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rpl14 rpl14 psbJ psbJ rps8 rps8 rpl16 rpl16 rpl22 rpl22 ndhF ndhF rpl32 rpl32 ccsA ccsA ndhA ndhA ndhH ndhH ycf1 ycf1 psbA psbA matK matK atpF atpF atpH atpH rpoC2 rpoC2 rpoB rpoB psbZ psbZ psaA psaA ndhC ndhC rbcL rbcL accD accD cemA cemA
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
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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
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textmining
co-expression
protein homology
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rpl1450S ribosomal protein L14, chloroplastic; Binds to 23S rRNA. (122 aa)
psbJPhotosystem II reaction center protein J; One of the components of the core complex 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. (40 aa)
rps830S ribosomal protein S8, chloroplastic; One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit. (134 aa)
rpl1650S ribosomal protein L16, chloroplastic; Belongs to the universal ribosomal protein uL16 family. (135 aa)
rpl2250S ribosomal protein L22, chloroplastic; The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome; Belongs to the universal ribosomal protein uL22 family. (141 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. (742 aa)
rpl3250S ribosomal protein L32, chloroplastic. (52 aa)
ccsACytochrome c biogenesis protein CcsA; Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment. (322 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. (363 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)
ycf1Protein TIC 214; Involved in protein precursor import into chloroplasts. May be part of an intermediate translocation complex acting as a protein- conducting channel at the inner envelope. (1871 aa)
psbAPhotosystem II protein D1; Photosystem II (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. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. (353 aa)
matKMaturase K; Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns. Belongs to the intron maturase 2 family. MatK subfamily. (506 aa)
atpFATP synthase subunit b, chloroplastic; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). (184 aa)
atpHATP synthase subunit c, 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. (81 aa)
rpoC2DNA-directed RNA polymerase subunit beta'; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. (1368 aa)
rpoBDNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. (1070 aa)
psbZPhotosystem II reaction center protein Z; Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna; Belongs to the PsbZ family. (62 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)
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)
rbcLRibulose bisphosphate carboxylase large chain; RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. Belongs to the RuBisCO large chain family. Type I subfamily. (475 aa)
accDAcetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic; Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA. (491 aa)
cemAEnvelope membrane protein, chloroplastic; May be involved in proton extrusion. Indirectly promotes efficient inorganic carbon uptake into chloroplasts. Belongs to the CemA family. (229 aa)
Your Current Organism:
Prunus persica
NCBI taxonomy Id: 3760
Other names: Amygdalus persica, P. persica, Persica vulgaris, Persica vulgaris Mill., Prunus persica (L.) Batsch, Prunus persica var. densa, Prunus persica var. densa Makino, peach
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