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.
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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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[Homology]
Score
sync_1651Identified by match to protein family HMM PF00675; match to protein family HMM PF05193; Belongs to the peptidase M16 family. (466 aa)    
Predicted Functional Partners:
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. Belongs to the Rieske iron-sulfur protein family.
  
 0.914
sync_1650
Peptidase M16B family, nonpeptidase homolog; Identified by match to protein family HMM PF05193.
 
    
0.851
atpA
ATP synthase F1, alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. Belongs to the ATPase alpha/beta chains family.
   
 0.815
atpH
ATP synthase F1, delta subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family.
   
 0.791
sync_0156
Polyketide synthase, putative; Identified by match to protein family HMM PF00106; match to protein family HMM PF00107; match to protein family HMM PF00109; match to protein family HMM PF00550; match to protein family HMM PF01073; match to protein family HMM PF01370; match to protein family HMM PF02801; match to protein family HMM PF07993; match to protein family HMM TIGR01746.
  
 
 0.784
petB
Cytochrome b6; 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.
    
 0.729
sync_1798
Transporter, stomatin/podocin/band 7/nephrosis.2/SPFH (Stomatin) family protein; Identified by match to protein family HMM PF01145.
 
 0.717
ndhH
NADH dehydrogenase I chain 7 (or 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.
   
 
 0.705
ndhJ
NADH dehydrogenase I chain J; 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.
   
 
 0.677
sync_1335
Conserved hypothetical protein.
   
 
 0.670
Your Current Organism:
Synechococcus sp. CC9311
NCBI taxonomy Id: 64471
Other names: S. sp. CC9311
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