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atpA atpA matK matK ndhF ndhF ndhB1 ndhB1 PetB PetB ndhH ndhH ndhA ndhA ndhD ndhD petB petB clpP clpP rpl20 rpl20 psbF psbF psaI psaI ndhK ndhK atpF atpF rps16 rps16
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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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
atpAATP synthase subunit alpha, chloroplastic; 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. (507 aa)
matKMaturase K; Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns. (515 aa)
ndhFNAD(P)H-quinone oxidoreductase subunit 5, chloroplastic; NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory 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 (By similarity). (738 aa)
ndhB1NAD(P)H-quinone oxidoreductase subunit 2 A, chloroplastic; NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory 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. (510 aa)
PetBCYTB_NTER domain-containing protein. (232 aa)
ndhHNAD(P)H-quinone oxidoreductase subunit H, chloroplastic; NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory 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. (393 aa)
ndhANAD(P)H-quinone oxidoreductase subunit 1, chloroplastic; NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory 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. (362 aa)
ndhDNAD(P)H-quinone oxidoreductase chain 4, chloroplastic. (500 aa)
petBCytochrome 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. (215 aa)
clpPATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. (216 aa)
rpl2050S ribosomal protein L20, chloroplastic; Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit. (119 aa)
psbFCytochrome b559 subunit beta; This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. Belongs to the PsbE/PsbF family. (39 aa)
psaIPhotosystem I reaction center subunit VIII; May help in the organization of the PsaL subunit. Belongs to the PsaI family. (36 aa)
ndhKNAD(P)H-quinone oxidoreductase subunit K, chloroplastic; NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory 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 20 kDa subunit family. (227 aa)
atpFATP synthase subunit b, chloroplastic; 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. (183 aa)
rps1630S ribosomal protein S16, chloroplastic. (85 aa)
Your Current Organism:
Sorghum bicolor
NCBI taxonomy Id: 4558
Other names: Andropogon sorghum, Andropogon sorghum (L.) Brot., S. bicolor, Sorghum bicolor (L.) Moench, Sorghum bicolor subsp. bicolor, Sorghum nervosum, Sorghum nervosum Besser ex Schult., Sorghum saccharatum, Sorghum saccharatum (L.) Moench, Sorghum vulgare, Sorghum vulgare Pers., broomcorn, milo, sorghum
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