lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Adapter protein that provides a link between the endocytic membrane traffic and the actin assembly machinery. Acts as a guanine nucleotide exchange factor (GEF) for CDC42, and thereby stimulates actin nucleation mediated by WASL and the ARP2/3 complex. Plays a role in the assembly and maturation of clathrin-coated vesicles. Recruits FCHSD2 to clathrin-coated pits. Involved in endocytosis of activated EGFR, and probably also other growth factor receptors. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR may involve association with DAB2. Promotes ubiquitination and subsequent degradation of EGFR, and thereby contributes to the down-regulation of EGFR-dependent signaling pathways. In chromaffin cells, required for normal exocytosis of catecholamines. Required for rapid replenishment of release-ready synaptic vesicles at presynaptic active zones. Inhibits ARHGAP31 activity toward RAC1; Plays a role in synaptic vesicle endocytosis in brain neurons.
Subcellular Localization:
Cell membrane. Cell projection, lamellipodium. Membrane, clathrin-coated pit. Nucleus envelope. Recycling endosome. Synapse, synaptosome.
Sequence:
MAQFPTSFGGSLDIWAITVEERAKHDQQFHSLKPTSGFITGDQARNFFFQSGLPQPVLAQIWALADMNNDGRMDQIEFSIAMKLIKLKLQGYQLPAALPPVMKQQPVAISGAPTFGIGGIASMPPLTAVAPVPMASIPVVGMSPPLVSSVSTAAVPPLANGTPSVIQPLPAFAHPAATLPKSSSFSRSGPGSQLNTKLQKAQSFDVASASPVAEWAVPQSSRLKYRQLFNSHDKTMSGHLTGPQARTILMQSSLPQTQLATIWNLSDIDQDGKLTAEEFILAMHLIDVAMSGQPLPPALPPEYIPPSFRRVRSGSGISVISSVSVDQRLPEEPVLEEEQQQLEKKLPVTFEDKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQVELEKQLEKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQDIRCRLAMQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQLLNDQLKQVQQNSLHRDSLLTLKRALEAKELARQQLRDQLDEVEKETRSKLQEIDIFNNQLKELREIHNKQQLQKQKNLEAERLKQKEKERKTVELEKQKEESQRRSQDKQWLDRVQQDEEYQRPKKLHDEEKLKEETVKKKDGEEKGKQDMKEKLTKLFQQHQEPARPALLAPSSSTEKGPFAISTQEDVKVVYYRALYPFESRSHDEITIQPGDIVMVKGEWVDESQTGEPGWLGGELKGKTGWFPANYAEKIPENEIPTPLKPAADSAPLPAPKLALHETPTPVTATSSESSTTSNNWADFSSTWPTNTNEKPETDNWDAWATQPSLTVPSAGQLRQRSAFTPATVTGSSPSPVLGQGEKVEGLQAQALYPWRAKKDNHLNFNKNDVITVLEQQDMWWFGEVQGQKGWFPKSYVKLISGPIRKSSSMDSGSSESPAVLKRVASPAAKLSIPGEEYIAMYTYESSEQGDLTFQQGDVILVTKKDGDWWTGTVADKSGVFPSNYVRLKDSAEVPGASGKAGSLGKKPEIAQVIASYTATGPEQLTLAPGQLILIRKKNPGGWWEGELQARGKKRQIGWFPANYVKLLSPGTSKVTPTEPPKSIALPAVCQVIGMYDYTAQNDDELAFNKGQIINVLNKEDPDWWKGEVNGQVGLFPSNYVKMTTDMDPSQQ
The following text describes a protein:
Function:
May act as a carbohydrate transporter.
Sequence:
MAATRLALALLLAAAVAASQLPAAAVAANYTVGDEKGWNPDVDYTAWVKKHKPFYKGDWLIFQYQNGRSDVVQVDEVGYDNCDKANALSSYSKGSTYAFQLKEAKDYYFICSYGYCYHGMKVHVTAKSSGSGSSSSGSGSGSGSSSGDDSSDSSDDDSSSDDSPSPPAKKSKAKSSSAAAPPPSLLAATPRAAAITAAVALLLNRML
The following text describes a protein:
Function:
Catalyzes the reversible hydration of CO(2) to H(2)CO(3). The main role may be to provide inorganic carbon for the bicarbonate-dependent carboxylation reactions catalyzed by pyruvate carboxylase, acetyl-CoA carboxylase and carbamoyl-phosphate synthetase (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MLPPFGALTTTKIPLPKTILQSTFNQIKSSSYSIIAAPRLTSRFIRFPCNYNSCLQSISFSSLGRKRLFFSSSQLLEKSDKKKKMPDRLKRRIEEIDHQDEIIDREASTASPVSGAGKIDQNGEIKDLLERNLTWSQQTSRKYPSFFTATKDIQTPQVLWIGCSDSRVPETTILNLLPGEVFVHRNIANVVPRSDINALAVMEYSVTVLKVKHIIVCGHYGCGGVAAALGPNLNNLLDHWLRHIRDVIEDNREELDAIEDPQLRRLKLAELNTRAQAISVTRVGFVREAMEKRGLQVHGWIYDLSNGQIKKLDITDAIKKAKYGTYDS
The following text describes a protein:
Function:
Binds bacterial lipopolysaccharide (LPS). Cooperates with TLR4 in the innate immune response to bacterial lipopolysaccharide (LPS), and with TLR2 in the response to cell wall components from Gram-positive and Gram-negative bacteria. Enhances TLR4-dependent activation of NF-kappa-B. Cells expressing both LY96 and TLR4, but not TLR4 alone, respond to LPS.
Subcellular Localization:
Secreted, extracellular space.
Sequence:
MLPFFLFSTLLSPIFTESERQQWICNSSDAIISYSYCDHMKIPISISSEPCIRLKGTNGFVHVEFIPRGNLKNLYFNLFININSIELPKRKEIVCHGYDDDYSFCRALKGEAVNTAIPFSFDGILFPKGHHRCVAEAIAGDTEEKLFCLNFTIIHHHNVN
The following text describes a protein:
Function:
Probable transcriptional regulator (By similarity). May regulates developmental traits such as flowering time.
Miscellaneous:
MISCELLANEOUS: In strain cv. 24, promotes the flowering time transition, probably via the transcription regulation of FT.
Subcellular Localization:
Nucleus.
Domain:
The methyl-CpG-binding domain (MBD) functions both in binding to methylated DNA and in protein interactions.
Sequence:
MDDGDLGNNHHNFLGGAGNRLSAESLPLIDTRLLSQSELRALSQCSSLSPSSSASLAASAGGDDDLTPKIDRSVFNESAGSRKQTFLRLRLARHPQPPEEPPSPQRQRDDSSREEQTQVASLLRSLFNVDSNQSKEEEDEGEEELEDNEGQIHYNSYVYQRPNLDSIQNVLIQGTSGNKIKRKRGRPRKIRNPSEENEVLDLTGEASTYVFVDKTSSNLGMVSRVGSSGISLDSNSVKRKRGRPPKNKEEIMNLEKRDSAIVNISAFDKEELVVNLENREGTIVDLSALASVSEDPYEEELRRITVGLKTKEEILGFLEQLNGEWVNIGKKKKVVNACDYGGYLPRGWRLMLYIKRKGSNLLLACRRYISPDGQQFETCKEVSTYLRSLLESPSKNQHYYLQSDNKTLGQQPVIANESLLGNSDSMDSETMQYLESGRTSSEVFEEAKAVENGNEADRVKTSLMQKDDNADFLNGVEDNDDDMKKRDGNMENLATLSNSEMTKSLPTTTNELQQYFSSQINRVQ
The following text describes a protein:
Function:
Component of the glutathione system which performs several activities such as glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage. GRX1 is less active as an oxidoreductase than GRX2.
Miscellaneous:
MISCELLANEOUS: Present with 3030 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MVSQETIKHVKDLIAENEIFVASKTYCPYCHAALNTLFEKLKVPRSKVLVLQLNDMKEGADIQAALYEINGQRTVPNIYINGKHIGGNDDLQELRETGELEELLEPILAN
The following text describes a protein:
Function:
Involved in the synthesis of glucuronoxylan hemicellulose in secondary cell walls.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MASPKHSHRHHRAAATKHRRPLALRRAMLHSCVCFLVGLVTGLAPSDWTDAASRAAVHANGAATAQVFRALHAMNQTAAAGALGQLLALQHYQQQPVVEKEKEKEKKPLDLVVVVTTTTTSTGLSERERRSAGLTRTAHALRLVSPPLVWLVVEAAREAGPTARLLRRTGVVYRHLTYAENFTSEAWEEERHHQRNQALAHIERHRLRGVVLFAGLADVYDGRLLEQLRRHIRTRSVGAWAVATVWEQEKRVAVEGPVVVCNTTTTTTSAASTACAWFSASDSTLLAAAAAAAPPVTADDSVHGFAFASDLLWDPSRWDRFPTSEPDQSQDSIKFVQRLVMAEYNKTRAIIPADDDYSSNRSQIMVWRVDTTLL
The following text describes a protein:
Function:
Receptor kinase that detects X.oryzae pv. oryzae protein Ax21 to promote innate immunity. Following X.oryzae pv. oryzae protein Ax21 detection, undergoes cleavage, releasing the processed protein kinase Xa21 chain; The processed protein kinase Xa21 chain released by protein cleavage after X.oryzae pv. oryzae protein Ax21 detection translocates into the nucleus where it can bind and regulate WRKY62, a transcription factor. Confers resistance to the bacterial pathogen X.oryzae pv. oryzae (Xoo).
Subcellular Localization:
Cell membrane; Single-pass membrane protein. Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MFPILLLLLLAYVPQMVPSASAIAVNKIPDEGILQEMKASLNQQQGVLAAWNATTKFCHWPGVSSSLKHKDRVTVLNLTSQGLSGTITPSIGNLTFLRILDLSSNKLQGEIPVSVGQLPRLQHLNLSNILLQGEITTQIELDSNFFMGEIPAWLGGLPLKAIHLRKNNFTGVIPESPCNLSSLQEINFARNKLEGTIPEGLGGLMLCLMFVDLGENHFSGIIPKTFFNISTLIHFRVTNNELHGMLPSDLGVHLPNLNVPPEIAKLCPDFLSFDTNQLTATTVQEWKFVTFLTNCTRLRIFDVQDNMLRAMLPSSVSNLSAQLQILYVGYNEISGKIKPSTIPSGISNLVGLTQLQLSNNRFTGLVPGSIGMLTSLQALGFQGNQLTGLLPSSLGNLTQLLKLYTENNLFEGHIPTSLGSLQDITMATFNNNKFTGPLPIHLFNLSSLSVLLNLAYNNFVGPLPPEVGSLTKLAYLYIAGNNLVGSLPDAISNCQSLIDLRLDTNSFNSSIPASISKMKGLAILTLDNNALSGVIPQELGLMDGLKEFYLSHNNLSGSITESFENMTLLDKLDLSFNHLDGKVPLHGVFSNVTRFLFDGNLALCGGIPELHLPPCLQNSMEHRKRKLVPILKVIVPIAGILFCFSLVLIFISLKKKQKAQSTSLAEFCMMDERYPRVSYDELLQGTNGFNPNNLIGKGRYGSVYKCSLPLKNMITTVAVKVFDLQQSGSSKSFISECEALNKIRHRNLISIITCCSSCDSTQNDFKALVFEFMPNGSLHRWLHLDEHTSQQWHGLTLTQRLNIAVDVADALEYLHNSCEPPIVHCDLKPSNILLDQDLVAHVGDFGLAKILPNPASEQQVDSNSTMGIRGTIGYVAPEYGEGGQISTCGDVYSFGIVLLELFTGLTPTEDMFRDGLTLQKHAENVFPGMLMNIIDPILVSDEEGHACTSQGVKNAMGDINKVMLSITKLALSCSKHAPTERINMRDAAAEMHRIRDTIVYDN
The following text describes a protein:
Function:
Required for the splicing of precursor tRNA molecules containing introns. The ligation activity requires three enzymatic activities: phosphorylation of the 5' terminus of the 3' half-tRNA in the presence of ATP, opening of the 2'3'-cyclic phosphodiester bond of the 5' half-tRNA leaving a 2'-phosphomonoester and ligation of the two tRNA halves in an ATP-dependent reaction.
Subcellular Localization:
Cytoplasm.
Domain:
Has three domain each corresponding to an enzymatic activity, namely in N- to C-terminal order: ligase, kinase and cyclic phosphodiesterase (CPDase).
Sequence:
MTRDQRVCIFGEKKSTVRSVTFKAPKSNYDLTSWRIWEQAFRLNVSNSKKCFDTISGHRITLPTNARGLFTGYDYESKRHRIVIRGYDKFFNIDEVPITTWDALSQHTKGPYELTVKENGCIIFIAALPDGQIIVSSKHSLGIVEGQSVSHANVGERWLEKHLQSVGRTKQELAHELLRRDMTAVAELCDDEFEEHILPYTGNSRGLYLHGLNRNCPQFITASSCEVAEFAEQWGFMKVSSFFMDSIHELKAFLENASKDGKWNNRAIEGFVIRCHSDHSSLEQQSSNDFFFKYKFPEPYGMFRQWREVTKMLISGKKPSYTKYKKVTAEYITFCDKKFKEDEDAKRLYMSNKGIISLRDEFLVLSKLDLMHLSVSNDNDCGKEFTLLVPIATIGCGKTTVAKILEKLFGWPVVQNDNLPSGKGGPKRFAKAIIEEFRNGHSVVFADRNNHISNMRSTLQTDILALIDGVRFVALPFKHTPEVPEFVQNRVLQRGDRHQSIKVSEGVDKVKAIMNTFYKQYKPFDPAGNKHDANYDDIIELDPLIGSLENARRIVNYFKKNIPELIPNDPSDDDYAAALNYAVNEYVPTYRKTFGNDSKKIKNKITAEGITGSSTCFKKAPRYFGVLLDRKTVESSLVQVLTIANLQWQEAFSRYTLQDSFHITMIHESQKPVNSRIWEQYLQHMHDKNTTKMGNISFRITHLVWDDRVICFRVTMNENSVWYGKTCNPQLHITLGTSSSDVKAFESNFLLKKLRWQGDEVDSTDGNVRYLTVLPKIIIEGMLEPVY
The following text describes a protein:
Function:
May be involved in regulating membrane traffic to and from trans-Golgi network.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein. Golgi apparatus, trans-Golgi network membrane; Single-pass type I membrane protein. Note=Primarily in trans-Golgi network. Cycles between the trans-Golgi network and the cell surface returning via endosomes.
Sequence:
MRFVVALVLLNVAAAGAVPLLATESVKQEEAGVRPSAGNVSTHPSLSQRPGGSTKSHPEPQTPKDSPSKSSAEAQTPEDTPNKSGAEAKTQKDSSNKSGAEAKTQKGSTSKSGSEAQTTKDSTSKSHPELQTPKDSTGKSGAEAQTPEDSPNRSGAEAKTQKDSPSKSGSEAQTTKDVPNKSGADGQTPKDGSSKSGAEDQTPKDVPNKSGAEKQTPKDGSNKSGAEEQGPIDGPSKSGAEEQTSKDSPNKVVPEQPSRKDHSKPISNPSDNKELPKADTNQLADKGKLSPHAFKTESGEETDLISPPQEEVKSSEPTEDVEPKEAEDDDTGPEEGSPPKEEKEKMSGSASSENREGTLSDSTGSEKDDLYPNGSGNGSAESSHFFAYLVTAAILVAVLYIAHHNKRKIIAFVLEGKRSKVTRRPKASDYQRLDQKS
The following text describes a protein:
Function:
Involved in the degradation of glucose via the Entner-Doudoroff pathway. Catalyzes the reversible, stereospecific retro-aldol cleavage of 2-keto-3-deoxy-6-phosphogluconate (KDPG) to pyruvate and D-glyceraldehyde-3-phosphate. In vitro, can also catalyze the cleavage of 2-keto-4-hydroxy-4-(2'-pyridyl)butyrate (KHPB), 2-keto-3-deoxy-6-phosphogalactonate (KDPGal), and of the substrate analogs 2-keto-3-deoxy-gluconate (KDG) and 2-keto-4-hydroxyoctonate (KHO). Can accept some nucleophiles other than pyruvate, including 2-oxobutanoate, phenylpyruvate and fluorobutanoate. In addition to its KDPG aldolase activity, catalyzes the reversible cleavage of 2-keto-4-hydroxyglutarate (KHG) to glyoxylate and pyruvate. The enzyme is stereoselective for the S-enantiomer of KHG. Cleavage of KHG could serve in tricarboxylic acid (TCA) cycle regulation or, when operating in the reverse direction, in the detoxification of glyoxylate (Probable). Finally, also shows a high level of oxaloacetate beta-decarboxylase activity. The enzyme could have several physiological roles and function as a stress response protein in addition to its role in the catabolism of sugar acids.
Subcellular Localization:
Cytoplasm.
Sequence:
MKNWKTSAESILTTGPVVPVIVVKKLEHAVPMAKALVAGGVRVLEVTLRTECAVDAIRAIAKEVPEAIVGAGTVLNPQQLAEVTEAGAQFAISPGLTEPLLKAATEGTIPLIPGISTVSELMLGMDYGLKEFKFFPAEANGGVKALQAIAGPFSQVRFCPTGGISPANYRDYLALKSVLCIGGSWLVPADALEAGDYDRITKLAREAVEGAKL
The following text describes a protein:
Function:
Highly selective inward-rectifying potassium channel that is specifically located in the tonoplast of large vacuoles. Functions independently of the voltage difference across the membrane.
Subcellular Localization:
Vacuole membrane; Multi-pass membrane protein. Note=Tonoplast of large vacuoles.
Domain:
Each of the two pore-forming region (also called P-domain or P-loop) is enclosed by two transmembrane segments (2P/4TM) and contains the GYGD signature motif which seems to be involved in potassium selectivity.
Sequence:
MDDNSIQQSLLADNPNVLQRKPSEGVNRFRRCRSTPSTDPLQGPPEKGSSVKAKELFKEMRPSFRLVGLLLFIYLLVGVLAFYAVMDEISGKRTNRVLDALYFCVVTMTTVGYGDLVPNNDTTKLLACAFVFMGMAVVALFVSKVADYLVEKQEVLFFKALHTNLKGGETKMLRAIETNRIKYKFYTNALLLVLSIISGTVFLWKVEKLSLVDSFYCVCATITTLGYGDKSFSSKLGRVFAVFWIITSTIIMAQFFMYLAEIYTERRQKMLANWVLTRKMTKMDLEAADLDDDRQVGAAEFVVYKLKELGKINQEEISSFLEEFEKLDVDHSGTLSPYDLTLAQSAQ
The following text describes a protein:
Function:
Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine). The elongator complex catalyzes the formation of carboxymethyluridine in the wobble base at position 34 in tRNAs.
Subcellular Localization:
Cytoplasm. Nucleus.
Domain:
Folds into a two seven-bladed beta-propeller structure which is required for elongator complex assembly.
Sequence:
MSAPIVQLAHAAFSVNRCPSCVSWSRTGILACATCHSIALYDPQKNVVISTLNGHTGRVNCVHWVQKNDCSAETELVSGGSDKKVIIWAIEKNKCEQPVAAEGHTEVVNAVHAVYTQRSENELLIVSAASDCTVRLWLRRNVKTECLQTLSFGKGFVLDVCISFLPGSLVPVLACGADDSRIHLYVLQNEQFEKTQVLHGHEDWIRGVEWAVTGQNLFLASCAQDCLIRIWKIFRKTAKENSKTEDENSIKLKENIFKVKEKDTETSYAVTLETVLTGHENSIYAVHWQPSFSRDGSIVQPMSLLSASMDKTMILWEPDEESGVWLEQVRVGEVGGNTLGFLGCQFSPDKSMILAHAFHGALHLWSRAPNKQNEWIPMVIISGHFDSVQDMRWDPDGQFVITVSADQTTRLFGPWKKKGQSHVTWHEIARPQIHGYDMQCLAMIGRFQFVSGADEKVLRVFAAPRNFIENFSNISCISVEKLLLNEDTNLPEGATVPALGLSNKAVFHGEILIQSTQEEGKYNSVSEQYSQPNFQPLNLTEPPTEDHLLQNTLWPEVQKLYGHGYEIFAVACNSAKTVIASACKASKREHAAIILWSTTSWKQLQSLSYHNLTVTQMAFSPDDEFLLVVSRDRNWSLWKKQEGIPEQTEPTFTLYASTDKNSCVHSRIIWACDWTPDSKYFVTGSRDKKVIVWGDCSLPSMNEEKSSALIRPCSSLLDTGDSITAVSVSQVLALDGSYIIAVGLDCGIIQLYKWKHSGTVNDWLKCLAMDQSLLSHTLTVKQLCWRSCLGRAGHDDRDNGDWIQLASCGADHCVKIFDVYRKAL
The following text describes a protein:
Function:
Transcription factor that plays a crucial role in tapetum development. Required for male fertility and pollen differentiation within the developing anther. Plays a major role in maintaining tapetum development, starting in early meiosis. Required for pollen mother cell meiosis. May regulate the anther-specific cysteine protease CP1 and lipid-transfer proteins C4 and C6. Required for anther development. Functions in parallel with GAMYB to regulate early anther development. Functions upstream of the transcription factor TDR and may positively regulate its transcription.
Subcellular Localization:
Nucleus.
Sequence:
MPRRARARGGGGGGGEEVKVEDDFIDSVLNFGGGGGGEEDGDDGEEEQQQQQAAAAAMGKEFKSKNLEAERRRRGRLNGNIFALRAVVPKITKMSKEATLSDAIEHIKNLQNEVLELQRQLGDSPGEAWEKQCSASCSESFVPTENAHYQGQVELISLGSCKYNLKIFWTKRAGLFTKVLEALCSYKVQVLSLNTISFYGYAESFFTIEVKGEQDVVMVELRSLLSSIVEVPSI
The following text describes a protein:
Function:
Self-assembles to form a helical, filamentous nucleocapsid mesuring 900 nm in length and 24 nm in width (Probable). Together with capsid protein 2, wraps arounds the DNA and maintains it in an A-form (Probable). Capsid proteins probably maintain the DNA in A-form by non-specific desolvation and specific coordination of the DNA phosphate groups by positively charged residues (Probable). This certainly protects the viral DNA under conditions such as the extreme desiccation of its host (Probable).
Subcellular Localization:
Virion.
Domain:
The N-terminus projects into a DNA groove.
Sequence:
MAKLNRKLRQDSTDRYKTKLYLWRNLGGLIPEDMAISVTESITADWKQYNDMMSKVRNETLDILKTNKVATEDYIGYIAFAEELAHQVWKNKNSSPDPNTANEASKTDLESKYSDVYGLDVTVLDAIYNAVIPIIMGGGS
The following text describes a protein:
Function:
Probable transcriptional repressor of multidrug resistance genes.
Subcellular Localization:
Nucleus.
Sequence:
MHLSKASFLFDCSRFILNFHERCLKNGVRTKKACVICRSKKQKCDGQLPCLYCKKYEYQCAYEGQATSTCNSEASLFNDANFKIGSDYRSKRIKVVSDTNNNKEDGDGKLSFTQCNPRMDIHHEAENFTAMVPYYEPKKFRFFYENSAIVFPRIYVFIYFEEVHPIFSMFDQKAMEKKIQFLWDNKSTDSCSEYVVISVKGKLVEHITQVLESSLSTTILSSIQLTVCWVLRTIYLHATTRPHLSWIASSVSMHYAEIVGLHQEITAEYGTRGIELTNITTQMVEEDGPAYQLVLLFKIIMEYQIISEDSRFVYLQAFQRLDQLCDIHSPALVLLKATVCFHLYRNLFLARIKPFCVIVSILFSVIDRALESCKQLVSQRKAW
The following text describes a protein:
Function:
Calcium-binding peroxygenase involved in the degradation of storage lipid in oil bodies. May be involved in the interaction between oil bodies and vacuoles during seed germination (By similarity).
Subcellular Localization:
Lipid droplet. Microsome membrane.
Domain:
Transmembrane regions are predicted by sequence analysis tools, but these regions probably constitute hydrophobic domains associated to phospholipids; The proline-knot motif may be involved in targeting to lipid bodies.
Sequence:
MATHVLAAAAERNAALAPDAPLAPVTMERPVRTDLETSIPKPYMARGLVAPDMDHPNGTPGHVHDNLSVLQQHCAFFDQDDNGIIYPWETYSGLRQIGFNVIASLIMAIVINVALSYPTLPGWIPSPFFPIYLYNIHKAKHGSDSGTYDTEGRYLPMNFENLFSKHARTMPDRLTLGELWSMTEANREAFDIFGWIASKMEWTLLYILARDQDGFLSKEAIRRCYDGSLFEYCAKMQRGAEDKMK
The following text describes a protein:
Function:
Catalyzes the dehydrogenation of both 9-fluorenol and 1,1a-dihydroxy-1-hydro-9-fluorenone to produce 9-fluorenone and 2'-carboxy-2,3- dihydroxybiphenyl, respectively.
Sequence:
MSESGGGTVATARQRQLVERALGEWQGEVAGRVIVVTGGARGIGRSLCEGLLRAGAKVVAADLTWDDADDFRKQLESDGSGMAVDMDITDDDALDAARDAVIDRFGTVDVLVNNASLVSETLFPPTGHRNTLDTTDRDWEVMFGVNVFGTLKAIRRFIEPMRAQQRGSIVNVVSSGVLAVAAGGGYHGLRPWTVEMPYQATKAAVMALTFYLAEEVRGDGVAVNAIMPGHTRASWFDATARAFNEQGIAYFMRPAIPEHLLPISLFLAAQDSAGASGRLYYVPEWNYDHGYGDYAAWQDHELPPDMEEIYSRLEAATPSYERAGVAHLPFDAQGALYAAGMANLGAQNSWTSNDSAQ
The following text describes a protein:
Function:
Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
Sequence:
MRIKFLGTSSAVPTKDRGLPAILVKTMGDSILLDCGEGTQRQMIMAKESIMDIDKVVITHLHGDHFFGLFPMIQTLSILRKGSELTILGPRSLEPLLTSIMEGTGSKPGFKVNFIGIERSEMRLGNFTLEFFEVNHNGFETYGVKVKERDRPGEFDPRKADELGVPVFMRGFLQKGYSVKLPDGRIVNPGDVMGPPRRGSVLVYSSDTRPTESVIRASRDADLLIHEATYLDELKDRAESTGHSTALEAGEVASASGVKRLILTHFSARYSDEDLLKFREEASKAYNGEVLVAKDFLTVEI
The following text describes a protein:
Function:
Involved in the regulation of abiotic stress responses. Acts as a negative regulator of abscisic acid (ABA) signaling and positive regulator of abiotic stress signaling. May be involved in panicle development (Probable).
Miscellaneous:
MISCELLANEOUS: Plants overexpressing P2C68 exhibit insensitivity to abscisic acid (ABA), and tolerance to high salt and mannitol stresses during seed germination, root growth and overall seedling growth. At adult stage, P2C68 overexpression leads to high tolerance to salt, mannitol and drought stresses with far better physiological parameters such as water loss, fresh weight, chlorophyll content and photosynthetic potential.
Subcellular Localization:
Nucleus. Cytoplasm, cytosol. Note=Localizes predominantly in the nucleus and partially in the cytosol.
Sequence:
MSMAEVCCDSAVVVGAEAEARARARAGRRRRAGVEGAGRWNATATAAGVAAEEAATRKRRASGGEAGLVVVAKRHGAASVAGRRREMEDAVSLREAFAAPANGEVAAARCDFYGVFDGHGCSHVADACRERMHELVAEEMGAGSPAAAAREPASWTETMERSFARMDAEVIAGCRAESGSCRCEGQKCDHVGSTAVVAVVEESRVVVANCGDSRAVLCRGGAPVQLSSDHKPDRPDELERIEAAGGRVIFWEGARVLGVLAMSRSIGDAYLKPYVTAVPEVTVTGRSDFDECLILASDGLWDVVSNEAACEVAQSCLRRGRQRWCAEAAAVLTKLALARRSSDNISVVVVDLRRGNAL
The following text describes a protein:
Function:
Regulates mitochondrial small subunit maturation by controlling 15S rRNA 5'-end processing. Localizes to the 5' precursor of the 15S rRNA in a position that is subsequently occupied by mS47 in the mature yeast mtSSU. Uses structure and sequence-specific RNA recognition, binding to a single-stranded region of the precursor and specifically recognizing bases -6 to -1. The exchange of Ccm1 for mS47 is coupled to the irreversible removal of precursor rRNA that is accompanied by conformational changes of the mitoribosomal proteins uS5m and mS26. These conformational changes signal completion of 5'-end rRNA processing through protection of the mature 5'-end of the 15S rRNA and stabilization of mS47. The removal of the 5' precursor together with the dissociation of Ccm1 may be catalyzed by the 5'-3' exoribonuclease Pet127. Involved in the specific removal of group I introns in mitochondrial encoded transcripts.
Sequence:
MQAILERADADVVRYGGISVLPPAIFFSLLNCHVKLQQTDSAELIWEYMLSQGIGISIASVNLMLQCYASLGRVDMVQALMKKCAEEGIAKLDIQSFVTLIDAYSKSGQTVSSLEVLDRALQSDIPLNIRIFNHIISGLAKNGKFAEMIKVLVFMQEKEFLPNTATFNIIIDLFAKQGDHENAFAMLDEMIKRGVQPNVVSYNTVLGAYGRAGMLSQAQDIFDTIDKMGISRTVTTYNLLISAYGFQGHMQTVLNLFEQIQDTNLSPDRNTFAVMISLHGMHDCYD
The following text describes a protein:
Function:
The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription. TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13. TAF2 forms a promoter DNA binding subcomplex of TFIID, together with TAF7 and TAF1.
Subcellular Localization:
Nucleus.
Sequence:
MPPTGLEPARMNRKKGDKGFESPRPYKLTHQVVCINNINFQRKSVVGFVELTIFPTVANLNRIKLNSKQCRIYRVRINDLEAAFIYNDPTLEVCHNESKQRNLNYFSNAYAAAVSAVDPDAGNGELCIKVPSELWKHVDELKVLKIHINFSLDQPKGGLHFVVPSVEGSMAERGAHVFSCGYQNSTRFWFPCVDSYSELCTWKLEFTVDAAMVAVSNGDLVETVYTHDMRKKTFHYMLTIPTAASNISLAIGPFEILVDPYMHEVTHFCLPQLLPLLKHTTSYLHEVFEFYEEILTCRYPYSCFKTVFIDEAYVEVAAYASMSIFSTNLLHSAMIIDETPLTRRCLAQSLAQQFFGCFISRMSWSDEWVLKGISGYIYGLWMKKTFGVNEYRHWIKEELDKIVAYELKTGGVLLHPIFGGGKEKDNPASHLHFSIKHPHTLSWEYYTMFQCKAHLVMRLIENRISMEFMLQVFNKLLSLASTASSQKFQSHMWSQMLVSTSGFLKSISNVSGKDIQPLIKQWVDQSGVVKFYGSFAFNRKRNVLELEIKQDYTSPGTQKYVGPLKVTVQELDGSFNHTLQIEENSLKHDIPCHSKSRRNKKKKIPLMNGEEVDMDLSAMDADSPLLWIRIDPDMSVLRKVEFEQADFMWQYQLRYERDVVAQQESILALEKFPTPASRLALTDILEQEQCFYRVRMSACFCLAKIANSMVSTWTGPPAMKSLFTRMFCCKTCPNIVKTNNFMSFQSYFLQKTMPVAMALLRDVHNLCPKEVLTFILDLIKYNDNRKNKFSDNYYRAEMIDALANSVTPAVSVNNEVRTLDNLNPDVRLILEEITRFLNMEKLLPSYRHTITVSCLRAIRVLQKNGHVPSDPALFKSYAEYGHFVDIRIAALEAVVDYTKVDRSYEELQWLLNMIQNDPVPYVRHKILNMLTKNPPFTKNMESPLCNEALVDQLWKLMNSGTSHDWRLRCGAVDLYFTLFGLSRPSCLPLPELGLVLNLKEKKAVLNPTIIPEAIAGNQEAAINPSSHAQLVGFQNPEDDHLAKEASCNMSAHQQGVKRKADTPLGSPLEPGQILEKNEDSSKVKLKIRFSNSQDEEEIDMDTVHDSQAFISHHLNMLERPSTPGLSKYRPTSSRSALIPQHSTGCDGTPTTKPQWSMELARKGTGKEQSPLEMSMHPVAAAPLSVFTKEPVSSKHSDHHHHHHHEHKKKKKKHKHKHKHKHKHDGKEKDKEPFSFSSPASGRSVHSPSLSD
The following text describes a protein:
Function:
Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MSLKKPPKGTSFWHGCRNDVRKRAPVVHFIVEMCLDKSMIRRLITLLVLFFLPIYALSEQPVPVDQAFQFSAMAKDYQTVIGLWNIKPGFYLYRNRIHFSSLKSADYLGEPLWPRVDTVKDYPGIGKLPVYQGQLRISVPVIKAMNQTLYLKVDYQGCSEKGFCYPPTTKTVAIDLAGNYMQPVAPLAIDIAPGKTAGPKAAPPITQQDRVTQLLTHKNLFFVLLSFFGFGLLLSFTPCVLPMIPVLSGIIVGQQKYPKRAFGLSLMYVLGMAITYAIAGVIFGFIGSTVQAAFQNPWLIGLFSLLFIAMALSLFGLYDLQLPQRWQTRLAQASDRQKHGTYLGTALMGALSTLILSPCVTPALVGVLGYISHTGNASLGGVALFTMGLGMGAPLLLLGAFSRKWLPKAGPWMTVIKHILGVLMLAVAVWLLARILPGTVTMFLWAALAVGSAIALGALSTTQTKMQKIGKTLGLFLLVYGIVLATGGLSGNTNPLRPISLASLPEKGEGPSFTAVYTLPDVEHQLKMATTKGQPTMIDFYADWCISCKQMEQFTFANQNVQKALAGFRLLRADVTRNDQGSTVLEKHFGVVAPPTVLFLDPQGKEIPNSRIVGEMSAFRFLKHLENLRS