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TIC214 TIC214 rpoC1 rpoC1 rps12 rps12 psaM psaM rps12-2 rps12-2 chlN chlN ndhF ndhF chlL chlL
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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Your Input:
TIC214Protein 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. (1603 aa)
rpoC1DNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Belongs to the RNA polymerase beta' chain family. RpoC1 subfamily. (679 aa)
rps12Ribosomal protein S12; Belongs to the universal ribosomal protein uS12 family. (126 aa)
psaMPhotosystem I reaction center subunit XII. (32 aa)
rps12-230S ribosomal protein S12, chloroplastic; With S4 and S5 plays an important role in translational accuracy. Located at the interface of the 30S and 50S subunits (By similarity). (123 aa)
chlNLight-independent protochlorophyllide reductase subunit N; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex; Belongs to the BchN/ChlN family. (474 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). (720 aa)
chlLLight-independent protochlorophyllide reductase iron-sulfur ATP-binding protein; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP. Belongs to the NifH/BchL/ChlL family. (295 aa)
Your Current Organism:
Physcomitrella patens
NCBI taxonomy Id: 3218
Other names: P. patens, Physcomitrella patens (Hedw.) Bruch & Schimp., Physcomitrella patens subsp. patens, Physcomitrium patens, Physcomitrium patens (Hedw.) Mitt.
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