protein_name
stringlengths 8
11
| species
stringclasses 13
values | sequence
stringlengths 5
2.31k
| annotation
stringlengths 19
1.16k
⌀ |
|---|---|---|---|
UGTK5_MANES | Manihot esculenta | MGSLASEIPPHAVLVPYPAQGHVNPLMQLGKLLHSRGFYITFVNTEHNHRRLIRSRGQEFIDGLPDFKFEAIPDGLPYTDRDATQHVPSLSDSTRKHCLAPFIDLIAKLKASPDVPPITCIISDGVMAFAIDAARHFGIPEIQFWTTSACGFMAYLHHIELVRRGIVPFKDESFLHDGTLDQPVDFIPGMPNMKLRDMPSFIRVTDVNDIMFDFMGSEAHKSLKADAIILNTYDELEQEVLDAIAARYSKNIYTVGPFILLEKGIPEIKSKAFRSSLWKEDLSCIEWLDKREPDSVVYVNYGCVTTITNEQLNEFAWGLANSKHPFLWIVRPDVVMGESAVLPEEFYEAIKDRGLLVSWVPQDRVLQHPAVGVFLSHCGWNSTIECISGGKPMICWPFFAEQQTNCKYACDVWKTGVELSTNLKREELVSIIKEMMETEIGRERRRRAVEWRKKAEEATSVGGVSYNNFDRFIKEAILQHKTK | UDP-glucosyltransferase catalyzing in planta synthesis of cyanogenic glucosides. Able to glucosylate acetone cyanohydrin and 2-hydroxy-2-methylbutyronitrile, forming linamarin and lotaustralin. Accepts also to some extent, a wide range of potential acceptor substrates, including simple alcohols, flavonoids, isoflavonoids and other hydroxynitriles such as p-hydroxymandelonitrile, mandelonitrile, (E)-4-hydroxy-2-methylbut-2-enenitrile and (E)- 2-(hydroxymethyl)but-2-enenitrile.
Expressed in the cortex, xylem and phloem parenchyma, and in specific cells in the endodermis of the petiole of the first unfolded leaf. |
UP01_DAUCA | Daucus carota | YGLAGDHVLDAR | null |
VATA_DAUCA | Daucus carota | MPSVYGDRLTTFEDSEKESEYGYVRKVSGPVVVADGMGGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGILGNIFDGIQRPLKTIAKRSGDVYIPRGVSVPALDKDTLWEFQPKKIGEGDLLTGGDLYATVFENSLMQHHVALPPDAMGKITYVAPAGQYSLKDTVLELEFQGVKKQFTMLQTWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDTVVYVGCGERGNEMAEVLMDFPQLTMTLPDGREESVMKRTTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKCLGGPERNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALESFYEKFDSDFIDIRTKAREVLQREDDLNEIVQLVGKDALAETDKITLETAKLLREDYLAQNAFTPYDKFCPFYKSVWMMRNIIHFYNLANQAVERGAGMDGQKISYTLIKHRLGDLFYRLVSQKFEDPAEGEDVLVGKFKKLHDDLTSGFRNLEDETR | Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. |
B2_DAUCA | Daucus carota | MIDQEESNFNFNFNQPQQPQQQQFHGKSVKKNKNKNNNNNSESGNKNGGENKNGVEKRFKTLPPAESLPRNETVGGYIFVCNNDTMQENLKRQLFGLPPRYRDSVRAITPGLPLFLYNYSTHQLHGVFEAASFGGTNIDPTAWEDKKNQGESRFPAQVRVMTRKICEPLEEDSFRPILHHYDGPKFRLELNIPEAISLLDIFEETKA | null |
C71E7_MANES | Manihot esculenta | MSVAILTSLPPQWLSILAVFLLPILTLLLFRGKDDNQKKGLKLPPGPRQLPLIGNLHQLGGQPYVDFWKMAKKYGPVMYLQLGRCPTVVLSSTETSKELMKDRDVECCSRPLSVGPGQLSYNFLDVAFSPYSDYWREMRKLFIFELLSMRRVQTFWYAREEQMDKMIEILDGAYPNPVNLTEKVFNMMDGIIGTIAFGRTTYAQQEFRDGFVKVLAATMDMLDNFHAENFFPVVGRFIDSLTGALAKRQRTFTDVDRYFEKVIEQHLDPNRPKPETEDIVDVLIGLMKDESTSFKITKDHVKAILMNVFVGGIDTSAVTITWAFSELLKNPKLMKKAQEEVRRAVGPNKRRVEGKEVEKIKYIDCIVKETFRKHPPVPLLVPHFSMKHCKIGGYDILPGTTIYVNAWAMGKDPTIWENPEEYNPDRFMNSEVDFRGSDFELVPFGAGRRICPGLAMGTTAVKYILSNLLYGWDYEMPRGKKFEDFPLIEEGGLTVHNKQDIMVIPKKHKWD | Catalyzes the conversion of (E)-2-methylpropanal oxime (valox) to 2-hydroxy-2-methylpropanenitrile (acetone cyanohydrin) and of (E)-2-methylbutanal oxime (ilox) to 2-hydroxy-2-methylbutyronitrile. The reaction takes place in three steps. First, the oxime is isomerized to the (Z)- isomer, next the (Z)-isomer is dehydrated to the corresponding nitrile, followed by a C-hydroxylation of the nitrile. Can use both aliphatic and aromatic oximes as substrates.
Subcellular locations: Microsome membrane
Expressed in storage roots, primary roots, petioles and vascular tissues. Expressed in the outer cortex cells, the endodermis and around the xylem, phloem cells and laticifers. |
CCNAL_DAUCA | Daucus carota | APSMTTPEPASKRRVVLGEISNNSSAVSGNEDLLCREFEVPKCVAQKKRKRGVKEDVGVDFGEKFDDPQMCSAYVSDVYEYLKQMEMETKRRPMMNYIEQVQKDVTSNMRGVLVDWLVEVSLEYKLLPETLYLAISYVDRYLSVNVLNRQKLQLLGVSSFLIASKYEEIKPKNVADFVDITDNTYSQQEVVKMEADLLKTLKFEMGSPTVKTFLGFIRAVQENPDVPKLKFEFLANYLAELSLLDYGCLEFVPSLIAASVTFLARFTIRPNVNPWSIALQKCSGYKSKDLKECVLLLHDLQMGRRGGSLSAVRDKYKKHKFKCVSTLSPAPEIPESIFNDV | Essential for the control of the cell cycle at the G2/M (mitosis) transition. Interacts with the CDC2 and CDK2 protein kinases to form MPF. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed at mitosis. |
CCSA_DAUCA | Daucus carota | MIFSTLEHILTHISFSIVCIVITIHLITLLIDEIIKLNNSSEKGMIATFLCITVLLVTRCIYSGHLPLSDLYESLIFLSWSLSFIHIVPYFKKNKSHLSTITASSVIFTQGFATSGLLTEIHQSAILVPALQSEWLIMHVSMMILGYAALLCGSLLSVALLVLTFRKNRNLLCKKNPLLLKLTEEFSFGEIQYINEINNIFGNASFFSDNNYYRSQLIQQLDYWSYRVISLGFIFLTIGILSGAVWANEAWGSYWNWDPKETWAFITWIVFAVYLHTRTNTNLQVENSAIVASMGFLIIWICYFGVNLLGIGLHTYGSFTLTSN | Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
CRTSO_DAUCA | Daucus carota | MSTSIFETPLPRSDLFLCSNSLLSQNYKLFDNSRSFGLKSLRPRCQKDGLLYPKPLNFGFCRVSRRKRKPNFVLNSVLSVDKELESDETVGLGRSREYDAIVIGSGIGGLVAATQLAVKGAKVLVLEKYLIPGGSSGYYERDGFTFDVGSSVMFGFSDKGNLNLITQALAAVGCKMEVIPDPSTVHFHLPSNLSVLVHREYNEFFSELTSKFPHEKEGIFKFYGECWKIFNALNSLELKSLEEPIYLFGQFFKKPMECLTLAYYLPQNAGDIARKFIKDPEVLSFIDAECFIVSTVNALKTPMINASMVLCDRHYGGINYPVGGVGGIAKSLAKGLVDQGSEIQYKANVKSIIVENGKAVGVRLANGNEIFAKNIISNATRWDTFGKLLKQDELPKEEENFQKLYIKAPSFLSIHLGVKSDVLPPDTDCHHFVLEDDWSNLEVPYGSIFLSIPTVLDSSLAPEGNHILHIFTTSSIEDWQGMSQKDYEKKKELVADEIISRLEKKLFPGLQSSIVLKEVGTPKTHRRYLARDSGTYGPMPQGTPKGLLGMPFNTTAIDGLYCVGDSCFPGQGVIAVAFSGVMCAHRVAADLGLEQKSPILDAALLRLLGWFRTLA | Carotene cis-trans-isomerase that converts 7,9,9'-tri-cis-neurosporene to 9'-cis-neurosporene and 7,9,9',7'-tetra-cis-lycopene (also known as prolycopene) into all-trans-lycopene. Isomerization requires redox-active components, suggesting that isomerization is achieved by a reversible redox reaction acting at specific double bonds. Isomerizes adjacent cis-double bonds at C7 and C9 pairwise into the trans-configuration, but is incapable of isomerizing single cis-double bonds at C9 and C9' (By similarity).
Subcellular locations: Plastid, Chloroplast membrane |
GRDH_DAUCA | Daucus carota | MASGGQFPPQKQESQPGKEHLMDPSPQHASPHYKPANKLQGKVALVTGGDSGIGRSVCYHFALEGATVAFTFVKGHEDKDANETLELLRKAKSSDAKDPIAIAADLGFDDNCKKVVDQVVNAFGSIDVLVNNAAEQYKASTVEDIDEERLERVFRTNIFAYFFMARHALKHMREGSTIINTTSINAYKGNAKLLDYTATKGAIVAFTRGLSLQLISKGIRVNGVAPGPVWTPLIPSSFDEEEVKQFGSEVPMKRAGQPYEIATAYVFLASCDSSYYSGQVLHPNGGAIVNG | May act as a short alcohol-polyol-sugar dehydrogenase possibly related to carbohydrate metabolism and the acquisition of desiccation tolerance. May also be involved in signal transduction.
Expressed in embryogenic cells, somatic embryos and seeds in the later stages of development, but not in non-embryogenic cells and mature leaves. |
HSP70_DAUCA | Daucus carota | MASKGGKAIGIDLGTTYSCVGVWQNDRVEIIANDQGNRTTPSYFAFTDTSRLIGDAKNQVAMNPSNTVFDAKRLIGRRFNHPSVQSDMKLWPLQVIPGPGEKPMIVVNYKGESKQFAAEEISSMVLIKMLEIAEAFLGHSVNDAVVTVPAYFNDSQRQATKDTGVIAGLNVMRIINEPNCAQIAYGLDKKSSNPPEQNVLIFDLGGGTFDVSLLTIEEGIYEVKAPKSDTHLGGEDFDNRLVNRFVTEFLTNNKKDIRWECEALRRLRTACERAKRTLSSSTAQTTIEIDSLYEGVDFYTTITRARFEELNMDLFKKCMDPVEKCLRDSKIDKAQVHEVVLVGGSTRIPKVQQLLQDFFNGKELCKSINPDEAVAYGAAVQAAILSGEGNERSDLLLLDVTPLSLGLETAGGVMTVLIPRNTTIPTKKEQIFSTYSDNQPGVLIQVYEGERARTRDNKLLGKLLGKFELTGIPPAPRGVPQINVVFDIDANGILNVFAEDKTAGVKNKITITNDNGRLSKDEIEKLVKEAEKYKAEDEEVKKKVEAKNALENYAYNMRNTIKDDKIPGKLDAGDKEKIETAVNEAIEWLEKNQLAEVDELEDKLKELEGLCNPIIARLYQGRGDVPIGGPGDMPGGGYGGSRGSSGAGPKIEEVD | null |
LEAD3_DAUCA | Daucus carota | MASHQDQSYKAGEPKGHAQEKTGQMADTMKDKAQAAKDKASEMAGSARDRTVESKDQTGSYVSDKAGAVKDKTCETAQAAKEKTGGAMQATKEKASEMGESAKETAVAGKEKTGGLMSSAAEQVKGMAQGATEAVKNTFGMAGADEEEKTTTTRVTRSSARTE | null |
LEAD8_DAUCA | Daucus carota | MASRKDERAAKEERAQAAAELAAKELRDVNQDRERGIKVVEHKEEVSGGPGVIGSILKSVQGTLGQAKEVVVGKAHDTAEVSRENTDYAYDKGREGGDVAAQKAEEAKEKAKMAKDTTMGKAGEYKDYTAQKAEEAKEKAAQKAEETKEKAGEYKNYTAQKAGEAKDTTLGKAGEYKDYAAQKAAEAKDTTAQKAAEAKEKTGEYKDYAAQKAAEAKVLAAQKAAEAKDTTGKDGEYKDYAAQKAAEAKDATMQKTGEYKDYAAQKTAETKDATMEKAKEYKEYAAQKAAEAKDATMQKTGEYKDYSAQKAAETKDATMEKTKEYKDYTAQKAAETKDATMEKAKEAKDTTVQKTGEYKDYAAEKAKEGKDVTVEKAKEGKDTTVGKMTELKDSAADAARKAMDMFLGKKEEVKGKAGETAEAAKEKYEDTEFAARKKMEELKLQEEGVKDEAKQRAEADRETAGDRGSAAKGTIFGAMGSVKDAIVGKLTMPSDVVKDKQQQEAVIKVDETRPGAVAEALKAADQMHGQAFNDVGKMGDEEVIVERKETRQGKM | May play a role in late embryogeny.
Subcellular locations: Cytoplasm, Secreted, Cell wall
Cytoplasmic, protein bodies, and cell walls of zygotic embryo and endosperm tissue. |
MDL2_PRUDU | Prunus dulcis | MEKSTMSAILLVLYIFVLHLQYSEVHSLATTSDHDFSYLSFAYDATDLELEGSYDYVIVGGGTSGCPLAATLSEKYKVLVLERGSLPTAYPNVLTADGFVYNLQQEDDGKTPVERFVSEDGIDNVRGRVLGGTSIINAGVYARANTSIYSASGVDWDMDLVNQTYEWVEDTIVYKPNSQSWQSVTKTAFLEAGVHPNHGFSLDHEEGTRITGSTFDNKGTRHAADELLNKGNSNNLRVGVHASVEKIIFSNAPGLTATGVIYRDSNGTPHQAFVRSKGEVIVSAGTIGTPQLLLLSGVGPESYLSSLNIPVVLSHPYVGQFLHDNPRNFINILPPNPIEPTIVTVLGISNDFYQCSFSSLPFTTPPFGFFPSASYPLPNSTFAHFASKVAGPLSYGSLTLKSSSNVRVSPNVKFNYYSNLTDLSHCVSGMKKIGELLSTDALKPYKVEDLPGVEGFNILGIPLPKDQTDDAAFETFCRESVASYWHYHGGCLVGKVLDGDFRVTGINALRVVDGSTFPYTPASHPQGFYLMLGRYVGIKILQERSASDLKILDSLKSAASLVL | Involved in cyanogenesis, the release of HCN from injured tissues. Catalyzes the stereospecific addition of HCN to a variety of aldehydes in vitro. Has no oxidase activity. The redox properties of the FAD cofactor appear to be unimportant for catalysis. |
MDL2_PRUSE | Prunus serotina | MVKSTMSAILVLALHLFVLHLQYSEVQSLANTSAHDFSYLEFVYDANDTELEGTYDYIIVGGGTAGCPLAATLSANYSVLVLERGTLPTEYPNLLTSDGFIYNLQQEDDGQTPVERFVSGDGIDNVRGRVLGGTSMINAGVYVRANTSFFNQTGIEWDMDLVNKTYDWVEDTIVFKPDFQFWQNLTGTAFLEVGILPDNGFSLDHLEGTRLTGSTFDNNGTRHASDELLNKGDPNNLRVAVHAAVEKIIFSSDSSGVTAIGVIYTDSNGTTHQAFVRGDGEVILSAGPIGSPQLLLLSGVGLESYLTSLNISVVASHPYVGQYIYDNPRNFINILPPNPIEASTVTVLGITSDFYQCSISSLPFSTAPFGFFPNPTYPLPNTTFAHIVNKVPGPLSHGTVLLQSTSDVRVAPNVTFNYYSNTTDLAHCVSGMKKIGEFLSSDALKPYKVEDLPGIEGFDILGIPLPENQTDDAAFETFCREAVASYWHYHGGCLVGEVLDDDFRVTGINALRVVDGSTFPSTPASHPQGFYLMLGRYMGTKILQERLASEEALHKSTFEPKILESLESALSFAFES | Involved in cyanogenesis, the release of HCN from injured tissues. Catalyzes the stereospecific addition of HCN to a variety of aldehydes in vitro. It is a major seed constituent, and could have the additional role of a storage form for reduced nitrogen (By similarity).
Subcellular locations: Vacuole, Aleurone grain
Primarily found within protein bodies of the cotyledonary parenchyma cells, with lesser amounts within the procambium. |
MDL3_PRUSE | Prunus serotina | MVKSTMSAVLLVLHIFVLHLQYSEVQSLANTSSHDFSYLSFVYDATDPELEGSYDYIIVGGGTAGCPLAATLSANYSVLVLERGSLPTEYPNLLISDGFVYNLQQEDDGKTPVERFVSEDGIDNVRGRVLGGTSMINAGVYVRANTSFFNQTGIEWDMDLVNQTYEWVEDTIVFEPDSQTWQTVIGTAYLEAGILPNNGFSVDHLAGTRLTGSTFDNNGTRHASDELLNKGDPNNLRVAVQAAVEKIIFSSNTSGVTAIGVIYTDSNGTTHQAFVRGEGEVILSAGPIGSPQLLLLSGVGPESYLTSLNISVVASHPYVGQYIYDNPRNFINILPPNPIEASTVTVLGITSDFYQCSISSLPFDTPPFSFFPTTSYPLPNQTFAHIVNKVPGPLSHGTVTLNSSSDVRVGPNVKFNYYSNLTDLSHCVSGMKKLGEVLSTDALEPYKVEDLPGIDGFNILGIPLPENQTDDAAFETFCRESVASYWHYHGGCLVGKVLDDGFRVTGINALRVVDGSTFPSTPASHPQGFYLMLGRYMGIQILQERSASEDAIRNLGFQENILDSPKSTSSFAF | Involved in cyanogenesis, the release of HCN from injured tissues. Catalyzes the stereospecific addition of HCN to a variety of aldehydes in vitro. It is a major seed constituent, and could have the additional role of a storage form for reduced nitrogen.
Subcellular locations: Vacuole, Aleurone grain
Primarily found within protein bodies of the cotyledonary parenchyma cells, with lesser amounts within the procambium. |
MDL4_PRUSE | Prunus serotina | MEKSTMSAVVLVLNLLVLHLQYSEVHSLANTSSEHDFGYLKFVYNAVDLELEGSYDYIIVGGGTSGCPLAATLSANYSVLVLERGTIATEYPNTLTVDGFAYNLQQQDDGKTPVERFVSEDGIDNVRSRILGGTTIINAGVYARANESFYNNSGVEWDLDLVNEAYEWVEDAIVYKPSNQSWQSITGTAFLEAGVHPDNGFGLVHEEGTRLTGSTFDNSGTRHASDELLNKGDPDNLKVAVEAAVQKIIFSTESSGLTAVGVVYTDSNGTSHRALVSGKGEVILSAGTLGTPQLLLLSGVGPESYLTSLNISVVASHPYVGQYVNDNPRNFINILPPNPIEPSTVTVLGITSDFYQCSLSSLPFDTPPFSLFPTTSYPLPNQTFAHIVSKVPGPLSAGSLTLQSSSNVSVAPNVKFNYCSDPVDLTHCVSGMKKIGVFLSTDALKPYKVDDLPGIDGFNILGTPLPENQTDDAAFEKFCRDTVASYWHYHGGAIVGKVIDGNFRVTGINALRVVDGSTFPATPASHPQGFYLMLGRYVGTKIVQERSASGEAIHTSTFKPKLMDSLKSALSFAF | Involved in cyanogenesis, the release of HCN from injured tissues. Catalyzes the stereospecific addition of HCN to a variety of aldehydes in vitro. It is a major seed constituent, and could have the additional role of a storage form for reduced nitrogen (By similarity).
Subcellular locations: Vacuole, Aleurone grain
Primarily found within protein bodies of the cotyledonary parenchyma cells, with lesser amounts within the procambium. |
NDHJ_MANES | Manihot esculenta | MQGRLSAWLVKHGLVHRFLGFDYQGIETLQIKPEDWHSIAVILYVYGYNYLRSQCAYDVAPGGLLASVYHLTRIEYGIDQPEEVCIKVFAPRKNPRIPSVFWVWKSADFQERESYDMLGIFYDNHPRLKRILMPESWIGWPLRKDYIAPNFYEIQDAH | 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 |
NLTP1_PRUAR | Prunus armeniaca | ITCGQVSSSLAPCIGYVRGGGAVPPACCNGIRNVNNLARTTPDRRTACNCLKQLSGSISGVNPNNAAALPGKCGVNIPYKISASTNCATVK | Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. |
NLTP1_PRUDO | Prunus domestica | ITCGQVSSNLAPCINYVKGGGAVPPACCNGIRNVNNLARTTADRRAACNCLKQLSGSIPGVNPNNAAALPGKCGVNVPYKISASTNCATVK | Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. |
NLTP1_PRUDU | Prunus dulcis | MAYSAMTKLALVVALCMVVSVPIAQAITCGQVSSNLAPCIPYVRGGGAVPPACCNGIRNVNNLARTTPDRQAACNCLKQLSASVPGVNPNNAAALPGKCGVNIPYQISPSTNCANVK | Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues (By similarity). |
NLTP1_PRUPE | Prunus persica | ITCGQVSSALAPCIPYVRGGGAVPPACCNGIRNVNNLARTTPDRQAACNCLKQLSASVPGVNPNNAAALPGKCGVHIPYKISASTNCATVK | Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. |
NMCP1_DAUCS | Daucus carota subsp. sativus | MGRVEDMGLNAKLMKLETELFDYQYNMGLLLIEKKEWTSKFEELQQVYTETKDALKQEQEAHLIAISDAEKREENLTKALGVEKQCVLDLEKALRDMRSDYAEIKFTSDSKLAEASALITKVEEKSLEVESKLHSADAKLAELSRKGSDIERKSHELEARESALRRERLALNAEREALTDNISRQREDLREWERKLQEDEERLAEVRRLLNQREERANENDRLYQQKQSELDGEQKKIEIIMVSLKNKEDDISSRIAKLNIKEKEADAVKHSLEVKEKDLTEFEQKLNAREQSEIQKLLDEHKAILEVKKQSFEMEMDKRKNDFENDLQNRAVEVEKKEVEVKHLEAKLAKREHALDQKHEKLKEKEQYLASKLQDLNEREKSMKLEENKIEDERNQLLSDKQEMLCLKAEIEKDRASTEEQRLKLSEEIERLKITEEERLELARLQSELKQEIENCRHQRELLLKEEDELKQEKMRFEKEWEDLDERRTALMKDLKDITVQKENFEKLKHSEEDRLNNKKLDTESYVQKELDALRLTKDSFAATMEHEKAVLAERTSSEKKQMLNDFELWKRELETKLFNEREDMENALRLREKQFDEEREKELNNINYIKEVISKEREDIKLERSRIAKEKQEILMHQKHLDEQHVVMQKDIGQLVSLSEKLKDQREQFFKERECFIRFVESQKSCKNCGEMTSEFVVSDLQSLAELENLKALSVPQLAENYLRQDLQGTPDKNLSTVTPGAVGLGSPASGGTKSWLQKCTSKIFIFSASKKNNSPDQNTSRRLHVEASPNKLLNTEVIPELPSGVAGETLEMQNMQVSNSNREMESNLNLSGTEQSNIDSKALDVEDSQQSDVRAGNRKPGKRAKGRVRRKRSAKEVAEEAKTVLADPIELNENEHSNGLASAYTNESRGDSSLVGKRTRNSRKRNPSQPSQSAAGDVGADSEGHSDSVTAGGRQKRRRKVVPAVQAPTGRYNLRRHKTAAPLVANGALSDPNKGKEKEIDDGGGIGEEIPDEVDGNTHLVQVTTLKKRINVVNEFSSAGFHGINATSESQDRDAANQLVSDTMLSEEVNGTPEQSRGYQNQGDTSGAEGEDEDGDEVEHPGEVSMRKKVWKFLTT | Architectural component of nuclear structure that plays different roles in controlling nuclear size and morphology.
Subcellular locations: Nucleus matrix, Nucleus lamina
Localizes at the nuclear periphery. |
NU2C2_DAUCA | Daucus carota | MIWHVQNENFILDSTRIFMKAFHLLLFDGSLIVPECILIFGLILLLMIDSTSDQKDIPWLYFISSTSLVMSITALLFRWREEPVISFSGNFQTNNFNEIFQFLILLCSTLCIPLSVEYIECTEMAITEFLLFVLTATLGGMFLCGANDLITIFVAPECFSLCSYLLSGYTKKDVRSNEATMKYLLMGGASSSILVHGFSWLYGSSGGEIELQEIVNGLINTQMYNSPGISIALIFITVGIGFKLSPAPSHQWTPDVYEGSPTPVVAFLSVTSKVAASASATRIFDIPFYFSSNEWHLLLETLAILSMILGNLIAITQTSMKRMLAYSSIGQIGYVIIGIIVGDSNDGYASMITYMLFYISMNLGTFACIVLFGLRTGTDNIRDYAGLYTKDPFLALSLALCLLSLGGLPPLAGFFGKLYLFWCGWQAGLYFLVLIGLLTSVVSIYYYLKIIKLLMTGRTQEITPHVRNYRRSPFRSNNSIELSMIVCVIASTIPGISMNPIIAIAQDTLF | 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 |
NU3C_DAUCA | Daucus carota | MFLLYEYDIFWAFLIISSLIPILAFFVSGVLAPINKGPEKLSSYESGIEPMGNAWLQFRIRYYMFALVFVVFDVETVFLYPWAMSFDVLGISVFVEALIFVLILIVGLVYAWRKGALEWS | 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 |
NU4LC_DAUCA | Daucus carota | MMLEHVLVLSAYLFSVGLYGLITSRNMVRALMCLELILNAVNINFVTFSDFFDSRQLKGSIFSIFVIAIAAAEAAIGLAIVSSIYRNRKSTRINQSNLLNK | 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 |
PAL1_DAUCA | Daucus carota | MDCENKNVVLGNGLCMQKDPLNWGMAAEALTGSHLDEVKRMVAEFRKPMVQLGGETLTVSQVAAIAAGSVKVELAESARAGVKASSDWVMESMNKGTDSYGVTTGFGATSHRRTKQGGALQKELIRFLNAGIFGSGNDSSNILPHSATRAAMLVRINTLLQGYSGIRFEILEAITKFLNQNITPCLPLRGTITASGDLVPLSYIAGLLTGRPNSKAVGPTGENLTAAEAFKLAGVDGGFFELQPKEGLALVNGTAVGSGMASMVLFETNILAVLAEVMSAIFAEVMQGKPEFTDHLTHKLKHHPGQIEAAAIMEHILDGSSYVKAAEKQHEMDPLQKPKQDRYALRTSPQWLGPQIEVIRSSTKMIEREINSVNDNPLIDVSRNKAIHGGNFQGTPIGVSMDNTRLAIAAIGKLMFAQFSELVNDFYNNGLPSNLSGGRNPSLDYGFKGAEIAMASYCSELQFLGNPVTNHVQSAEQHNQDVNSLGLISSRKTAEAVEILKLMSTTFLVGLCQAVDLRHLEENLKSTVKNTVSQVAKKVLTMGVNGELHPSRFCELDLLRVVDREYIFAYIDDPCSATYPLMQKLRQVLVEHALKNGETEKNLSTSIFQKIAAFEDELKALLPKEVESARAVVESGNPAIPNRIKECRSYPLYKFIREELGTVYLTGEKVTSPGEEFDKVFTAMSKGEIIDPLLACLESWNGAPLPIA | 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 |
PER6_DAUCA | Daucus carota | LVSGCADLTALAAR | 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. |
PETL_DAUCA | Daucus carota | MPTITSYFGFLLAALTVTSALFIGLSKIRLI | 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. PetL is important for photoautotrophic growth as well as for electron transfer efficiency and stability of the cytochrome b6-f complex.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
PMLN_PRUPE | Prunus persica | GSSFCDSKCGVRCSKAGYQERCLKYCGICCEKCHCVPSGTYGNKDECPCYRDLKNSKGNPKCP | Expressed in peel and pulp of fruit (at protein level). |
PROF_LITCN | Litchi chinensis | MSWQTYVDDHLMCETDGQHLTAAAIIGHDGSVWAQSANFPQFKPAEIAAIMKDFDEPGSLAPTGLHLGGTKYMVIQGEPGAVIRGKKGPGGITVKKTTQALIIGIYDEPMTPGQCNMVVERLGDYLVDQGL | Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG (By similarity).
Subcellular locations: Cytoplasm, Cytoskeleton |
PROF_PRUAV | Prunus avium | MSWQAYVDDHLMCDIDGNRLTAAAILGQDGSVWSQSATFPAFKPEEIAAILKDLDQPGTLAPTGLFLGGTKYMVIQGEAGAVIRGKKGSGGITVKKTNQALIIGIYDEPLTPGQCNMIVERLGDYLIEQGL | Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG (By similarity).
Subcellular locations: Cytoplasm, Cytoskeleton |
PROF_PRUDU | Prunus dulcis | MSWQQYVDDHLMCDIDGNRLTAAAILGQDGSVWSQSATFPAFKPEEIAAILKDFDQPGTLAPTGLFLGGTKYMVIQGEAGAVIRGKKGSGGITVKKTNQALIIGIYDEPLTPGQCNMIVERLGDYLIEQGL | Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG (By similarity).
Subcellular locations: Cytoplasm, Cytoskeleton |
PROF_PRUPE | Prunus persica | MSWQAYVDDHLMCEIEGNHLSAAAIIGHDGSVWAQSATFPQLKPEEVTGILNDFNEPGSLAPTGLYLGGTKYMVIQGEPGAVIRGKKGPGGVTVKKSTLALLIGIYDEPMTPGQCNMIVERLGDYLVEQGL | Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG (By similarity).
Subcellular locations: Cytoplasm, Cytoskeleton |
PRS7_PRUPE | Prunus persica | MAPEPEDIKDEKNPRPLDEDDIALLKTYGLGPYSTHIKKAEKEVKDLAKKVNDLCGIKESDTGLAAPSQWDLVSDKQMMQEEQPLQVARCTKIINPNSEDAKYVINVKQIAKFVVGLGDKVSPTDIEEGMRVGVDRNKYQIQIPLPPKIDPSVTMMTVEEKPDVTYNDVGGCKEQIEKMREVVELPMLHPEKFVKLGIDPPKGVLCYGPPGTGKTLLARAVANRTDACFIRVIGSELVQKYVGEGARMVRELFQMARSKKACIVFFDEVDAIGGARFDDGVGGDNEVQRTMLEIVNQLDGFDARGNIKVLMATNRPDTLDPALLRPGRLDRKVEFGLPDLESRTQIFKIHTRTMNCERDIRFELLARLCPNSTGADIRSVCTEAGMYAIRARRKTVTEKDFLDAVNKVIKGYQKFSATPKYMVYN | The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity).
Subcellular locations: Cytoplasm, Nucleus |
PSBA_MANES | Manihot esculenta | MTAILERRESESLWGRFCNWITSTENRLYIGWFGVLMIPTLLTATSVFIIAFIAAPPVDIDGIREPVSGSLLYGNNIISGAIIPTSAAIGLHFYPIWEAASVDEWLYNGGPYELIVLHFLLGVACYMGREWELSFRLGMRPWIAVAYSAPVAAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLIRETTENESANEGYRFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVVGIWFTALGISTMAFNLNGFNFNQSVVDSQGRVINTWADIINRANLGMEVMHERNAHNFPLDLAAVEAPSTNG | 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.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
PSBD_DAUCA | Daucus carota | MTIALGKFTKDEKDLFDIMDDWLRRDRFVFVGWSGLLLFPCAYFAVGGWFTGTTFVTSWYTHGLASSYLEGCNFLTAAVSTPANSLAHSLLLLWGPEAQGDFTRWCQLGGLWTFVALHGAFGLIGFMLRQFELARSVQLRPYNAIAFSGPIAVFVSVFLIYPLGQSGWFFAPSFGVAAIFRFILFFQGFHNWTLNPFHMMGVAGVLGAALLCAIHGATVENTLFEDGDGANTFRAFNPTQAEETYSMVTANRFWSQIFGVAFSNKRWLHFFMLFVPVTGLWMSALGVVGLALNLRAYDFVSQEIRAAEDPEFETFYTKNILLNEGIRAWMAAQDQPHENLIFPEEVLPRGNAL | 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 |
PSBI_DAUCA | Daucus carota | MLTLKLFVYTVVIFFVSLFIFGFLSNDPGRNPGREE | One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. 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 |
PSBJ_DAUCA | Daucus carota | MADTTGRIPLWIIGTVAGILVIGLIGIFFYGSYSGLGSSL | 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 |