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A0A0E0N5W9 A0A0E0N5W9 A0A0E0N7V8 A0A0E0N7V8 A0A0E0NB78 A0A0E0NB78 A0A0E0NGV4 A0A0E0NGV4 A0A0E0NKW0 A0A0E0NKW0 A0A0E0NL22 A0A0E0NL22 A0A0E0NLC2 A0A0E0NLC2 A0A0E0NPX2 A0A0E0NPX2 A0A0E0P210 A0A0E0P210 A0A0E0P727 A0A0E0P727 A0A0E0P8Y8 A0A0E0P8Y8 A0A0E0PC43 A0A0E0PC43 A0A0E0PGC6 A0A0E0PGC6 A0A0E0PL34 A0A0E0PL34 A0A0E0PQZ3 A0A0E0PQZ3 A0A0E0PR53 A0A0E0PR53 A0A0E0PX40 A0A0E0PX40 A0A0E0Q416 A0A0E0Q416 A0A0E0Q7E9 A0A0E0Q7E9 A0A0E0Q8E7 A0A0E0Q8E7 A0A0E0QA98 A0A0E0QA98 A0A0E0QGN7 A0A0E0QGN7 A0A0E0QJF7 A0A0E0QJF7 A0A0E0QME4 A0A0E0QME4 A0A0E0QN99 A0A0E0QN99 A0A0E0QRX8 A0A0E0QRX8 A0A0E0REQ6 A0A0E0REQ6 A0A0E0RF34 A0A0E0RF34 A0A0E0RGJ1 A0A0E0RGJ1 psaJ psaJ ndhK ndhK ndhC ndhC psaI psaI ndhD ndhD ndhE ndhE ndhG ndhG ndhB ndhB psaB psaB psaA psaA
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:
A0A0E0N5W9Uncharacterized protein. (211 aa)
A0A0E0N7V8Uncharacterized protein. (164 aa)
A0A0E0NB78Chlorophyll a-b binding protein, chloroplastic; The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated; Belongs to the light-harvesting chlorophyll a/b-binding (LHC) protein family. (269 aa)
A0A0E0NGV4Uncharacterized protein. (225 aa)
A0A0E0NKW0Uncharacterized protein. (170 aa)
A0A0E0NL22Peptidylprolyl isomerase. (205 aa)
A0A0E0NLC2Chlorophyll a-b binding protein, chloroplastic; The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated; Belongs to the light-harvesting chlorophyll a/b-binding (LHC) protein family. (261 aa)
A0A0E0NPX2Uncharacterized protein. (359 aa)
A0A0E0P210Uncharacterized protein. (236 aa)
A0A0E0P727Complex1_30kDa domain-containing protein. (101 aa)
A0A0E0P8Y8Uncharacterized protein. (142 aa)
A0A0E0PC43Uncharacterized protein. (220 aa)
A0A0E0PGC6Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. (250 aa)
A0A0E0PL34Uncharacterized protein. (158 aa)
A0A0E0PQZ32Fe-2S ferredoxin-type domain-containing protein. (199 aa)
A0A0E0PR53Uncharacterized protein. (142 aa)
A0A0E0PX40Chlorophyll a-b binding protein, chloroplastic; The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated; Belongs to the light-harvesting chlorophyll a/b-binding (LHC) protein family. (268 aa)
A0A0E0Q416Uncharacterized protein. (133 aa)
A0A0E0Q7E9Uncharacterized protein. (108 aa)
A0A0E0Q8E72Fe-2S ferredoxin-type domain-containing protein. (210 aa)
A0A0E0QA98Chlorophyll a-b binding protein, chloroplastic; The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated; Belongs to the light-harvesting chlorophyll a/b-binding (LHC) protein family. (263 aa)
A0A0E0QGN7Uncharacterized protein. (509 aa)
A0A0E0QJF7Chlorophyll a-b binding protein, chloroplastic; The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated; Belongs to the light-harvesting chlorophyll a/b-binding (LHC) protein family. (244 aa)
A0A0E0QME4Uncharacterized protein. (203 aa)
A0A0E0QN99Uncharacterized protein. (257 aa)
A0A0E0QRX8Chlorophyll a-b binding protein, chloroplastic; The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated; Belongs to the light-harvesting chlorophyll a/b-binding (LHC) protein family. (414 aa)
A0A0E0REQ6Uncharacterized protein. (207 aa)
A0A0E0RF34Complex1_49kDa domain-containing protein. (72 aa)
A0A0E0RGJ1PsaL domain-containing protein. (201 aa)
psaJPhotosystem I reaction center subunit IX; May help in the organization of the PsaE and PsaF subunits. Belongs to the PsaJ family. (44 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. (253 aa)
ndhCNAD(P)H-quinone oxidoreductase subunit 3, 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. (120 aa)
psaIPhotosystem I reaction center subunit VIII; May help in the organization of the PsaL subunit. Belongs to the PsaI family. (36 aa)
ndhDNAD(P)H-quinone oxidoreductase chain 4, chloroplastic. (500 aa)
ndhENAD(P)H-quinone oxidoreductase subunit 4L, 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. (101 aa)
ndhGNAD(P)H-quinone oxidoreductase subunit 6, 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. (176 aa)
ndhBNAD(P)H-quinone oxidoreductase subunit 2, 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)
psaBPhotosystem I P700 chlorophyll a apoprotein A2; PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin. (734 aa)
psaAPhotosystem I P700 chlorophyll a apoprotein A1; PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin. (750 aa)
Your Current Organism:
Oryza rufipogon
NCBI taxonomy Id: 4529
Other names: O. rufipogon, Oryza rufipogon Griff., common wild rice, red rice
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