STRINGSTRING
A0A0E0N1I9 A0A0E0N1I9 A0A0E0N1S4 A0A0E0N1S4 A0A0E0N367 A0A0E0N367 A0A0E0NM91 A0A0E0NM91 A0A0E0NMQ3 A0A0E0NMQ3 A0A0E0NMQ4 A0A0E0NMQ4 A0A0E0NMU0 A0A0E0NMU0 A0A0E0NP75 A0A0E0NP75 A0A0E0NQF8 A0A0E0NQF8 A0A0E0NQH8 A0A0E0NQH8 A0A0E0NQV9 A0A0E0NQV9 A0A0E0NTS1 A0A0E0NTS1 A0A0E0NU67 A0A0E0NU67 A0A0E0NWL8 A0A0E0NWL8 A0A0E0P0E8 A0A0E0P0E8 A0A0E0P1X2 A0A0E0P1X2 A0A0E0P770 A0A0E0P770 A0A0E0PPS3 A0A0E0PPS3 A0A0E0PQE3 A0A0E0PQE3 A0A0E0Q2M0 A0A0E0Q2M0 A0A0E0QAH7 A0A0E0QAH7 A0A0E0QAX6 A0A0E0QAX6 A0A0E0QBU9 A0A0E0QBU9 A0A0E0QBZ3 A0A0E0QBZ3 A0A0E0QN72 A0A0E0QN72 A0A0E0R2V9 A0A0E0R2V9 A0A0E0R2Y7 A0A0E0R2Y7 A0A0E0R4L3 A0A0E0R4L3 A0A0E0RI10 A0A0E0RI10 A0A0E0RI14 A0A0E0RI14 A0A0E0RI22 A0A0E0RI22 ndhJ ndhJ ndhH ndhH ndhF ndhF psaC psaC ndhI ndhI ndhA ndhA
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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
A0A0E0N1I9Uncharacterized protein; Belongs to the peptidase M16 family. (505 aa)
A0A0E0N1S4Oxidored_q6 domain-containing protein; Belongs to the complex I 20 kDa subunit family. (199 aa)
A0A0E0N367Plus3 domain-containing protein. (902 aa)
A0A0E0NM91Uncharacterized protein; Belongs to the cyclin family. (358 aa)
A0A0E0NMQ3Cytochrome c domain-containing protein. (136 aa)
A0A0E0NMQ4Cytochrome c domain-containing protein. (230 aa)
A0A0E0NMU0Epimerase domain-containing protein. (414 aa)
A0A0E0NP75Uncharacterized protein. (109 aa)
A0A0E0NQF8DUF1618 domain-containing protein. (585 aa)
A0A0E0NQH8Uncharacterized protein. (77 aa)
A0A0E0NQV9Uncharacterized protein. (212 aa)
A0A0E0NTS1CHCH domain-containing protein. (110 aa)
A0A0E0NU67Uncharacterized protein. (173 aa)
A0A0E0NWL8Uncharacterized protein. (97 aa)
A0A0E0P0E8Uncharacterized protein; Belongs to the complex I 75 kDa subunit family. (747 aa)
A0A0E0P1X2Uncharacterized protein. (222 aa)
A0A0E0P770L51_S25_CI-B8 domain-containing protein. (99 aa)
A0A0E0PPS3Uncharacterized protein. (303 aa)
A0A0E0PQE3Oxidored_q6 domain-containing protein; Belongs to the complex I 20 kDa subunit family. (335 aa)
A0A0E0Q2M0Uncharacterized protein; Belongs to the complex I LYR family. (113 aa)
A0A0E0QAH7Uncharacterized protein. (159 aa)
A0A0E0QAX6Complex1_49kDa domain-containing protein. (327 aa)
A0A0E0QBU9Uncharacterized protein. (131 aa)
A0A0E0QBZ3NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial; Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. (504 aa)
A0A0E0QN72Uncharacterized protein. (149 aa)
A0A0E0R2V9Uncharacterized protein. (105 aa)
A0A0E0R2Y7NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12; Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. (198 aa)
A0A0E0R4L3UCR_hinge domain-containing protein. (119 aa)
A0A0E0RI10Cytochrome c oxidase subunit 1; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (223 aa)
A0A0E0RI14Uncharacterized protein. (222 aa)
A0A0E0RI22Uncharacterized protein. (81 aa)
ndhJNAD(P)H-quinone oxidoreductase subunit J, 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. (159 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)
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. (734 aa)
psaCPhotosystem I iron-sulfur center; Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. 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, [...] (81 aa)
ndhINAD(P)H-quinone oxidoreductase subunit I, 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 23 kDa subunit family. (180 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)
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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