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 |