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
AFZ55054.1beta-Ig-H3/fasciclin; PFAM: Fasciclin domain; COGs: COG2335 Secreted and surface protein containing fasciclin-like repeats; InterPro IPR000782; KEGG: cyc:PCC7424_1101 beta-Ig-H3/fasciclin; PFAM: FAS1 domain; SMART: FAS1 domain; SPTR: Beta-Ig-H3/fasciclin. (133 aa)    
Predicted Functional Partners:
AFZ55053.1
PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein; InterPro IPR010220; KEGG: cyt:cce_0605 protein involved in constitutive low affinity CO2 uptake; PFAM: CO2 hydration; SPTR: Protein involved in constitutive low affinity CO2 uptake; TIGRFAM: CO2 hydration.
   
 
 0.982
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.
    
 
 0.955
AFZ55052.1
PFAM: NADH-Ubiquinone/plastoquinone (complex I), various chains; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; COGs: COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M); InterPro IPR001750:IPR010227; KEGG: syp:SYNPCC7002_A0173 NAD(P)H-quinone oxidoreductase subunit M; PFAM: NADH:ubiquinone/plastoquinone oxidoreductase; PRIAM: NADH dehydrogenase (quinone); SPTR: NADH dehydrogenase subunit M; TIGRFAM: NADH-quinone oxidoreductase, chain M.
   
 
 0.827
AFZ55051.1
NAD(P)H dehydrogenase, subunit NdhF3 family; PFAM: NADH-Ubiquinone/plastoquinone (complex I), various chains; NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminus; TIGRFAM: NAD(P)H dehydrogenase, subunit NdhF3 family; COGs: COG1009 NADH:ubiquinone oxidoreductase subunit 5 (chain L)/Multisubunit Na+/H+ antiporter MnhA subunit; InterPro IPR001750:IPR010217; KEGG: cyh:Cyan8802_4309 NAD(P)H-quinone oxidoreductase subunit F; PFAM: NADH:ubiquinone/plastoquinone oxidoreductase; PRIAM: NADH dehydrogenase (quinone); SPTR: NAD(P)H dehydrogenase, subunit NdhF3 family; TIGRFAM: NAD(P)H d [...]
   
 
 0.791
AFZ52382.1
PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein; InterPro IPR010220; KEGG: cyc:PCC7424_1376 CO2 hydration protein; PFAM: CO2 hydration; SPTR: CO2 hydration protein; TIGRFAM: CO2 hydration.
    
 
 0.722
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.
    
 
 0.628
ndhL
NAD(P)H-quinone oxidoreductase subunit L; 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.
    
 
 0.589
ndhB
NADH dehydrogenase subunit N; 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.
    
 
 0.587
ndhM
NAD(P)H-quinone oxidoreductase subunit M; 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.
    
   0.578
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.
    
   0.578
Your Current Organism:
Cyanobacterium aponinum
NCBI taxonomy Id: 755178
Other names: C. aponinum PCC 10605, Cyanobacterium aponinum PCC 10605, Cyanobacterium sp. PCC 10605
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