 aa)    
Predicted Functional Partners:
AFZ12486.1
Amino acid adenylation domain protein; PFAM: Male sterility protein; Phosphopantetheine attachment site; Methyltransferase domain; AMP-binding enzyme; Condensation domain; PilZ domain; TIGRFAM: amino acid adenylation domain; thioester reductase domain; COGs: COG1020 Non-ribosomal peptide synthetase modules and related protein; InterProIPR020806:IPR000873:IPR013217:IPR006163:IPR 001242:IPR009875:IPR013120:IPR010071:IPR010080; KEGG: npu:Npun_CR072 amino acid adenylation domain-containing protein; PFAM: AMP-dependent synthetase/ligase; Methyltransferase type 12; Phosphopantetheine-binding [...]
  
 0.958
AFZ11265.1
Amino acid adenylation domain protein; PFAM: Phosphopantetheine attachment site; Nonribosomal peptide synthase; AMP-binding enzyme; Condensation domain; TIGRFAM: amino acid adenylation domain; COGs: COG1020 Non-ribosomal peptide synthetase modules and related protein; InterProIPR020806:IPR010071:IPR000873:IPR006163:IPR 001242:IPR013624; KEGG: cyt:cce_3073 peptide synthetase; PFAM: Condensation domain; AMP-dependent synthetase/ligase; Phosphopantetheine-binding; Non-ribosomal peptide synthetase; PRIAM: Long-chain-fatty-acid--[acyl-carrier-protein] ligase., Glutamate racemase; SMART: Pol [...]
   
 0.940
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.
   
 0.933
ndhH
NAD(P)H-quinone oxidoreductase 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. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
   
 0.911
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.
   
 0.902
AFZ14932.1
Hypothetical protein; PFAM: Respiratory-chain NADH dehydrogenase 24 Kd subunit; KEGG: ava:Ava_4529 hypothetical protein; SPTR: Putative uncharacterized protein.
   
 0.825
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.
   
 0.787
ndhA
NADH dehydrogenase (quinone); 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.
    
 0.783
petC
Cytochrome b6-f complex iron-sulfur subunit; Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
  
 
 0.783
ndhB
NAD(P)H-quinone oxidoreductase subunit 2; 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.
   
 0.756
Your Current Organism:
Crinalium epipsammum
NCBI taxonomy Id: 1173022
Other names: C. epipsammum PCC 9333, Crinalium epipsammum PCC 9333, Crinalium sp. PCC 9333
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