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monsoon-nlp
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greenbeing-proteins

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evaluation · 338 rows

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evaluation · 338 rows

protein_name stringlengths 8 11	species stringclasses 13 values	sequence stringlengths 5 2.31k	annotation stringlengths 19 1.16k ⌀
85A19_PRUDU	Prunus dulcis	MSPVASKEKPHAVFVPFPAQGHINPMLQLAKLLNYKGFHITFVNTEFNHKRMLESQGSHALDGLPSFRFETIPDGLPPADADARRNLPLVCDSTSKTCLAPFEALLTKLNSSPDSPPVTCIVADGVTSFTLDAAEHFGIPEVLFWTTSACGLMGYVQYYRLIEKGLTPFKDAKDFANGYLDTEIDWIPGMKDVRLKDMPSFIRTTDPNDIMLHYMVSETERSKKASAIILNTFDALEQEVVDALSTLLPPIYSIGPLQLPYSEIPSEYNDLKAIGSNLWAENTECLNWLDTKEPNSVVYVNFGSTTVMTNEQLVEFSWGLANSKKPFLWIIRPGLVAGETAVVPPEFLEETKERGMLASWCPQEQVLLHSAIGGFLTHSGWNSTLEALCGGVPLICWPFFAEQQTNVRYSCTQWGIGIEIDGEVKRDYIDGLVRTLMDGEEGKKMRKKALEWKMLAEDATAPKGSSYLALENVVSKVLLSPRD	Involved in the biosynthesis of the cyanogenic glycoside (R)-prunasin, a precursor of (R)-amygdalin, which at high concentrations is associated with intense bitterness in kernels of almond . Stereo-selectively glucosylates (R)-mandelonitrile to produce (R)-prunasin .
AATC_DAUCA	Daucus carota	MSSVFANVVRAPEDPILGVTVAYHKDQSPNKLNLGVGAYRTEEGKPLVLNVVKKAEQMLVNDQSRVKEYLPIVGLADFNKLSAKLIFGADSPAIQENRVATVQCLSGTGSLRVGGEFLARHYHEHTVYIPQPTWGNHPKIFTLAGLSVKTYRYYNPETRGLDFEGMLEDLGSAPLGAIVLLHACAHNPTGVDPTIEQWEQIRQLMRSKSLLPFFDSAYQGFASGSLDADAQSVRIFVADGGECLAAQSYAKNMGLYGERVGALSIVCKTADVASKVESQLKLVIRPMYSSPPLHGASIVAAILKDGDLYNEWTLELKAMADRIISMRQELFNALQAKGTPGDWSHIVKQIGMFTFTGLNSEQVTFMTNEYHIYLTSDGRISMAGLSSRTVPHLADAIHAAVTGKA	Important for the metabolism of amino acids and Krebs-cycle related organic acids. In plants, it is involved in nitrogen metabolism and in aspects of carbon and energy metabolism. Subcellular locations: Cytoplasm
ABP20_PRUPE	Prunus persica	MPQATMIFPILFTFFLLLSSSNAAVQDFCVADLAAPEGPAGFSCKKPASVKVNDFVFSGLGIAGNTSNIIKAAVTPAFVAQFPGVNGLGISIARLDLAVGGVVPFHTHPGASEVLIVAQGTICAGFVASDNTPYLQTLEKGDIMVFPQGLLHFQVNGGEAPALAFASFGSASPGLQILDFALFKNDLPTEVIAQTTFLDAAQIKKLKGVLGGTN	Probable receptor for the plant growth-promoting hormone auxin. Subcellular locations: Secreted, Extracellular space, Apoplast, Secreted, Cell wall
CEMA_DAUCA	Daucus carota	MSKKKAFTSLLYLASIVFLPWWISLSFNKSLESWVTDWWNTRQSEIFWNDIQEKNIIKNFIELEEILLLEEMIKEDSETHLQNLRIGIHKETLQLIKIHNEDHIHTILHFSTNIICFVILSGYSILGNEELVILNSWAQEFIYNLSDTIKAFWILLLTDFFIGFHSTRGWELMIGFVYKDFGFAHNDQILSSLVCIFPVILDTLFKFWVFRYLNCVSPSLVVIYHSMNE	Contributes to K(+)/H(+) antiport activity by supporting proton efflux to control proton extrusion and homeostasis in chloroplasts in a light-dependent manner to modulate photosynthesis. Prevents excessive induction of non-photochemical quenching (NPQ) under continuous-light conditions. Indirectly promotes efficient inorganic carbon uptake into chloroplasts. Subcellular locations: Plastid, Chloroplast inner membrane
CYB_DAUCA	Daucus carota	MTIRNQRFSLLKQPIFSILNQHLINYPTPSNLNYWAGFGPLAGICLVIQIVTGVFLAMHYTPHVDLAFNSVEHIMRDVEGGWFLRYMHANGASMFLIVVHFHMFRSLYYGSYSSPREFVRCSGVVIFLLMIVTAFIGYVPPWGQMSFWGATVITSLASAIPVVGDTIVTWLWGGFSVGNATLNRFFSLHYLLPFLLVGASILHLGALHQYGSNNPLGINSYTDKIASYPYYYVKDLVGWVAFAIFSSIFIFYAPNVLGHPDNYIPANPMPTPPHIVPEWYFLPIHAILRSIPDKAGGVAAIAPVFICLLALPFLNQSMYVRSAKFRPIYHIIYLLFLADRLLLGWIGCQPVEAPFVTIGQISPFVFFLFFAIMPIPGRVQRENPNYFSENFAFSYPKK	Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis. Subcellular locations: Mitochondrion inner membrane
DRTS_DAUCA	Daucus carota	MASELLANPTNGSGITRPDPQRTYQVVVAATQNMGIGKDGKLPWRLPSDMKFFKDVTMTTSDPLKRNAVIMGRKTWESIPIQHRPLPGRLNVVLTRSGSFDIATVENVVICGSMISALELLAGSPYCVSVEKVFVIGGGQIYREALNAPGCDAVHITEIEEHIECDTFIPLLDESVFQPWYSSFPLVENKIRYCFTTYVRVRNSVAELTSQTNGCSSDSKSDSGNFEIQNFSFLPKTVFEKHEEYLYLGLVENIISNGVTKNDRTRTGTVSIFGCQMRFNLRKSFPLLTTKKVFWRGVVEELLWFISGSTNAKILKEKGVNIWEGNGSREYLDSIGLTDREEGDLGPIYGFQWRHFGARYTDMHADYSGQGFDQLLDVISKIKNNPDDRRIIQSAWNPSDLRLMALPPCHMFAQFYVANGELSCQMYQRSADMGLGVPFNIAAYALLTCMIAHVCDLVPGDFVHSIGDAHVYSNHLSDLFETSFRMLPKTFPVLKINSGEKDIDSFEAADFKLIGYDPHQKIEMKMAV	Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism. Can play two different roles depending on the source of dihydrofolate: de novo synthesis of tetrahydrofolate or recycling of the dihydrofolate released as one of the end products of the TS catalyzed reaction. Catalyzes an essential reaction for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP (By similarity).
EF1A_MANES	Manihot esculenta	MGKEKVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTPKYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQIQEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFGPTGLTTEVKSVEMHHEALQEALPGDNVGFNVKNVAVKDLKRGIVASNSKDDPAKEAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELEKEPKFLKNGDAGFVKMIPTKPMVVETFSAYPPLGRFAVRDMRQTVAVGVIKSVEKKDPSGAKVTKSAAKKGGK	This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. Subcellular locations: Cytoplasm
EP1G_DAUCA	Daucus carota	MARFFPLTLTILLFFIQRIDFCHTLVPANETFKFVNEGELGQYISEYFGDYRPLDPFTSPFQLCFYNQTPTAFTLALRMGLRRTESLMRWVWEANRGNPVDENATLTFGPDGNLVLARSNGQVAWQTSTANKGVVGLKILPNGNMVLYDSKGKFLWQSFDTPTDTLLVGQSLKMGAVTKLVSRASPGENVNGPYSLVMEPKGLHLYYKPTTSPKPIRYYSFSLFTKLNKNESLQNVTFEFENENDQGFAFLLSLKYGTSNSLGGASILNRIKYNTTLSFLRLEIDGNVKIYTYNDKVDYGAWEVTYTLFLKAPPPLFQVSLAATESESSECQLPKKCGNFGLCEESQCVGCPTSSGPVLAWSKTCEPPKLSSCGPKDFHYNKLGGWITT	May be involved in the limitation of water flow through the outer epidermal cell wall, either by direct modification of wall structure or as a signal instructing the protoplast to restrict water transport across the cell wall. Subcellular locations: Secreted In 14-day old seedlings, expressed in the epidermis and apical dome of the shoot and in the hypocotyl, cotyledon and epidermis of the root. In developing seeds, expressed in both the inner and outer epidermis of the integument.
IF1C_DAUCA	Daucus carota	MKEQKWIHEGLITESLPNGMFRIRLDNQDMILGYVSGKIRRSFIRILPGDRVKIEVSRYDSTRGRIIYRLRNKDSKD	One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex. Subcellular locations: Plastid, Chloroplast
MATK_DAUCA	Daucus carota	MEEFQRYLKLNRSQQHYFLYPLIFQEYIYALAHDHGLNRNRSIFLENVGYNKFSLLIVKRAIERMYQYEQKHLILFDNDFNQNRFFGRNNNFSFQMISEGFAVIVEIPFYLRLLSSLEKKGIVKSNNLRSIHSIFPFLEDNFSHLIYVLEILIPYPAHLEILIQTLRYWVKDASSLHLLRFFLHEYRSWNTPNKASSFFSKRNQRFFFVLYNSHICEYESIFVFLRNQSSHLCSTSSGTLLERIYFYGKLEHLVLVEAFAKAFQANLWLFKDPFMHYVRYQGKSILASKGTPPLMKKWTYYFVNLWECRFYLWSQPGRICINQLYNNSLSLLGYISSAGLNPSMVRSQMLENAFIIDNPIKKFDTLVPIVPLIGSLAKARFCNVLGHPISKAVWTDLSDSDIIVRFGRICRNLSHFFSGSSQKKSLYRIKYILRLSCARTLARKHKSTVRAFLKRSGSGLLEEFFTAEEQVLYLTFPRASSTSHRLYRRRIWYLDIICINDLASHELNDSLV	Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns. Subcellular locations: Plastid, Chloroplast
MATK_PRUDU	Prunus dulcis	MEEFQGYLELDRYQQHDFLYPLIFREYIYALAHDHGLNRSILLDNVGYDNKSSLLIIKRLISRMYKQNHFFISANDSNQKKKLGYNKNLYSQKISEGFTVIVEISFSLQLVSSLEATKTVKSYNLRSIHSIFPFLEDKFPHLNYVSDVLIPYPIHLEILVQTLRYWVKDASSLHLLRLFLHEYYNWNSLITSNNFFFSKSNPRLFLLLYNSHVCEYEFILLFLRNQSSHLQLTSSGIFFERIHFYEKIKYPVEEVFANDFPASILWFFKDPFMHYVRYQGKSILASKDTPLLMNKWKYYLVNLWQCHSYVWSQPGRIYINKLSKHSLDFLGYFSSIRPNLSVVRSQMLENSFITDNAMKKLDTLVPIIPLIGSLAKVKFCNALGHPISKSTWADSSDFDIIDRFLRICRNLSHYYSGSSRKKSLYRIKYILRLSCLKTLARKHKSTVRTFLKRLGSKLLEEFFTEEEQILSLVFPRASYTFTFKKFYRGRIWYLDIFCINDLINYE	Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns. Subcellular locations: Plastid, Chloroplast
MATK_PRULA	Prunus laurocerasus	MEEFQGYLELDRYQQHDFLHPLIFREYIYALAHDHGLNRSILLGYDNKSSLLIIKRLISRMYKQNRFIISANDSNQKKNLGYNKNLYSQIISEGFAVIVEIPFSLRLVSSATEIVKSYNLRSIHSIFPFLEDKFPQLNYVSDVLIPYPIHLEILVQTLRYWVKDASSLHLLRLFLHEYYNWNSLITSNNFFFFSKSNPRLFLLLYNSHVCEYEFILLFLRNQSSHLQLISSGIFFERIHFYEKIKYPVEEVFANDFPAAILWFFKDPFMHYVRYQGKSILASKDTPLLMNKWKYYLVNLWQCHSYVWSQPGRIYINKLSKHSLDFLGYFSSIRPNLSVVRSQMLENSFITDNAMKKLDTLVPIIPLIGSLAKVKFCNALGHPISKSTWADSSDFDIIDRFLRIFRNLSHYYSGSSRKKSLYRIKYILRLSCVKTLARKHKSTVRTFLKRLGSKLLEEFFTEEEQILSLIFPRASYTLKKFYSGRIWYLDIFCINDLINHE	Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns. Subcellular locations: Plastid, Chloroplast
MATK_PRUPE	Prunus persica	MEEFQGYLELDRYQQHDFLYPLIFREYIYALAHDHGLNRSILLDNVGYDNKSSLLIIKRLISRMYKHNHFFISANASNQKKKLGYNKNLYSQKISEGFTVIVEISFSLRLVSSLEATETVKSYNLRSIHSIFPFLEDKFPHLNYVSDVLIPYPIHLEILVQTLRYWVKDASSLHLLRLFLHEYYNWNSLITSNNFFFSKSNPRLFLLLYNSHVCEYEFILLFLRNQSSHLQLTSSGIFFERIHFYEKIKYPVEKVFANDFPASILWFFKDPFMHYVRYQGKSILASKDTPLLMNKWKYYLVNLWQCHSYVWSQPGRIYINKLSKHSLDFLGYFSSIRPNLSVVRSQMLENSFITDNAMKKLDTLVPIIPLIGSLAKVKFCNALGHPISKSTWADSSDFDIIDRFLRICRNLSHYYSGSSRKKSLYRIKYILRLSCLKTLARKHKSTVRTFLKRLGSKLLEEFFTEEEQILSLVFPRASYTFTFKKLYRGRIWYLDIFCINDLINYE	Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns. Subcellular locations: Plastid, Chloroplast
METK2_DAUCA	Daucus carota	MDTFLNTSESVNEGHPDKLCDQISDAVLDACLEQDPDSKVACETCSKTNMVMVFGEITTKANVDYEKIVRKTCRDIGFVSDDVGLDADNCKVLVQIEQQSPDIAQGVHGHLTKRPEDIGAGDQGHMFGYATDETPELMPLSHVLATKLGAKLTEVRKNGTCPWLRPDGKTQVTVEYYNDKGAMVPIRVHTVLISTQHDETVTNDEIAADLKEHVIKPIIPAKYLDEKTIFHLNPSGRFVIGGPHGDAGLTGRMIIIDTYGGWGAHGGGAFSGKDPTKVDRSGAYIVRQAAKSIVANGLARRCIVQVSYAIGVPDPLSVFVDSYGTGNIPDKEILKIVKETFDFRPGMIAINLDLKRGGNNRFLKTAAYGHFGRDDADFTWEVVKPLKWEKPQA	Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate. Subcellular locations: Cytoplasm
MT3_PRUAV	Prunus avium	MSSKCSNCDCSDSSQCTKKGYSFDLVIVETENRSMDTVIMDAPAAENGGNCKCGPSCACVDCKC	Metallothioneins have a high content of cysteine residues that bind various heavy metals.
NDHH_MANES	Manihot esculenta	MNVPATRKDLMIVNMGPHHPSMHGVLRLIVTLDGEDVIDCEPILGYLHRGMEKIAENRTIIQYLPYVTRWDYLATMFTEAITVNGPELLGNIQVPKRAGYIRVIMLELSRIASHLLWLGPFMADIGAQTPFFYIFRERELVYDLFEAATGMRMMHNFFRIGGVASDLPHGWIDKCLDFCDYFLTGVTEYQKLITRNPIFLERVEGVGIVGTEEAINWGLSGPMLRASGVQWDLRKVDHYECYDEFDWEIQWQKEGDSLARYLVRIGEMLESIKIIQQALEGIPGGPYENLETRRFDRERDSEWNDFEYRFISKKTSPTFELPKQELYVRVEAPKGELGIFLIGDQSGFPWRWKIRPPGFINLQILPELVKRMKLADIMTILGSIDIIMGEVDR	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. Subcellular locations: Plastid, Chloroplast thylakoid membrane
NDHJ_DAUCA	Daucus carota	MQGRLSAWLVKHGLIHRSLGFDYQGIETLQIKPEDWHSIAVILYIYGYNYLRSQCAYDVAPGGLLASVYHLTRIEYGVDQPEEVCIKVFSPRKNPRIPSVFWVWKGVDFQERESFDMLGISYDNHPRLKRILMPESWIGWPLRKDYIAPNFYEIQDAH	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. Subcellular locations: Plastid, Chloroplast thylakoid membrane
NU4C_DAUCA	Daucus carota	MNFFPWLTIIVILPIFAGSIILFLPHRGNRVIRWYTICICILELLLTTYAFCYHFQLDDPLIQLVEDFKWIDFFDFHWRLGIDGLSIGPILLTGFITTLATLAAWPVTRDSRLFHFLMLAMYSGQIGLFASRDLLLFFIMWELELIPVYLLLSMWGGKKRLYSATKFILYTAGGSVFLLMGVLGVGLYGSTEPTLNFATLVNQSYPVALEIILYIGFFIAFAVKSPIIPLHTWLPDTHGEAHYSTCMLLAGILLKMGAYGLIRINMELLSHAHSIFSPWLVIVGTIQIIYAASTSLGQRNLKKRIAYSSVSHMGFILIGIGSINDTGLNGAILQIVSHGFIGAALFFLAGTSYDRIRLVYLDEMGGIAIPMPKIFTMFSSFSMASLALPGMSGFVAEFIVFFGIITSQKYLLISKLGITFVMAIGIILTPIYSLSMLRQMFYGYKLFNAPNSYVFDSGPRELFVSIAIFIPVIGIGMYPDFVLSLSVDKVEVLLSNFVYR	Subcellular locations: Plastid, Chloroplast thylakoid membrane
PALY_PERAE	Persea americana	MESMDKGTDSYGVTTGFGATSHRRTKQGGALHKELIRFLNAGIFGTNGESGHTLAPSATRAAMLVRINTLLQGYSGIRFEILEAITSLLNHSITPCLPLRGTITASGDLVPLSYIAGMLTGRPNSKGDWPDGKEIDAGEAFRLAGIPSGFFELQPKEGLALVNGTAVGSGLASMVLFEANVLSVLSEVISAIFCEVMQGKPEFTDHLTHKLKHHPGQIEAAAIMEHILDGSSYMKVAKKLHELDPLQKPKQDPYAALRTSPQWLGPQIEVIRNATLSIEREINSVNDNPLIDVSRNKALHGRNFQGTPIGVSMDNTRLAIAAIGKLMFAQFSELVNDFYNNGLPSNLSGGRNPSLDYGFKGAEIAMAAYCSELQFLANPVTNHVQSAEQHNQDVNSLGLISSRKTAEAVEILKLMSSTFLVGLCQAIDLRHLEENLKSTVKNTVSQVAKRVLTIGVNGELHPSRFCEKDLIKVVDGEHLFAYIDDPCSCTYPLMQKLRQVLVEHALINGEKEKDSSTSIFQKIGAFEEELKTHLPKEVESARIELERGNSAIPNRIKECRSYPLYKFVREELKTSLLTGEKVRSPGEEFDKVFSAICQGKVIDPLLECLREWNGAPIPIC	This is a key enzyme of plant metabolism catalyzing the first reaction in the biosynthesis from L-phenylalanine of a wide variety of natural products based on the phenylpropane skeleton. Subcellular locations: Cytoplasm
PH3_PRUSE	Prunus serotina	GTYPPVVLATLXRTH	null
PSBE_DAUCA	Daucus carota	MSGSTGERSFADIITSIRYWVIHSITIPSLFIAGWLFVSTGLAYDVFGSPRPNEYFTENRQGIPLITGRFDPLEQLDEFSRSF	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. Subcellular locations: Plastid, Chloroplast thylakoid membrane
PSBK_DAUCA	Daucus carota	MLNIFSLICICLNSAFYSSSLFFAKLPEAYAFLNPIVDLMPVIPLFFFLLAFVWQAAVSFR	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. Subcellular locations: Plastid, Chloroplast thylakoid membrane
PSBN_DAUCA	Daucus carota	METATLVAIFISGLLVSFTGYALYTAFGQPSQQLRDPFEEHGD	May play a role in photosystem I and II biogenesis. Subcellular locations: Plastid, Chloroplast thylakoid membrane
RK32_DAUCA	Daucus carota	MAVPKKRTSISKKRIRKNIWKGKGSWAALKALSLGKSLSTGNSKSFFVRQKKNKS	Subcellular locations: Plastid, Chloroplast
RL24_PRUAV	Prunus avium	MVLKTELCRFSGAKIYPGKGIRFIRSDSQVFLFANSKCKRYFHNRLKPSKLTWTAMYRKQHKKDIAQEAVKKRRRTTKKPYSRSIVGATLEVIQKRRTEKPEVRDAAREAALREIKERIKKTKDEKKAKKAEVTKSQKSQGKGSIAKGGAQPKGPKLGGWRWQALSHCSVAYLLGSRVIDRTCLFV	null
RR14_DAUCA	Daucus carota	MARKGLIQRENKRQKLEQKYHSIRRSSKKEIRQVLSLSDKWEIYGKLQSPPRNSAPTRLHRRCFSTGRPRANYRDFGLSGQILREMVHACLLPGATRSSW	Binds 16S rRNA, required for the assembly of 30S particles. Subcellular locations: Plastid, Chloroplast
RR2_MANES	Manihot esculenta	MIRRYWNINFEEMMKAGVHFGHGTRKWNPRMAPYISAKRKGIHITNLTRTARFLSEACDLVFDAASRRKQFLIVGTKNKAADSVARAAIRARCHYVNKKWLGGILTNWSTTETRLQKFRDLRMEQKAGRLNRLPKGDAARLKRQLAHLQTYLGGIKYMTGLPDIVIIVDQQEEYTALRECMTLGIPTICLIDTNCDPDLADISIPTNDDAIASIRLILNKLVFAICEGRSSYIRNP	Subcellular locations: Plastid, Chloroplast
RRFC_DAUCA	Daucus carota	WTAAANYVKIKVGTGKFARKTVVLSQKRTGTLKCATMEEIEAEKSLIEKSVKERMEKTIENVKASFNSIRTXRSNPDMLDKIKVEYYGTPTSLKSIAQISTPDSSSLLVNPYDKSSLKDIEKAIVNSDLGITPNNDGDVIRLSIPQLTADRRKELSKIVAKQAEEGKVALRNIRRDAIKSYDKLEKEKKLSEDNVKDLSSDLQKVIDEYIKKVDSIFKQKEKELMTV	Responsible for the release of ribosomes from messenger RNA at the termination of chloroplastic protein biosynthesis. Subcellular locations: Plastid, Chloroplast
RSSA_DAUCA	Daucus carota	MASGARELSTMEADIQMMCAAEVHLGTKNCDFQMERYVFKRRNDGIYIINLGKTWEKLMLAARVIVSIENPQDIIVQSARPYGQRAVLKFAQYTGAHAIAGRHTPGTFTNQLQTSFSEPRLLILTDPRTDHQPIKEAALGNIPTIAFCDTDSPMRYVDIGIPANNKGKHSIGCLFWLLARMVLQMRGVISQGHKWEVMVDLFFYREPEETKDQEEEDLPVGDYVADYAAAPIGGADQWNAIPDAQWGGDVVQPANSAVPAGTWTDAGPIAGDGWDAAAAPPVPGAVGLDVPAPTGWE	Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Subcellular locations: Cytoplasm
SSG1_MANES	Manihot esculenta	MATVIAAHFVSRSSHLSIHALETKANNLSHTGPWTQTITPNGLRSLNTMDKLQMKTQSKAVKKVSATGNGRPAAKIICGHGMNLIFVGAEVGPWSKTGGLGDVLGGLPPAMAARGHRVMTVSPRYDQYKDAWDTSVSVEIKIGDRIETVRFFHSYKRGVDRVFVDHPMFLEKVWGKTGSKIYGPRAGLDYQDNQLRFSLLCLAALEAPRVLNLNSSKNFSGPYGEEVAFIANDWHTALLPCYLKAIYQPMGIYKHAKVAFCIHNIAYQGRFAFSDFPRLNLPDKFKSSFDFIDGYEKPVKGRKINWMKAGILESDRVLTVSPYYAQEVISGVERGVELDNFIRKTGIAGIINGMDVQEWNPVTDKYIDIHYDATTVMDAKPLLKEALQAEVGLPVDRNVPLIGFIGRLEEQKGSDIFVAAISQLVEHNVQIVILGTGKKKFEKQIEHLEVLYPDKARGVAKFNVPLAHMITAGADFMLVPSRFEPCGLIQLHAMRYGTVPIVASTGGLVDTVKEGYTGFQMGALHVECDKIDSADVAAIVKTVARALGTYATAALREMILNCMAQDLSWKGPARMWEKMLLDLEVTGSEPGTEGEEIAPLAKENVPTP	Responsible for the synthesis of amylose in reserve starch. Subcellular locations: Plastid, Chloroplast, Plastid, Amyloplast Amyloplast or chloroplast, granule-bound. Synthesized in a number of different organs, but most abundantly in tubers.
TBA_DAUCA	Daucus carota	MRECISVHIGQAGIQIGNACWELYCLEHGIQPNGQMPSDKTVGGGDDAFNTFFSETGAGKHVPRAIFVDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTVYPSPQISTSVVEPYNSVLSTHSLLEHTDVSVLLDNEAIYDICKRSLDIERPTYTNLNRLVSQVISSLTASLRFDGALNVDVTEFQTNLVPYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAFEPSSMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVGTIKTKRTIQFVDWCPTGFKCGINYQAPTVVPGGDLAKVQRAVCMISNSTSVAEVFSRIDTKFDLMYSKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGAESAEGDDEDEGEDY	Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. Subcellular locations: Cytoplasm, Cytoskeleton
UP02_DAUCA	Daucus carota	VGLVFNPYNR	null
UP03_DAUCA	Daucus carota	CSVVDLAR	null
ALL1_PRUDU	Prunus dulcis	VTXEEGXYSISDQSKVGEQXIRSPDREM	null
ATPI_DAUCA	Daucus carota	MNVLSCSINKLNGLYDISGVEVGQHFYWKIGGFQVHGQVLITSWVVIAILLGSATLAVRNPQTIPTSGQNFFEYVLEFIRDVSKTQIGEEYGPWVPFIGTMFLFIFVSNWSGALLPWKIIQLPHGELAAPTNDINTTVALALLTSVAYFYAGISKKGLGYFGKYIQPTPILLPINILEDFTKPLSLSFRLFGNILADELVVVVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIGESMEGHH	Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Subcellular locations: Plastid, Chloroplast thylakoid membrane
C7317_PRUMU	Prunus mume	MLNPLQVLQELNESSSFLQPLAFTLLAIFLVLLYTWYSSTKTTTQKSTQPPSPPKLPIIGNLHQIGSYPHRSLQALSQRHGPLMLLHFGSVPVLVVSSAEAAREILKTHDLTFSDRPKSTIFEKLLYNYKDVASAPYGEYWRQVRSICVLNLLSNRRVRSFRSVREEETKSMIRNIKGSSSSVLNLSEMFVRLTNDVVCKVALGRKYSDGEGGESGRMFKEILGEFGDLLGTVNIGDYVPWLSWLSHVNGLGAKLDKVAKQLDDFIDTVVQEHMNHSSRSGDDDQKDFLDILLAIQKETSAGIPIDGVSVKGIILDMFAAGTDTTYSALEWAMTELLRHPRVMNKLQNEVRGIVGNRTDVITEDDLVEMHYLKAVTKETLRLHPPIPLLVPRMSTRDVEVNGYNIKANTQVFISAWQIGRDPKLYDKPEEFEPERFLNNGIDYKGNDFELIPFGAGRRVCPGIQFAMAVNEIALANIVHKFDWALPDEASGEDLDMTETTGLTAHKKYPLKAVAFPHF	Subcellular locations: Membrane Expressed at similar levels in fruit kernel, seedlings, leaves, stems and buds.
CDPK_DAUCA	Daucus carota	MGGCFSKKEYQADGNGYRSAPTAYHTVTDQSYEKSSQRSQPQAQPQPQVQQTGPSLKPRQVHRPESNTILGKPFEDIRGKYTLGKELGRGQFGCVYQCTENSSGQLYACKSILKRKLVSKNDKEDIKREIQILQHLSGQPNIVEFKGVFEDRQSVHLVMELCAGGELFDRIIAQGHYSERAAATICRQIVNVVHVCHFMGVMHRDLKPENFLLSSKDKDAMLKATDFGLSVFIEEGKVYRNIVGSAYYVAPEVLRRSYGKEIDIWSAGVILYILLSGVPPFWAENEKGIFDAILEGVIDFESEPWPSVSNSAKDLVRKMLTQDPRRRITSAQVLDHPWMREGGEASDKPIDSAVLSRMKQFRAMNKLKQLALKVIAESLSEEEIKGLKSMFANMDTDKSGTITYEELKSGLARLGSKLSEVEVQQLMDAADVDGNGTIDYLEFITATMHRHKLESYEHQAFQYFDKDNSGFITKDELESAMKEYGMGDEATIKDIISEVDSDNDGRINYDEFCAMMRRARNRRKLFSVSLTS	May play a role in signal transduction pathways that involve calcium as a second messenger. Subcellular locations: Membrane
COMT1_PRUDU	Prunus dulcis	MGSTGETQMTPTQVSDEEANLFAMQLASASVLPMVLKAAIELDLLEIMAKAGPGVFLSPTDIASQLPTKNPDAPVMLDRMLRLLASYSILTYSLRTLADGKVERLYGLGPVCKFLTKNEEGVSIAPLCLMNQDKVLLESWYHLKDAVLEGGIPFNKAYGMTAFEYHGTDPRFNKVFNRGMADHSTITMKKILETYKGFEGLTSVVDVGGGTGAVLNMIVSKYPSIKGINFDLPHVIEDAPQYPGVEHVGGDMFVSVPKGDAIFMKWICHDWSDEHCLKFLKNCYAALPDNGKVILGECILPVAPDSSLATKGVVHIDVIMLAHNPGGKERTEQEFQALAKGAGFQGFNVACSAFNTYVIEFLKKN	Catalyzes the conversion of caffeic acid to ferulic acid and of 5-hydroxyferulic acid to sinapic acid. The resulting products may subsequently be converted to the corresponding alcohols that are incorporated into lignins.
EF1A2_DAUCA	Daucus carota	MGKEKIHISIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTPKYSKSRFEEIVKEVSSYLKKVGYNPDKIAFIPISGFEGDNMIDRSTNLDWYKGPTLLEALDQISEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPSGLTTEVKSVEMHHEALQEALPGDNVGFNVKNVAVKDLKRGYVASNSKDDPAKEAANFTAQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEIQTKIDRRSGKELEKEPKFLKNGDAGFVKMIPTKPMVVETFMSYPPLGRFAVRDMRQTVAVGVIKSVEKKDPTGAKVTKAAIKKK	This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. Subcellular locations: Cytoplasm
EML_DAUCA	Daucus carota	MASGQEKRSELDARAKQGETVVPGGTGGKSLEAQEHLAEGRSKGGHTRKEQLGTEGYQEIGTKGGETRREQMGKEGYEQMGRMGGLATKDKSGAERAEEEGIDIDQSKFRTKS	Expressed in embryogenic cells, somatic embryos and seeds at the later stages of development. Not detected in leaves.
FABG_PERAE	Persea americana	VYEQVSIEVPQSVEAPVVIITGASEIEASTIQALSFGPDVXKEADVEAMIKAVDAWGQVDVLINNAGITRAGVIGLQKNINVNAIAPGFIASDMTAKILETIPLGR	Subcellular locations: Plastid, Chloroplast, Plastid And non-photosynthetic plastids. Mesocarp.
INV2_DAUCA	Daucus carota	MLIRCFHIKMALVTCFHSMLFLSAVVFIFSLDVNIRGVEASHQVFPELQSVSAVNVQLVHRTGYHFQPKKHWINDPNGPMYYKGFYHLFYQYNPKGAVWGNIVWAHSISKDLINWVALEPAIFPSKPFDKYGCWSGSATVLPGGKPVIMYTGIVTPSPVNTQVQNFAVPANYSDPYLREWIKPDNNPIVRARSENSSSFRDPTTAWFDGVHWKILVGSRRKHRGIAYLYRSRNFLKWTKAKHPLHSKDRTGMWECLDFYPVAPKGMNGLDTSVTGQDIKHVLKVSLYSTRYEYYTVGEYDRDNDIYVPDNTSVDGWAGLRYDYGNFYASKTFFDPDKQRRILWGWANESDSKQDDVQKGWAGIQLIPRKLWLDPNGKQLIQWPIEEIQLLRGQNVHMGSQVLNTGEHIEVKGVTAAQADVDATFSFKSLDRAEWFDPNWAKLDALDVCDWMGSTVRGGLGPFGFLTLASEKLEEYTPVFFRVFKTKDKLKVLMCSDAKRSSTTAEGLYKPPFAGYVDVDLSDKKISLRSLIDNSVVESFGAHGRTCITSRVYPKIAIYNNAHVFVFNNGTEAITIDSLDAWSMKAPSLMNNN	May play an important role in phloem unloading and in stress response. Subcellular locations: Secreted, Cell wall Ionically bound to the cell wall.
INV3_DAUCA	Daucus carota	MARTKILVFSSDSSLFLLSIFSFIFLNINGVDSTHRVFPELQSISAVDVKLVHRTGYHFQPQKHWINDPNGPMFYKGYYHLFYQYNPKGSVWGNIVWAHSVSKDLINWIALEPAIFPSKPFDQYGCWSGSATILPGNKPVILYTGIVSPDPENAQVQNYAVPANYSDPFLREWVKPDNNPLVGVHTENPSAFRDPTTAWFDGGHWKMLVGSSRKHRGIAYLYRSKDFKKWKRSPHPIHTKAETGMWECPDFYPVSPRSEDGLDNSKMGRGIKHVLKVSLNSTRYEYYTIGRYNRVRDFYVPDNTSVDGWAGLRYDYGNFYASKTFYDPIKKRRILWGWANESDSQIDDVQKGWAGIQLIPRRIWLDPSGRQLVQWPIEEVEGLRGSELHMRNQKLDMGVHVEVTGITAAQADVDATFSFKSLDKAESFDPEWINLDAQDVCDSMGSTIQGGLGPFGLLTLASKDLEEYTPVFFRIFKAEDQKLKVLMCSDAKRSSLAEGLYKPSFRGFVDVDLSDKKISLRSLIDNSVVESFGAQRKNLISSRVYPTLAIYNNAHLFVFNNGTEPITVDNLDAWSMNSPSEMN	May play an important role in phloem unloading and in stress response. Subcellular locations: Secreted, Cell wall Ionically bound to the cell wall.
MATK_MANES	Manihot esculenta	MEERYLELDRSRKNDFLYPFIFREYIYTFAHDHSLNRSILLENVGYDNKSSLLIVKRLITRMYQQNHLIISANDSNQNLFFRYNKNLYYQMISEGFAVIVEIPFSLRLVSSLDLERSEIVKSHKLRSIHSIFPFLEDKFPHLNYVSDILIPYPIHLEKLVQTLRYWVKDPSSLHLLRLFLHEYWNLNSLIIPKKFITIFIKRNPRFFLFLYNSHVYEYESIFFFLRNQSFHLRSIFLRVLLERIFFYGKIEHFAEVFANDFQAILWLFKDPFMHYVRYQGKSILASKDRPFLMKKWKYYLVNLCQCHFYVWFQPEKIYINSLSKHSLNFLGYLSNVQLNPLVVRSQMLENSFIIDKDSTMKKLDTIVPIIPLIGSLAKTKFCNAVGHPISKPIRADSADSDIIDRFVRICRNLSHYYSGSSKKKSLYRIKYILRLSCVKTLARKHKSTVRAFLKRLGSELLEEFFTEEEQILSLIFPKVSSSSRRLYRGRVWYLDIISINDLANHE	Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns. Subcellular locations: Plastid, Chloroplast
NU4LC_MANES	Manihot esculenta	MMLEHVLVLSAYLFSIGIYGLITSRNMVRALMCLELILNAVNLNFVTFSDFFDSRQLKGNIFSIFVIAIAAAEAAIGPAIVSAIYRNRKSIHINQSNLLNK	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. Subcellular locations: Plastid, Chloroplast thylakoid membrane
NU5C_DAUCA	Daucus carota	MEQTYQYAWIIPFLPLPVPMLIGAGLLLFPSATKSLRRMWAFQSVFLLSIVMLFSINLSIQQINGSSIYQYVWSWIINNDFSLEFGYLIDPLTSIMSILITTIGIMVLIYSDNYMSYDQGYLRFFAYMSFFSTSMLGLVTSSNLIQIYIFWELVGMCSYLLIGFWFTRPVAANACQKAFVTNRVGDFGLLLGILGFYWITGSFEFRDLFKILNNLISNNEVNFLFVTFCAVLLFAGAVAKSAQFPLHVWLPDAMEGPTPISALIHAATMVAAGIFLVARLIPLFIVIPHIMNFISLVGVITILFGATFALAQKDIKRGLAYSTMSQLGYMMLALGMGSYRSALFHLITHAYSKALLFLGSGSVIHSMETLVGYSPNKSQNMVFMGGLTKHVPITKTSFLLGTLSLCGIPPLACFWSKDEILNDTWLYSPIFAIIAWFTAGLTAFYMFRIYLLTFEGHLNVHFQNYSGKKNTPFYSISLWGKENSKRINKNFSLLTMKNPEIFSFFSKKTYQIDQNARNITQPFITITRFGNKKFFLYPYESDNTMLFPILVLVLFTLFVGSLGIPFNHEGVRLDILSKWLTPSINLLHKNLNNSIGWYEFLKDALFSVSIAIFGIFIAFFLYKPVYSSLQNWDLINSFVKTGPKRILLDKIINGIYDWSYNRGYIDAFYARFFIGGIRGLAKLTSFFDRRVIDGITNGVGVLSFFLGEGIKSIGGGRISSYLFLYFFFVAILLLIINFLLI	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). Subcellular locations: Plastid, Chloroplast thylakoid membrane
PAL1_PRUAV	Prunus avium	MATNSIKQNGHKNGSVELPELCIKKDPLNWGVAAETLKGSHLDEVKRMVAEYRKPVVKLGGESLTISQVAAIATHDSGVKVELSESARAGVKASSDWVMDSMSKGTDSYGVTTGFGATSHRRTKQGAALQKELIRFLNAGVFGSTKESGHTLPHQATRAAMLVRINTLLQGYSGIRFEILEVITKFLNNNVTPCLPLRGTITASGDLVPLSYIAGMLTGRPNSKAVGPDGQTLSAAEAFEFVGINSGFFELQPKEGLALVNGTAVGSGLASTVLFDTNILALLSEILSAIFAEVMQGKPEFTDHLTHKLKHHPGQIEAAAIMEHILDGSSYVKAAKKLHEQDPLQKPKQDRYALRTSPQWLGPQIEVIRYSTKSIEREIDSVNDNPLIDVSRNKALHGGNFQGTPIGVSMDNTRLAIASIGKLMFAQFSELVNDFYNNGLPSNLSGGRNPSLDYGFKGAEIAMASYCSELQFLANPVTNHVQSAEQHNQDVNSLGLISSRKTAEAVDILKLMSSTFLVALCQAIDLRHLEENLRNTVKNTVSQVAKRTLTTGVNGELHPSRFCEKDLLKVVDREYVFAYIDDPCSATYPLMQKLRQVLVEHALTNGENEKNASTSIFQKIVAFEEELKVLLPKEVDSARAALDSGSAGVPNRITECRSYPLYKFVREELGAEYLTGEKVRSPGEECDKVFTAICEGKIIDPILDCLEGWNGAPLPIC	This is a key enzyme of plant metabolism catalyzing the first reaction in the biosynthesis from L-phenylalanine of a wide variety of natural products based on the phenylpropane skeleton. Subcellular locations: Cytoplasm
PETG_DAUCA	Daucus carota	MIEVFLFGIVLGLIPVTLAGLFVTAYLQYRRGDQSDL	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. PetG is required for either the stability or assembly of the cytochrome b6-f complex. Subcellular locations: Plastid, Chloroplast thylakoid membrane
PETN_MANES	Manihot esculenta	MDIVSLAWAALMVVFTFSLSLVVWGRSGL	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. Subcellular locations: Plastid, Chloroplast thylakoid membrane
PLAS_DAUCA	Daucus carota	AEVKLGADDGALVFSPSSFSVAKGEGISFKNNAGFPHNIVFDEDEVPAGVDVSKISQEDYLDGAGESFTVTLTEKGTYKFYCEPHAGAGMKGEVTVT	Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I. Subcellular locations: Plastid, Chloroplast thylakoid membrane Loosely bound to the inner thylakoid membrane surface in chloroplasts.
PSKR1_DAUCA	Daucus carota	MGVLRVYVILILVGFCVQIVVVNSQNLTCNSNDLKALEGFMRGLESSIDGWKWNESSSFSSNCCDWVGISCKSSVSLGLDDVNESGRVVELELGRRKLSGKLSESVAKLDQLKVLNLTHNSLSGSIAASLLNLSNLEVLDLSSNDFSGLFPSLINLPSLRVLNVYENSFHGLIPASLCNNLPRIREIDLAMNYFDGSIPVGIGNCSSVEYLGLASNNLSGSIPQELFQLSNLSVLALQNNRLSGALSSKLGKLSNLGRLDISSNKFSGKIPDVFLELNKLWYFSAQSNLFNGEMPRSLSNSRSISLLSLRNNTLSGQIYLNCSAMTNLTSLDLASNSFSGSIPSNLPNCLRLKTINFAKIKFIAQIPESFKNFQSLTSLSFSNSSIQNISSALEILQHCQNLKTLVLTLNFQKEELPSVPSLQFKNLKVLIIASCQLRGTVPQWLSNSPSLQLLDLSWNQLSGTIPPWLGSLNSLFYLDLSNNTFIGEIPHSLTSLQSLVSKENAVEEPSPDFPFFKKKNTNAGGLQYNQPSSFPPMIDLSYNSLNGSIWPEFGDLRQLHVLNLKNNNLSGNIPANLSGMTSLEVLDLSHNNLSGNIPPSLVKLSFLSTFSVAYNKLSGPIPTGVQFQTFPNSSFEGNQGLCGEHASPCHITDQSPHGSAVKSKKNIRKIVAVAVGTGLGTVFLLTVTLLIILRTTSRGEVDPEKKADADEIELGSRSVVLFHNKDSNNELSLDDILKSTSSFNQANIIGCGGFGLVYKATLPDGTKVAIKRLSGDTGQMDREFQAEVETLSRAQHPNLVHLLGYCNYKNDKLLIYSYMDNGSLDYWLHEKVDGPPSLDWKTRLRIARGAAEGLAYLHQSCEPHILHRDIKSSNILLSDTFVAHLADFGLARLILPYDTHVTTDLVGTLGYIPPEYGQASVATYKGDVYSFGVVLLELLTGRRPMDVCKPRGSRDLISWVLQMKTEKRESEIFDPFIYDKDHAEEMLLVLEIACRCLGENPKTRPTTQQLVSWLENIDVSS	Phytosulfokine receptor with a serine/threonine-protein kinase activity. Regulates, in response to phytosulfokine binding, a signaling cascade involved in plant cell differentiation, organogenesis and somatic embryogenesis. Subcellular locations: Cell membrane Expressed ubiquitously in leaf, apical meristem, hypocotyl and root.
RBL_DAUCA	Daucus carota	MSPQTETKAGVGFKAGVKDYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYGIEPVAGEENQFIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMMKRAIFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNEIIREATKWSPELAAACEVWKEIKFEFEAMDTL	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. Subcellular locations: Plastid, Chloroplast
RBL_MANES	Manihot esculenta	MSPQTETKASVGFKAGVKDYKLTYYTPDYQTKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYGLEPVPGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRVPPAYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMIKRAVCARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHIHAGTVVGKLEGERDITLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNDIIREASKWSPELAAACEVWKEIKFEFAAVDTLDK	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. Subcellular locations: Plastid, Chloroplast
RK22_MANES	Manihot esculenta	MIKIKKRKRNTYEVYALGQHICMSPHKARRIIDQIRGRSYEETLMILELMPYRACYPIFKLIYSAAANASHNMGFNEANLIISKAEVNEGTTVKKLKPQARGRGYPIKRSTCHISIVLKNISLYEEYDEYIYI	This protein binds specifically to 23S rRNA. 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. Subcellular locations: Plastid, Chloroplast
RL23A_DAUCA	Daucus carota	MSPAKVDVTKKSDAKAQALKTAKAVKSGTTKFKKVKKIRTSVTFHRPRTLTKDRNPKYPRISATPRNKLDQYQILKYPLTTESAMKKIEDNNTLVFIVDIRANKKKIKDAVKKMYDIQTKKVNTLIRPDGTKKAYVRLTPDYDALDVANKIGII	This protein binds to a specific region on the 26S rRNA.
RPOB_DAUCA	Daucus carota	MLRDGNEGMSTIPGFNQIQFEGFCRFMDQGLTEELYKFPKIEDTDQEIEFQLFVETYQLVEPLIKERDAVYESLTYSSEFYISAGLIWKTSRDMQEQTIFLGNIPLMNSLGTSIVNGIYRIVINQILQSPGIYYRSELDHNGISVYTGTIISDWGGRLELEIDKKARIWARVSRKQKISILVLSSAMGSNLREILENVCYPEIFLSFLTDKEKKKIGSKENAILEFYQQFACVGGDPVFSESLCKELQKKFFQQKCELGKIGRRNMNRRLRLDISQNNTFLLPRDILAAADHLIGMKFGMGTLDDMNHLKNKRIRSVADLIQDQLGLALVRLENMIRGTIGGALRHKLIPSPQNLVTSTPLTSTYESFFGLHPLSQVLDRTNPLTQIVHGRKLSYLGPGGLTGRTASFRIRDIHPSHYGRICPIDTSEGINVGLIGSLAIHAKIGRGGSLESPFYEISQRSKGARMLYLSPGKDEYYMVAAGNPLALNQGLQEEQVVPARYRQEFLTIAWEQVHLRSIFSFQYFSIGASLIPFIEHNDANRALMSSNMQRQAVPLSRSEKCIVGTGLERQAALDSGVLAIAEHEGKVIYTDTDKILLSGNGDTLNIPLVMYQRSNKNTCMHQKPQVQRGKYIKKGQILAYGAATIGGELALGKNVLVAYMPWEGYNFEDAVLISERLVYEDIYTSFHIRKYEIQTHVTSQGPERVTREIPHLEAHLLRNLDKNGIVMLGSWVETGEILVGKLTPQMVKESSYAPEDRLLRAILGIQVSTSKETCLKLPIGGRGRVIDVRWIQKRVGSSYNPETIRVYILQKREIKVGDKVAGRHGNKGIISKILPRQDMPYLQDGRPVDMVFNPLGVPSRMNVGQIFECSLGLAGGLLDRHYRIAPFDERYEQEASRKLVFSELYQASKQTATPWVFEPEYPGKSRIFDGRTGDPFEQPVIIGKPYILKLIHQVDDKIHGRSSGHYALVTQQPLRGRAKQGGQRVGEMEVWALEGFGVAYILQEMLTYKSDHIRARQEVLGTTIIGGAIPNPEDAPESFRLLVRELRSLALELNHFFVSEKTFKIKRKEA	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Subcellular locations: Plastid, Chloroplast
RPOC2_MANES	Manihot esculenta	MEVLMAERANLVFHNKAIDGTAIKRLISRLIDHFGMAYTSHILDQVKTLGFQQATATSISLGIDDLLTIPSKGWLVQDAEQQSLILEKHYHYGNVHAVEKLRQSIEIWYATSEYLRQEMNLNFRMTEPFNPVHIMSFSGARGNTSQVHQLVGMRGLMSDPQGQMIDLPIQSNLREGLSLTEYIISCYGARKGVVDTAVRTSDAGYLTRRLVEVVQHIVVRRTDCGTARGISVSPRNGMMPERIFIQTFIGRVLADNIYMGLRCIAIRNQDIGIGLANRFITFRTQTISIRTPFTCRSTSWICRLCYGRSPTHGDLVELGEAVGIIAGQSIGEPGTQLTLRTFHTGGVFTGGTAEHVRAPSNGKIKFNEDLVHPIRTRHGHPAFLCYIDLYVTIKSQDIIHNVTIPPKSFLLVQNDQYVESEQVIAEIRAGAYTLNFKEKVRKHIYSDSEGEMHWSTDVYHAPEFTYSNVHLLPKTSHLWILSGSSCRSSIVPFSLHKDQDQMNVHSLSVKRRYISSPSVNNDQVKHKFFSSDFSGKKESGIPDYSELNRSICTGHCNLIYSTILYKNSDLLAKRRRNKFIIPFQSIQEREKELMTQSAISIEIPINGIFRRNSVFAYFDDPQYRKKSSGITKYGAIGVHSIVKKEDLIEYRGVKEFKPKYQTKVDRFFFIPEEVYILPESSSLMVRNNSIIGVDTQIALNTRSRVGGLVRVERKKKKMELKIFSGDIHFPGETDKISRHSDILIPPGTVKTNSKESKKVKNWIYIQRITPTKKKYFVLVRPVIIYEIANGINLETLFPQDLLQEKDNLKLRVVNYILYGTGKPIRGISDTSIQLVRTCLVLNWDQDKKSSSIEEARAAFVEISTNGLIRDFLRINLVKFHISYIGRKRNDPSGSEPISNNGSDRTNINPFYPIYSKTRVQQSLKQNQGTISTLLNINKECQSLIILSSSNCFQMDPFNDVKHHNVIKESIKRDPIIPIRNSLGPLGTALQIANFYLFYHLNLITHNQISVTKYSKLYNLKQTFQVLKYYLMDENGRIVNPDPCSNSVLNPFNLNWYFLHHNYCESFFTIISLGQFICENLCMAKNGPHLKSGQVIIVHIDSVVIRSAKPYLATPGATVHGHYGEILYEGNTLVTFIYEKSRSGDITQGLPKVEQVLEVRSIDSISINLEKRVEGWNECITRILGIPWGFLIGTELTIVQSRISLVNKIQKVYRSQGVQIHNRHIEIIVRQITSKVLVSEDGMSNVFSPGELIGLLRAERTGRALEEAICYGAILLGITRASLNTQSFISEASFQETTRVLAKAALRGRIDWLKGLKENVVLGGMIPVGTGFKGLVQGSRQHKNIPLKTKKKNLFEGEFRDRDILFHHRELFDSCISKNLYDTSEQSFIGFNDS	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Subcellular locations: Plastid, Chloroplast
RR11_DAUCA	Daucus carota	MAKTIPRIGSRKNGRIGSRKNTRRIPKGVIHVQASFNNTIVTVTDVRGRVVSWSSAGTCGFKGTRRGTPFAAQTAAGNAIRTVVDQGMQRAEVMIKGPGLGRDAALRAIRRSGILLTFVRDVTPMPHNGCRPPKKRRV	Subcellular locations: Plastid, Chloroplast
RR15_MANES	Manihot esculenta	MVKNSFISVISQEEKDENKGSVEFQIVSFTNKIRRLTSHFELHRKDYLSQRGLRKILGKRQRLLSYLAKKNRVRYKELISRLDIRESKTR	Subcellular locations: Plastid, Chloroplast
RR3_DAUCA	Daucus carota	MGQKINPLGFRLGTTQSHHSLWFTQPKNYSEGLQEDQKIRDFIKNYVQKNLKISSGVEGIARIEIHKRIDLIQVIIYMGFPKLLIENRPGGIEKLQMNLQKEFNCVNRKLNITITRIAKPYGSPNILAEFIAGQLKNRVSFRKAMKKAIELTEQADTKGIQVQISGRIDGKEIARVEWIREGRVPLQTIRAKIDYCSYTVRTIYGVLGIKIWIFLDGE	Subcellular locations: Plastid, Chloroplast
TLP_PRUAV	Prunus avium	MMKTLVVVLSLSLTILSFGGAHAATISFKNNCPYMVWPGTLTSDQKPQLSTTGFELASQASFQLDTPVPWNGRFWARTGCSTDASGKFVCATADCASGQVMCNGNGAIPPATLAEFNIPAGGGQDFYDVSLVDGFNLPMSVTPQGGTGDCKTASCPANVNAVCPSELQKKGSDGSVVACLSACVKFGTPQYCCTPPQNTPETCPPTNYSEIFHNACPDAYSYAYDDKRGTFTCNGGPNYAITFCP	Subcellular locations: Secreted Abundantly expressed in ripening fruit.
YCF2_MANES	Manihot esculenta	MKGHQLKSWIFELREILREIKSVGSFIHIFFHQERFIKLLDSRIWSILLSRNSQGSTSNRYFTIKGVVLFVVVVLIYRINNRKMVERKNLYLTGLLPIPMNSIGPRNDTLEESFWSSNINRLIVSLLYLPKGKKISESSFLDPKESTWVLPITKKCIMSESNWGSRWWRNWIGKKRDSSCKISNETVAGIEISFKEKDIKYLEFLFVYYMDDPIRKDHDWELFDRLSPRKGRNIINLNSGQLFEILVKDWICYLMFAFREKIPIEVEGFFKQQGAGSTIQSNDIEHVSHLFSRKKWAISLQNCAQFHMWQFRQDLFVSWGNNPHESDFLRNISRENWIWLDNVWLVNKDRFFSKARNISSNIQYDSTRSSFVQGRNSSQLKGSSDQSRDHFDSISNEDSEYHTLINQRKIQQLKERSILWDPSFLQTERTEIESDRFPKCLSGYSSMSRLFTEGEKEMNNHLLPEEIEEFLGNPTRSIRSFFSDRSSELHLGSNPTERSTRNQKLLKKEQDVSFVPSRRSENKEIVNIFKIITYLQNTVSIHPISSDPGCDMVLKDELDMDSSNKISFLNKNPFFDLFHLFHDRNGGGYTLHHDFESEERFQEMADLFTLSITEPDLVYHKGFTFFIDSYGLDQKQFLNEVFNSRDESKKKSLLVLPPIFYEENESFYRRIRKKWVRISCGNDLEDPKQKIVVFASNNIMEAVNQYGLILNLIQIQYSTYGYIRNVLTQFFLMNRSDRNFEYGIQRDQIGNDTLNHRTIMKYTINQHLSNLKQSQKKWFDPLIFIFLSRTERSMNWDPNAYRYKWSNGSKNFQEHLEHFISEQKSRFLFQVVFDRLRINQYSIDWSEVIDKKDLSKSLRFFLSKLLLFLSKFLLFLSNSLPFFFVSFGNIPIHRSEIHIYELKGPNDQLCNQLVEPIGLQIVHLKKLKPFLLLLDDHDTSQKSKFLINGGTISPFLFNKIPKWMIDSFHTRNNRRKSFDNTDSYFSMISHDQDNWLNPVKPFHRSSLISSFYKANRLRFLNNLHHFCFYCNKRFPFYVEKARIKNYDFTYGQFLNILFIRNKIFSLCGGKKKHAFLERDTISPIESQVSNIFIPNDFPQSGNERYNLYKSFHFPIRSDPFVRRAIYSIADISGTPLTEGQIVNFERTYCQPLSDMNLSDSEGKNLHQYLNFNSNMGLIHTPCSEKYLPSEKRKKRSLCLKKCVEKGQMYRTFQRDNAFSTLSKWNLFQTYMPWFLTSTGYKYLNLIFLDTFSDLLPILSSSQKFLSIFHDIMHGSDISWLIFQKRLWKICRNLISEISSKCLHNLLLSEEMIHRNNEPPLISTHLRSPNVREFLYSILFLLLVAGYLVCTHLLFVSHAYSELQTEFEKVKSLMIPSYMIELRKLLDRYPTSELNSFWLKNLFLVALEQLGDFLEEMRGSASGGNMLWGGGPAYGVKSIRSKKKFWNINLIDLISIIPNPINRITFSRNTRHLSHTSKEIYSLIRKRKNVNGDWIDDKIESLVANSDWIDDKEREFLVQFSTLTTEKRIDQILLSLTHSDHLSKNDSGYQMIEEPGAIYLRYLVDIHKKYLMNYEFNTPCLAERRIFLAYYQTTTYSQTSCGVNSFHFPSHGKPFSLRLALSPSRGILVIGSIGTGRSYLVKYLATNSYLPFVTVFLNKFLNNKPKGFLIDDSDDIDDSDDIDDSDDIDASDDIDVSDDIDVSDDDIDRDFDFDTELEFLTTMDALTIDMMPEIEINRFYITLQFELAKAMSPCIIWIPNIHDLDVNESNYLSLGLLVNYLSRDCERCSTRNILVIASTHIPQKVDPALIAPNKLNTCIKIRRFLIPQQRKHFFTLSYTRGFHLENKMFHTNGFGSITMGSNVRDLVALTNEALSISITQKKSIIDTNIIRSALHRQTWDLRSRVRSVQDHGIFFYQIGRAVAQNVFLSNCPIDPISIYMKKKSCNEGDSYLYKWYFELGTSMKKLTILLYLLSCSAGSVAQDLWSLPGPDEKNGITYYGLVENDSDLVHGLLEVEGALVGSSRTEKDCSQFDNDRVTLLLRPEPRSPLDMMQNGSCSILDQRFLYEKYESEFEEGEGEEVLDPQQIEEDLFTHIVWAPRIWRPWGFLFDCIERPNELGFPYWARSFRGKRIIYDEEIIYDEEIIYDEEDELQENDSEFLQSGTMQYQIRDRSSKEQGFFRISQFIWDPADPLFFLFKDQPFVSVFSHREFFADEEMSKGLLTSQTDPPTSIYKRWFIKNTQEKRFELLIHRQRWLRTNSSLSNGFFRSNTLSESYQYLSNLFLSNGTLLDQMTKALLRKRWLFPDEMKIGFM	Probable ATPase of unknown function. Its presence in a non-photosynthetic plant (Epifagus virginiana) and experiments in tobacco indicate that it has an essential function which is probably not related to photosynthesis. Subcellular locations: Plastid, Chloroplast stroma
ACCO_PERAE	Persea americana	MDSFPVINMEKLEGQERAATMKLINDACENWGFFELVNHSIPVELMDEVERLTKEHYKKCMEQRFKELMASKVEGAVVDANDMDWESTFFIRHLPVSNLSEIPDLTDEHRKVMKEFAEKLEKLAEQVLDLLCENLGLEKGYLKMAFAGTTTGLPTFGTKVSNYPPCPRPELFKGLRAHTDAGGLILLFQDDRVAGLQLLKDGEWVDVPPMNHSIVINLGDQVEVITNGKYKSVMHRVVAQTDGNRMSLASFYNPGSDAVIFPAPALVEKEAEEKKEVYPKFVFEDYMNLYAGLKFQAKEPRFEVMKMKAVETANLSPITT	null
ACCO_PRUMU	Prunus mume	MENFPIINLEGLNGEGRKATMEKIKDACENWGFFELVSHGIPTEFLDTVERLTKEHYRQCLEQRFKELVASKGLEAVKTEVNDMDWESTFYLRHLPKSNISEVPDLEDQYRNVMKEFALKLEKLAEQLLDLLCENLGLEKGYLKKAFYGTNGPTFGTKVSNYPPCPNPELIKGLRAHTDAGGLILLFQDDKVSGLQLLKDGQWIDVPPMRHSIVINLGDQLEVITNGKYRSVEHRVIAQTDGTRMSIASFYNPGSDAVIYPAPTLVEKEAEEKNQVYPKFVFEDYMKLYAGLKFQPKEPRFEAMKAVETNISLVPIATA	null
ATPA_MANES	Manihot esculenta	MVTIRADEISNIIRERIEQYNREVKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSRLGEGSMTALPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFVELEAFAQFASDLDKATQNQLARGQRLRELLKQSQSAPLTVEEQIMTIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAETLLKEAIQEQKERFVIQEQV	Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. Subcellular locations: Plastid, Chloroplast thylakoid membrane
ATPB_MANES	Manihot esculenta	MRINPTTSTSGPGVSALEKKNLGRIAQIIGPVLDVAFPPGKMPNIYNALVVKGRDTAGQEINVTCEVQQLLGNNRVRAVAMSATDGLTRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDDLGPVDTRATSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEENIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPQIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFKLILSGELDSLPEQAFYLVGNIDEATAKATNLEMENNLKK	Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. Subcellular locations: Plastid, Chloroplast thylakoid membrane
ATPE_DAUCA	Daucus carota	MTLNLCVLTPNRTVWNSKVNEIILSTNSGQIGVLPNHASVATAVDIGILKIRLDGQWLTMALMGGFAIIGNNEITVLVNDAEKGSDIDSQEAQQTLEIAEANFRKAEGKRQKIEANLALRRARTRVETINAIS	Produces ATP from ADP in the presence of a proton gradient across the membrane. Subcellular locations: Plastid, Chloroplast thylakoid membrane
ATPH_DAUCA	Daucus carota	MNPLISAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQPEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV	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. Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits. Subcellular locations: Plastid, Chloroplast thylakoid membrane
C79D2_MANES	Manihot esculenta	MAMNVSTTATTTASFASTSSMNNTAKILLITLFISIVSTVIKLQKRASYKKASKNFPLPPGPTPWPLIGNIPEMIRYRPTFRWIHQLMKDMNTDICLIRFGKTNVVPISCPVIAREILKKHDAVFSNRPKILCAKTMSGGYLTTIVVPYNDQWKKMRKVLTSEIISPARHKWLHDKRAEEADQLVFYINNQYKSNKNVNVRIAARHYGGNVIRKMMFSKRYFGKGMPDGGPGPEEIMHVDAIFTALKYLYGFCISDYLPFLEGLDLDGQEKIVLNANKTIRDLQNPLIEERIQQWRSGERKEMEDLLDVFITLQDSDGKPLLNPDEIKNQIAEIMIATIDNPANAVEWAMGELINQPELLAKATEELDRVVGKDRLVQESDIPNLNYVKACAREAFRLHPVAYFNVPHVAMEDAVIGDYFIPKGSWAILSRYGLGRNPKTWPDPLKYDPERHLNEGEVVLTEHDLRFVTFSTGRRGCVAALLGTTMITMMLARMLQCFTWTPPPNVTRIDLSENIDELTPATPITGFAKPRLAPHLYPTSP	Involved in the biosynthesis of the cyanogenic glucosides linamarin and lotaustralin. Can use L-valine or L-isoleucine as substrate. Subcellular locations: Microsome membrane Expressed in the epidermis, the next two cortex cell layers, the endodermis and the pericycle of leaf petioles. Strong expression around the laticifers among the phloem cells and in parenchymatic cells between the protoxylem and the metaxylem cells. In the leaves, preferentially expressed in the mesophyll cells adjacent to the epidermis.
CCBS_DAUCA	Daucus carota	MSIYELFHYSLFLGLFVAFTYNKKQPPVFGAALAFWCILLSFLGLSFRHIPNNLSNYNVLTANAPFFYQISGTWSNHEGSISLWCRILSFYGFLLCYRGRPQSHNVSKRGGHRETLFYSFVSNFVKNPILSLPRYEQKSRAAPQLYTPFVLRTFVDSELRSRRNRTFDGPALFYVYAPLYPERKMSFAPLGARLPVVRGEGKRMSLLLHLARDDKERASSIDEQRIDGALGIALFFSPFLSASSDPFVRNFFVRTEPLAESNPVPQDPISAIHPPCIYAGDVASAMGFGLCRSKMMNGIVALHSPPMRKDAAEKNGTLFRSAGCVGSRITSELFTLKFKHVGEKCYPALLLRSNRSPLMLLRRRFFALSSLWTGALVDTGREQAKRVVRNGKKDTTTSPLCWTAGANTVVSDQDQEPIRIWILTCRWFLNVGILLGSWWAHHELGRGGWWFRDPVENASFMPRVLATARIHSVILPLLHSWTSFLNIVTLPCCVSGTSSIRSGLLAPVHSFATDDTRGIFLWRFFLLMTGISMILFSQMKQQASVRRTYKKEMVMARSTLVHLRHSARAQPRPVMLWKN	Could be involved in assembly and maturation of cytochromes c. May play a role in guidance of apocytochromes and heme groups for the covalent linkage introduced by the cytochrome-c-heme lyase. Subcellular locations: Mitochondrion
CHSY_PERAE	Persea americana	MVNVEAIRKVQRAEGPATIMAIGTSTPPNAVDQSEYPDYYYFGSPTASTRPSSRRSFKRMCEKSMIKKRYMYLTETYWKRIQMFVPTWLLPLKARQDMVVVEVPKLGKEVQPKAIKGMGQPKSKINPLVFCTTSGVDMPGADYQLTKVFGLPPSVKRLMMYQQGCFAGGTVLRLAKDLAENNKGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFGDGAAALIVGADPVPGVENPMFELVSAGQTILPDSDGAIDGHLREVGLTFHLLKVVPGLISKNIEKSLVEAFEPLGISDWNSLFWIAHPGGPAILDPGGDQTRPEARESCGNQACFSVSMATCQVFVCSSFSTRCEGSPKEEGLKTTGEGIEWGVLFGFGPGLTVETVVLHSLPTH	The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin.
CONG1_PRUDU	Prunus dulcis	MASFLHNFLLFFCSLSLIILTSSATKSQTHVPIRPNKLVLKVQKDRATNLHVVQIHKRTPLVQFPFVIDLTGRFLSVNCENQYTSSTYKAPVCHSSQCARANSHTCRTCSSSKTRPGCHTNACGLLTTNPVTQQSAQGELAEDVLKIPSTQGSSPGPMVTYPHFLFACAPSNILQKGLPKNVQGVAGLGHSPISLPYQLASHFGFPPKFAVCLTSSPGKNGAVFFGEGPYFMKPGIDVSRQLTYAPFTIGQQGEYYINVQSFKINNAMLPSIPKGGFGGAMISTTTPYTTLQTPIFRALNQLFMNQLRGVPHVKPVAPFGACFDANRIPTSKMGPTVPSIDLVLDNKKNIMWRIFGANAMIQPRPGVMCLAFVDGGMRPKAPIVIGTQQLEDNLLQFDLMNSRLGFSSSLLFRRTNCANFNFGTSSTNTDP	Sulfur-rich seed storage protein that remains undegraded at germination. Subcellular locations: Secreted, Extracellular space Present in the extracellular spaces of germinating seedlings.
DAU1_DAUCA	Daucus carota	MGAQSHSLEITSSVSAEKIFSGIVLDVDTVIPKAAPGAYKSVEVKGDGGAGTVRIITLPEGSPITSMTVRTDAVNKEALTYDSTVIDGDILLGFIESIETHLVVVPTADGGSITKTTAIFHTKGDAVVPEENIKFADAQNTALFKAIEAYLIAN	null
DC103_DAUCA	Daucus carota	MGVQKHEQEITSSVPAEKMFHGLILDIDNILPKAAPGAYKNVEIKGDGGVGTIKHITLPDGGPVTTMTLRTDGLDKKGFTIDYSVIDGDVLMGFIDKIENHLSVVPTADGGSTTKTTAIFHTKGDAVVPEENIKYAEAQNTMLFKAVEAYLIAN	Expressed in roots.
DRO1_PRUPE	Prunus persica	MKLFGWMQNKLNGKQGNKKPNTVPITTHPAKQEPREEFSDWPHGLLAIGTFGNNDLKENAAESQDIQEDPTSSEEILDNFTPEEVGKLHKELTKLLTRKPNIEKEIADLPLDRFLNCPSSLEVDRRNSNALCSDSADDHKDEDIEKTISVILGRCKEICGDKNKKAIGKKSISFLLKKMFVCRSGFAPQPSLRDTLQESRMEKLLRVMLNKKIINPQGSSRAASMKKYLEDRQIPTKKESNTEDDTKEKINNGCKWVKTDSEYIVLEI	Involved in the development of the root system architecture by influencing lateral root angles and primary root length. Expressed in roots.
EF1A1_DAUCA	Daucus carota	MGKEKVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETNKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDPTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTPKYSKARYDEIVKEVSSYLKKVGYNPEKIAFVPISGFEGDNMIERSTNLDWYKGPTLLDALDQINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGTIKPGMVVTFGPSGLTTEVKSVEMHHESLLEALPGDNVGFNVKNVSVKDLKRGYVASNSKDDPAKGAASFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAELLTKIDRRSGKELEKEPKFLKNGDAGMVKMLPTKPMVVETFAEYPPLGRFAVRVMRQTVAVGVIKAVEKKDPTGAKVTKAAAKKGAK	This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. Subcellular locations: Cytoplasm
EMB1_DAUCA	Daucus carota	MASQQEKKELDARARQGETVVPGGTGGKSLEAQQHLAEGRSKGGQTRKEQLGGEGYHEMGRKGGLSNNDMSGGERAEQEGIDIDESKFRTKK	Subcellular locations: Nucleus Expressed in embryogenic cells, somatic embryos and seeds at the later stages of development. In the embryos, expressed in the procambium, the root and shoot meristem and the protoderm of the cotyledons. Not detected in the endosperm or the aleurone layer, in young leaves or roots.
EXTN_DAUCA	Daucus carota	MGRIARGSKMSSLIVSLLVVLVSLNLASETTAKYTYSSPPPPEHSPPPPEHSPPPPYHYESPPPPKHSPPPPTPVYKYKSPPPPMHSPPPPYHFESPPPPKHSPPPPTPVYKYKSPPPPKHSPAPVHHYKYKSPPPPTPVYKYKSPPPPKHSPAPEHHYKYKSPPPPKHFPAPEHHYKYKYKSPPPPTPVYKYKSPPPPTPVYKYKSPPPPKHSPAPVHHYKYKSPPPPTPVYKSPPPPEHSPPPPTPVYKYKSPPPPMHSPPPPTPVYKYKSPPPPMHSPPPPVYSPPPPKHHYSYTSPPPPHHY	Structural component in primary cell wall. Subcellular locations: Secreted, Primary cell wall
GUNX_PRUPE	Prunus persica	PEDMDTPRNVYKVSTQNPGSDVAAETAAALAAASIVFKDSDPSYSGKLLHTAMKVFDFADRYRGSYSDSIGSVVCPFYCSYSGHHDELLWGASWIHRASQNRSYLVYIKSNGHILGEDDDGFSASWDDKETGTKVLLVSKSFLERHVEEFQLYKAHSGNYICSLLPGTSNFQGQYTPGGLLYKASESNLQYVTSTTLLLLTYAKYLRTNGGVATCGSSKVTAETLISEAKKQVDYILGNNPAKISYMVGFG	Degrades carboxymethylcellulose (CMC).
HSP11_DAUCA	Daucus carota	MSIIPSFFGGRRSNVFDPFSLDVWDPFKDFPLVTSSASEFGKETAAFVNTHIDWKETPQAHVFKADLPGLKKEEVKVELEEGKVLQISGERNKEKEEKNDKWHRVERSSGKFLRRFRLPENAKVDEVKAAMANGVVTVTVPKVEIKKPEVKAIDISG	Subcellular locations: Cytoplasm
HSP12_DAUCA	Daucus carota	MSIIPSFFGSRRSNVLNPFSLDIWDPFQDYPLITSSGTSSEFGKETAAFANTHIDWKETPQAHVFKADLPGLKKEEVKVEVEEGKVLQISGERNKEKEEKNNKWHRVEFSSGKFLRRFRLPENANVDEVKAGMENGVLTVTVPKVEMKKPEVKSIHISG	Subcellular locations: Cytoplasm
NDHH_DAUCA	Daucus carota	MTAPATRNDLMIVNMGPQHPSMHGVLRLIVTLDGEDVIDCEPILGYLHRGMEKIAENRTIIQYLPYVTRWDYLATMFTEAITVNAPEQLGNIQVPKRASYIRVIMLELSRIASHLLWLGPFMADIGAQTPFFYIFRERELIYDLFEAATGMRMMHNFFRIGGVAADLPHGWIDKCLDFCDYFLTRVTEYQRLITRNPIFLERVEGVGIIGGEEAINWGLSGPMLRASGIQWDLRKVDHYESYDEFDWGVQWQKEGDSLARYLVRISEMTESVKIIQQALEGITGGPYENLEIRRFDKVWDPEWNDFDYRFISKKPSPTFELSKQELYVRVEAPKGELGIFLIGDKGIFPWRWKIRPPGFINLQILPQLVKRMKLADIMTILGSIDIIMGEVDR	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. Subcellular locations: Plastid, Chloroplast thylakoid membrane
OLEO1_PRUDU	Prunus dulcis	MADQHFQQPLHFQGSYGQQQPRSYQVAKAATAVTAGGSLLVLSGLVLAGTVIALTIATPLLVIFSPVLVPALITVALITMGFLTSGGFGVAAVTVLSWIYKYVTGKQPPGADQLDQARHKLAGKARDIKDRAEQFGQQHVPSGQQQSS	May have a structural role to stabilize the lipid body during desiccation of the seed by preventing coalescence of the oil. Probably interacts with both lipid and phospholipid moieties of lipid bodies. May also provide recognition signals for specific lipase anchorage in lipolysis during seedling growth (By similarity). Subcellular locations: Lipid droplet, Membrane Surface of oil bodies. Oleosins exist at a monolayer lipid/water interface.
PER1_DAUCA	Daucus carota	WNETSDKDLYTDSR	Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
PETN_DAUCA	Daucus carota	MDIVSLAWAALMVVFTFSLSLVVWGRSGL	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. Subcellular locations: Plastid, Chloroplast thylakoid membrane
PGLR_PERAE	Persea americana	MALTRLLLPISILWFCFYSSHTILQKDPLLICVNGDPGFDQRAYPTYFGPILDEFSSIMGFEPSILSLERFNPVGGPETSPDTDISVDDFGARGDGTDDTKAFEKAWKDACSSGSVLIVPENKNYLLKQITFSGPCKSDLRVKIRGTIEASSDQSDWVGHNRKRWIEFEDISNLTLEGGGTSNGNGETWWDSSCKRKKSLPCKSAPTALTFRSCKNLIVSDLSIKDSQKMHLSFDKCQDVIASNLMVTAPEHSPNTDGIHITGTQRIHVMNSVIGTGDDCISIESGSKMVIATNITCGPGHGISIGSLGDRNSEAHVSGVLVDGGNLFDTTNGLRIKTWQGGSGSAKNIKFQNIVMHNVTNPIIIDQYYCDSKDPCPEQESAVKVSNVAYMNIRGTSASEVAVKFDCSKSSPCQGYIVGNINLVGNGGKETTMSCSNIVQGLLREGLSTFLFMKRRVHECSY	Acts in concert with the pectinesterase, in the ripening process. Is involved in cell wall metabolism, specifically in polyuronide degradation. Subcellular locations: Secreted, Secreted, Cell wall
PGLR_PRUPE	Prunus persica	MANRRSLFSLSLIFVFMINSAIASPLTYNVASLGAKADGKTDSTKAFLSAWAKACASMNPGVIYVPAGTFFLRDVVFSGPCKNNAITFRIAGTLVAPSDYRVIGNAANWIFFHHVNGVTISGGILDGQGTALWACKACHGESCPSGATTLGFSDSNNIVVSGLASLNSQMFHIVINDFQNVQMQGVRVSRSGNSPNTDGIHVQMSSGVTILNSKIATGDDCVSIGPGTSNLWIEGVACGPGHGISIGSLGKEQEEAGVQNVTVKTVTFSGTQNGLRIKSWGRPSTGFARNILFQHATMVNVENPIVIDQHYCPDNKGCPGQVSGVQISDVTYEDIHGTSATEVAVKFDCSPKHPCREIKLEDVKLTYKNQAAESSCSHADGTTEGVVQPTSCL	Acts in concert with the pectinesterase, in the ripening process. Is involved in cell wall metabolism, specifically in polyuronide degradation. Subcellular locations: Secreted, Secreted, Cell wall
PRU01_PRUDU	Prunus dulcis	MAKAFVFSLCLLLVFNGCLAARQSQLSPQNQCQLNQLQAREPDNRIQAEAGQIETWNFNQEDFQCAGVAASRITIQRNGLHLPSYSNAPQLIYIVQGRGVLGAVFSGCPETFEESQQSSQQGRQQEQEQERQQQQQGEQGRQQGQQEQQQERQGRQQGRQQQEEGRQQEQQQGQQGRPQQQQQFRQFDRHQKTRRIREGDVVAIPAGVAYWSYNDGDQELVAVNLFHVSSDHNQLDQNPRKFYLAGNPENEFNQQGQSQPRQQGEQGRPGQHQQPFGRPRQQEQQGSGNNVFSGFNTQLLAQALNVNEETARNLQGQNDNRNQIIRVRGNLDFVQPPRGRQEREHEERQQEQLQQERQQQGGQLMANGLEETFCSLRLKENIGNPERADIFSPRAGRISTLNSHNLPILRFLRLSAERGFFYRNGIYSPHWNVNAHSVVYVIRGNARVQVVNENGDAILDQEVQQGQLFIVPQNHGVIQQAGNQGFEYFAFKTEENAFINTLAGRTSFLRALPDEVLANAYQISREQARQLKYNRQETIALSSSQQRRAVV	Seed storage protein. Expressed in seed (at protein level) (, ).
PRU1_PRUAR	Prunus armeniaca	MGVFTYETEFTSVIPPEKLFKAFILDADNLIPKVAPTAVKGTEILEGDGGVGTIKKVTFGEGSQYAYVKHRVDGIDKDNLSYSYTLIEGDALSDVIENIAYDIKLVASPDGGSIVKTTSHYHTKGDVEIKEEQVKAGKEKAAGLFKLVEAYLLANPDAYN	null
PRU1_PRUAV	Prunus avium	MGVFTYESEFTSEIPPPRLFKAFVLDADNLVPKIAPQAIKHSEILEGDGGPGTIKKITFGEGSQYGYVKHKIDSIDKENYSYSYTLIEGDALGDTLEKISYETKLVASPSGGSIIKSTSHYHTKGNVEIKEEHVKAGKEKASNLFKLIETYLKGHPDAYN	null
PRU1_PRUDU	Prunus dulcis	MAKAFVFSLCLLLVFNGCLAARQSQLSPQNQCQLNQLQAREPDNRIQAEAGQIETWNFNQGDFQCAGVAASRITIQRNGLHLPSYSNAPQLIYIVQGRGVLGAVFSGCPETFEESQQSSQQGRQQEQEQERQQQQQGEQGRQQGQQEQQQERQGRQQGRQQQEEGRQQEQQQGQQGRPQQQQQFRQLDRHQKTRRIREGDVVAIPAGVAYWSYNDGDQELVAVNLFHVSSDHNQLDQNPRKFYLAGNPENEFNQQGQSQPRQQGEQGRPGQHQQPFGRPRQQEQQGNGNNVFSGFNTQLLAQALNVNEETARNLQGQNDNRNQIIQVRGNLDFVQPPRGRQEREHEERQQEQLQQERQQQGEQLMANGLEETFCSLRLKENIGNPERADIFSPRAGRISTLNSHNLPILRFLRLSAERGFFYRNGIYSPHWNVNAHSVVYVIRGNARVQVVNENGDAILDQEVQQGQLFIVPQNHGVIQQAGNQGFEYFAFKTEENAFINTLAGRTSFLRALPDEVLANAYQISREQARQLKYNRQETIALSSSQQRRAVV	Seed storage protein. Expressed in seed (at protein level) ( ). Expressed in seed .
PSBC_DAUCA	Daucus carota	MKTLYSLRRFYPVETLFNGTLALAGRDQETTGFAWWAGNARLINLSGKLLGAHVAHAGLIVFWAGGMNLFEVAHFVPEKPMYEQGLILLPHLATLGWGVGPGGEVIDTFPYFVSGVLHLISSAVLGFGGIYHALLGPETLEESFPFFGYVWKDRNKMTTILGIHLILLGIGAFLLVFKALYFGGVYDTWAPGGGDVRKITNLTLNPSIIFGYLLKSPFGGEGWIVSVDDLEDIIGGHVWLGSICIFGGIWHILTKPFAWARRALVWSGEAYLSYSLAALSVFGFIACCFVWFNNTAYPSEFYGPTGPEASQAQAFTFLVRDQRLGANVGSAQGPTGLGKYLMRSPTGEVIFGGETMRFWDLRAPWLEPLRGPNGLDLSRLKKDIQPWQERRSAEYMTHAPLGSLNSVGGVATEINAVNYVSPRSWLATSHFVLGFFLFVGHLWHAGRARAAAAGFEKGIDRDFEPVLSMTPLN	One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. Subcellular locations: Plastid, Chloroplast thylakoid membrane
PSBD_MANES	Manihot esculenta	MTIALGKFTKDENDLFDIMDDWLRRDRFVFVGWSGLLLFPCAYFAVGGWFTGTTFVTSWYTHGLASSYLEGCNFLTAAVSTPANSLAHSLLLLWGPEAQGDFTRWCQLGGLWTFVALHGAFGLIGFMLRQFELARSVQLRPYNAIAFSGPIAVFVSVFLIYPLGQSGWFFAPSFGVAAIFRFILFFQGFHNWTLNPFHMMGVAGVLGAALLCAIHGATVENTLFEDGDGANTFRAFNPTQAEETYSMVTANRFWSQIFGVAFSNKRWLHFFMLFVPVTGLWMSALGVVGLALNLRAYDFVSQEIRAAEDPEFETFYTKNILLNEGIRAWMAAQDQPHENLIFPEEVLPRGNAL	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/PsbD) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. D2 is needed for assembly of a stable PSII complex. Subcellular locations: Plastid, Chloroplast thylakoid membrane
PSBM_DAUCA	Daucus carota	MEVNILAFIATALFILVPTAFLLIIYVKTETQNKNKKD	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. This subunit is found at the monomer-monomer interface. Subcellular locations: Plastid, Chloroplast thylakoid membrane
PSMD3_DAUCA	Daucus carota	MTQDVEMKEVPAPAPSNSVTAATPSTLQHLKEIASLIESGAYAREVRRILRAVRLTIALRKKLNASVVNAFLNFSLVPGSEVHARLASYLPKEDEHDMEVDTAMSATTTLAKHSLPELEIYCYLLVLIFLIDQKKYSEAKACSSASIARVKNLNRRTVEVLASRLYFYYSLSYELTGDLAEIRGNLLALHRIATLRHDELGQETLLNLLLRNYLHYNLYDQAEKLRSKAPRFEAHSNQQFCRYLFYLGKIRTIQLEYTDAKESXLQAARKAPVAALGFRVQCNKWAVIVRLLLGEIPERTVFMQKGMEKALRPYFXLTNAVRIGDLELFRXVADKFASTFTADRTHNLIVRLRHNVIRTGLRNISISYSRISLVDVARKLRLDSPNPVADAESIVSKAIRDGAIDATIDHANGWMVSKETGDIYSTNEPQAAFNSRIAFCLNMHNEAVRALRFPANSHKDKESAEKRRERQQQEQELAKHIAEEDDDEF	Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. Subcellular locations: Nucleus
RK20_MANES	Manihot esculenta	MTRIRRGYIARRRRTKIRLFASSFRGAHSRLTRTIIQQKIRALVSAHRDRDRQKRNFRRLWVTRINAVIRESTVSYSYSRLINNLYKRQLLLNRKILAQIAILNRNCLYMISNDILK	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. Subcellular locations: Plastid, Chloroplast
RK2_DAUCA	Daucus carota	MAIHLYKTSTPSTRNRTVDSRVKSNPRNNLIYGQHRCGKGRNARGIITAGHRGGGHKRLYRKIDFRRNEKDIYGRIVTIEYDPNRNAYICLIHYGDGEKRYILHPRGAIIGDTIVSGTEVPIKMGNALPLTDMPLGTAIHNIEITRGRGGQLARAAGAVAKLIAKEGKSATLKLPSGEVRLISKNCSATVGQVGNVGVNQKSLGRAGSKRWLGKRPVVRGVVMNPVDHPHGGGEGRAPIGRKKPTTPWGYPALGRRSRKRNKYSDNLILRRRSK	Subcellular locations: Plastid, Chloroplast
RL12_PRUAR	Prunus armeniaca	MPPKFDPSQVVDVYVRVTGGEVGAASSLAPKIGPLGLSPKKIGEDIAKETANDWKGLRVTVKLTVQNRQAKVSVVPSAAALVIKALKEPERDRKKTKNIKHSGHISLDDVIEIAKIMKHRSMAKELAGTVKEILRTCVSVGCTVDGKDPKDLQQEIADGDVEIPLD	This protein binds directly to 26S ribosomal RNA.
RL36_DAUCA	Daucus carota	MAPKQPNTGLFVGLNKGHIVTKKELAPRPSDRKGKTSKRTHFVRNLIREVAGFXPYEKRITELLKVGKDKRALKVRQEKVGHSQESKEEERGDVQCSPPDEGWWWY	null
RR18_DAUCA	Daucus carota	MDKSKRPFLKSKRSFRRRLPPIQSGDRIDYRNMSLISRFISEQGKILSRRVNRLTLKQQRLITIAIKQARILSLLPFLNNEKQFERTESTTRTAGLRARNK	Subcellular locations: Plastid, Chloroplast

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GreenBeing Proteins dataset

Proteins from UniProtKB (knowledge base), from select food crops and related species.
Amino acid sequences use IUPAC-IUB codes where letters A-Z map to amino acids.

Usage (due to different schema on splits):

load_dataset("monsoon-nlp/greenbeing-proteins", "pretraining", split="pretraining")

XML source from https://www.uniprot.org/help/downloads
CoLab notebook: https://colab.research.google.com/drive/1M6sO0Ws6i5z9VUXIXopiOqo1OkQ7K-1g?usp=sharing

Pretraining split

Amino acid sequences for unreviewed proteins (TrEMBL)

Each row contains a species or subspecies name (for filtering), and the amino acid sequence of a protein. Large proteins are split into a new row every 8,000 letters.

Share of taxa

In the pretraining split:

31% Papilionoideae/Faboideae (soybeans, peas, pulses, peanuts)
19% Triticeae (wheat, barley, rye, and relatives)
17% Oryzeae (rice, wild rice, and relatives)
12% Paniceae (most millets)
6% Solanum (potatoes, tomatoes, other nightshades, etc.)
5% Zea (corn/maize)
2% Sorghum
2% Lactuca sativa (lettuce)
2% Capsicum (chili peppers)
2% Cucurbita (squash, pumpkins)
0.8% Spinacia
0.7% Asparagus
0.2% Beta vulgaris (beet)
0.1% Bambusa (includes edible bamboo shoots)

Finetuning split

Reviewed proteins (Swiss-Prot) from above taxa. Each row contains a gene name, species or subspecies, an amino acid sequence, and comments / annotations available in UniProt.

A gene name may match multiple entries on UniProt from different accessions.

Annotations may be empty, or may include information such as:

likely function, written in English
location inside of cell (e.g. "Subcellular locations: Vacuole")
locations in the plant (e.g. "Expressed in roots, stems")

Removed PubMed reference numbers to avoid training models to hallucinate PubMed references.

In the current state of plant genomics research, about half of the finetuning split are from rice and related species, a fifth are from Papilionoideae/Faboideae, and seven taxa have less than 1% each.

Evaluation split

Reviewed proteins (Swiss-Prot) from other genera (avocado, carrot, cassava, lychee, prunus (i.e. peaches, cherries, plums)). Each row contains a gene name, species or subspecies, an amino acid sequence, and comments / annotations available in UniProt.

A gene name may match multiple entries on UniProt from different accessions.

Annotations may be empty, or may include information such as:

likely function, written in English
location inside of cell (e.g. "Subcellular locations: Vacuole")
locations in the plant (e.g. "Expressed in roots, stems")

Removed PubMed reference numbers to avoid training models to hallucinate PubMed references.

Research split

Proteins from quinoa (~99%), cañihua, and the three species of amaranth which are currently grown for grain.

Columns contain UniProt/TrEMBL gene names, species, and the amino acid sequence. Large proteins are split into a new row every 8,000 letters.

Limitations and Safety Notes

Proteins and review status on UniProt are from March 29, 2024.

You should at least pretrain on more than Oryza sativa, because its reviewed proteins are probably some of the most common/important.

Understanding reviewed/unreviewed proteins: https://www.uniprot.org/help/uniprotkb_sections

The reviewed sequences are often similar to unreviewed sequences from related species and accessions, and are not suitable to test predicting/infilling/completion.

Species include inedible wild relatives.
Some people have allergic reactions to wheat/gluten, nightshades, maize, lychee, and other crops.
Chili peppers can be painfully spicy.

Downloads last month: 23

Edit dataset card

Size of downloaded dataset files:

1.56 GB

Size of the auto-converted Parquet files:

1.34 GB

Number of rows:

3,949,406

Models trained or fine-tuned on monsoon-nlp/greenbeing-proteins

Collection including monsoon-nlp/greenbeing-proteins

Bio Series

Collection

Embeddings and NLG related to biology / amino acid sequences • 10 items • Updated 24 days ago • 1